protein_name
stringlengths 8
11
| species
stringclasses 13
values | sequence
stringlengths 5
2.31k
| annotation
stringlengths 19
1.16k
⌀ |
|---|---|---|---|
PSAJ_MANES | Manihot esculenta | MRDLKTYLSVAPVISTLWFGSLAGLLIEINRFFPDALTFPFFSF | May help in the organization of the PsaE and PsaF subunits.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBA_DAUCA | Daucus carota | MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSTNG | Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBB_DAUCA | Daucus carota | MGLPWYRVHTVVLNDPGRLLAVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITSSWGGWSITGGATPNPGIWSYEGVAGAHIVFSGLCFLAAIWHWTYWDLAIFCDERTGKPSLDLPKIFGIHLFLAGLACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQSVNPAWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLVDGDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGAFQKLGDPTTRRQTV | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
RK23_DAUCA | Daucus carota | MDGIKYAVFTDKSIRLLGKNQYTSNVESGSTRTEIKHWVELFFGVKVIAMNSHRLPGKGRRMGPIMGQTMHYRRMIITLQPGYSIPPLRKKRT | Binds to 23S rRNA.
Subcellular locations: Plastid, Chloroplast |
RPOA_DAUCA | Daucus carota | MVREKVTVSTRTLQWKCVESKADNKRLYYGRFILSPLMKGQADTIGISMRRALLGEIEGTCITRAKSEKIPHEYSTLVGIQESVHDILMNLKEIVLRSNLYGTCDASICVRGPGYVTAQDIILPPYVEVVDNTQHIASLTEPIELCIGLQIERNRGYLIKTPNNNSKDGSYPIDAVFMPVRNANHSIHSYGNGNDKQEILFLEIWTNGSLTPKEALHEASRNLIDLFIPFLHTEEENLHLANNQHMVPLPPFTFHDKLDKLRKNKKKRALKSIFIDQSELPPRIYNCLKRSNIYTLLDLLNNSQEDLMKIEHFRIKDVKQILGILEKNFSINLGKKPKMGFESLAQLIDSKSG | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular locations: Plastid, Chloroplast |
RPOC1_MANES | Manihot esculenta | MIDRYKHQQLRIGSVSPQQISAWANKILPNGEIVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNYRVIRNEKEDQKFCEQCGVEFVDSRIRRYQMGYIKLACPVTHVWYLKRLPSYIANLLDKPLKELEGLVYCDFSFARPIAKKPTFLRLRGSFEYEIQSWKYSIPLFFTTQCFDTFRNREISTGAGAIREQLADLDLRIIIDYSSVEWKELGEEGPTGNEWEDRKVGRRKDFLVRRVELAKHFIRTNIEPEWMVLCLLPVLPPELRPIIQIDGGKLMSSDINELYRRVIYRNNTLIDLLTTSRSTPGELVMCQEKLVQEAVDTLLDNGIRGQPMRDGHNKVYKSFSDVIEGKEGRFRETMLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQIFVIRGLIRQHLASNIGVAKSKIREKEPIVWEILHEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVCKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVPTQDMLIGLYVLTSGNRRGICANRYNPCNRRNYQNKRIDGNNDKYTKEPLFSNSYDALGAYRQKRIHLDSPLWLRWQLDQRAITSREAPIEVHYESLGTYHEIYEHYLIVRNIKKEILCIYIRTTVGHISLYREIEEAIQGFCQACSDGI | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular locations: Plastid, Chloroplast |
RR15_DAUCA | Daucus carota | MIKNSFSAIFFKEENEDNKGSVEFQVVSFTNRIRKLTSHLELHKKDYLSQRGLRKILGKRQRLLAYLSKKNRVRYKELIGQLEIRETKKN | Subcellular locations: Plastid, Chloroplast |
RR18_MANES | Manihot esculenta | MDKSKRLFLKSKRSFRRRLPPIQSGDRIDYRNMSLISRFISEQGKILSRRVNRLSLKQQRLITIAIKQARILSSLPFLNNEKQFEKKRVGRYNY | Subcellular locations: Plastid, Chloroplast |
RR2_DAUCA | Daucus carota | MTKRYWNIDLEEMMKAGVHFGHGTRKWNPKMAPYISAKRKGIHIINLTRTARFLSEACDLVFDAASRGKQFLIVGTKNKAADLVAWAAIRARCHYVNKKWLGGMLTNWSTTETRLHKFRDLRTEQKTGRLRRLPKRDAAVLKRQLSHLQTYLGGIKYMTGLPDIVIIIDQHEEYTALQECITLGIPTISLIDTNCDPDLADISIPANDDAISSIRLILNKLVFAIREGRSSYIRNP | Subcellular locations: Plastid, Chloroplast |
SODM_PRUPE | Prunus persica | MALRTLVSRRTLATGLGFRQQLRGLQTFSLPDLPYNYGALEPAISGDIMQLHHQNHHQTYVTNYNKALEQLHDAISKGDAPTVAKLHSAIKFNGGGHINHSIFWKNLAPVREGGGEPPKGSLGWAIDTNFGSLEALVQKMNAEGAALQGSGWVWLALDKELKKLVVETTANQDPLVTKGPTLVPLLGIDVWEHAYYLQYKNVRPDYLKNIWKVINWKYASEVYEKESP | Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular locations: Mitochondrion matrix
Expressed most abundantly in parts of the plant which exhibit a high metabolic activity. Expressed in pre-shooting flower buds, vegetative buds, immature fruits and fully expanded leaves of basal shoots and seedlings. |
SUS1_DAUCA | Daucus carota | MGEPVLTRVHSLRERMDSTLANHRNEILMFLSRIESHGKGILKPHQLLAEYEAISKEDKLKLDDGHGAFAEVIKSTQEAIVSPPWVALAIRLRPGVWEYVRVNVHHLVVEELSVPQYLQFKEELVIGSSDANFVLELDFAPFTASFPRPTLTKSIGNGVEFLNRHLSAKMFHGKDSMHPLLEFLRLHNYNGKTLMLNNRVQNVNGLQSMLRKAGDYLSTLPSDTPYSEFEHKFQEIGFERGWGDTAERVTEMFHMLLDLLEAPDASTLETFLGKIPMVFNVVILSPHGYFAQENVLGYPDTGGQVVYILDQVPALEREMIKRIKEQGLDIKPRILIVTRLLPDAVGTTCNQRLEKVFGAEHAHILRVPFRTEKGILRKWISRFEVWPYIETFTEDVAKEIALELQAKPDLIIGNYSEGNLVASLLAHKLGVTQCTIAHALEKTKYPDSDIYWEKFDKKYHFSSQFTADLIAMNHTDFIITSTFQEIAGSKDTVGQYESHTAFTMPGLYRVVHGIDVFDPKFNIVSPGADTSVYFSYKEKEKRLTTLHPEIEELLYSSVENEEHLCIIKDKNKPILFTMARLDNVKNLTGFVEWYAKSPKLRELVNLVVVGGDRRKESKDLEEQAQMKKMYELIDTYKLNGQFRWISSQMNRVRNGELYRYIADTKGAFVQPAFYEAFGLTVVEAMTCGLPTFATLHGGPAEIIVHGKSGFHIDPYHGEQVAELLVNFFEKCKTDPSQWDAISAGGLKRIQEKYTWQIYSERLLTLAGVYGFWKHVSKLDRLEIRRYLEMFYALKYRKLAESVPLAKDE | Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.
Expressed in stems, in roots at different developmental stages, and in flower buds, flowers and maturing seeds, with the highest levels in strong utilization sinks for sucrose such as growing stems and tap root tips. |
TAC1_PRUPE | Prunus persica | MKIFNWVHKRLHQRVVKDGFAGNVKKSELETNDKDTQAFLKQVGLVNVDGLDGWRDGILTIGTFGFDPLKPSTHQNEYFVLESEEDDQESHGFSHSGNDDDDDDDEHYDHSVEDEELNPLMFTTFEHSFEDIGSNFDAIVQKPADVILTVDGVPLTPFEGSSEISTKPDQSANDQSKNKKGQRITLADLFQADVPDVGQLKLDSGKVQPEMEKKMNARTRSGLAFAKKLIPRVKDDSSPIKNMQRLMRRMLKRKIHPAELEVKIHKSDGQKQPSAVELISNVENDAYESVSLLPIQGAPCVH | Involved in the regulation of axillary shoot growth angle . Promotes horizontal shoot growth .
Highly expressed in flower buds . Expressed in branch attachment sites, vegetative buds and young fruits . |
TLP1_PRUPE | Prunus persica | MMKSQAALLGLTTLAILFFSGAHAAKITFTNKCSYTVWPGTLTGDQKPQLSLTGFELATGISRSVDAPSPWSGRFFGRTRCSTDASGKFTCATADCGSGQVSCNGNGAAPPATLVEITIASNGGQDFYDVSLVDGFNLPMSVAPQGGTGKCKASTCPADINKVCPAPLQVKGSDGSVIACKSACLAFNQPKYCCTPPNDKPETCPPPDYSKLFKTQCPQAYSYAYDDKSSTFTCSGRPAYLITFCP | May be involved in protecting plant tissues from pathogen infection.
Subcellular locations: Secreted
Equally expressed in the abscission zone and surrounding tissues of both fruitlets and leaves. |
TLP2_PRUPE | Prunus persica | MMKTLGAVLSLSLTLLSFGGAHAATMSFKNNCPYTVWPASFGNPQLSTTGFELASQASFQLDTPVPWSGRFWARTRCSTDASGKFVCETADCDSGQLMCNGKTGIPPATLAEFTIAAGGGQDFYDVSLVDGFNLPMSVTPQGGTGTCKMGSCAANVNLVCPSELQKIGSDGSVVACLSACVKFGEPQYCCTPPQETKEKCPPTNYSQIFHEQCPDAYSYAFDDNKGLFTCSGGPNYLITFCP | May be involved in protecting plant tissues from pathogen infection.
Subcellular locations: Secreted
Preferentially expressed in the abscission zone of fruit. Also expressed in leaf abscission zone. |
14KD_DAUCA | Daucus carota | MGSKNSASVALFFTLNILFFALVSSTEKCPDPYKPKPKPTPKPTPTPYPSAGKCPRDALKLGVCADVLNLVHNVVIGSPPTLPCCSLLEGLVNLEAAVCLCTAIKANILGKNLNLPIALSLVLNNCGKQVPNGFECT | May be connected with the initiation of embryogenesis or with the metabolic changes produced by the removal of auxins.
Subcellular locations: Membrane |
1A11_PRUMU | Prunus mume | MGSSSATANRFLLSKIATSEGHGENSPYFDGWKAYDRNPFHPTKNPEGVIQMGLAENQLSFDSIEDWIKKNPKASICTPEGVEEFKNVAIFQDYHGFPEFRKAVAMFMSKARGGRVTFDPNRVVMSGGATGANELVMFCLADPGDAFLVPSPYYPAFFRDLGWRTGVQIVPVDCDSSNNFKITKEALEAAYEKAQKNNINVKGLIITNPSNPLGTTLDRNTLESLVEFINQKNIHLVCDEIYAATVFSSPTFTCISEVIQNMNCNPNLIHIVYSLSKDMGLPGLRVGIVYSYNDDVVNIGRKMSSFGLVSSQTQHMLPSMLLDEEFVARFLETSPKRLAKRHGVFTKGLEEVGINCLKSNAGLFCWMDLRRLLEDQTFDGEMVLWRVIVNEVGPNVSPGSSFKCVEPGWFRVCFANMDDETLEVALKRIRTFVRQGKKAQDQVVQVKSPKRWKSNLRLSFSSSSTRRFDQESVNVLSPHMMSPHSPLVRAKT | Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants. |
AH1_PRUSE | Prunus serotina | AKTDPPIHCASLXRSS | null |
AH2_PRUSE | Prunus serotina | AKTDPPIHFASLXRS | null |
AH3_PRUSE | Prunus serotina | ADPPIHIASL | null |
AH4_PRUSE | Prunus serotina | TDPPIHIASLXRS | null |
ARF1_DAUCA | Daucus carota | MGLSFTKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEIIDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIASKS | GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular locations: Golgi apparatus |
ATPH_MANES | Manihot esculenta | MNPLISAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
C7916_PRUMU | Prunus mume | MEANVGFLTLCLAITLVRFLMKRYWHQSKINDKNNKAIKQHYPLPPTPKGLRPWPIVGNLPEMLMNKPTFRWIHKLMEESNTQIACIRLANVHVTPVSCPILSREILKKQDATFATRPLSISTFLITKGYITTVMVPFGEQWKKMRKVITSELLSPMRHKWLTDKRIEEADHLVRYVFNQCNNDEGSGIVDLRLATQHYCANVIKRMIFNQRYFTEEMKDGGPSVEEQNYVNAVFDMLRYIYAFSASDYISCLRGLDLDGHEKIIKDCIKLTRKRQDPVIEERIREHQKLGGNKVPVDLLDILISLKDASGQPLLSTDEIKGQVNEMIMAAVDNPSNAAEWAIAEMINQPHLFEKARQELDAVVGKERQVQESDLSQLNFVKACAREAFRLHPVAPFNVPHVSMADTTVGDYFIPKGSHVMLSRIGLGRNPKIWDEPLKYKPERHLKDDGSGVVLTESELRFISFSTGMRGCVASTLGTSMTVMLFARLLHGFTWEAPPNESRIDLTEADGELLLAKPLFALAKPRLPAHVYQT | Involved in L-phenylalanine-derived cyanogenic glycoside biosynthesis, including prunasin and amygdalin defensive agents . Catalyzes the conversion of L-phenylalanine (Phe) into phenylacetaldoxime (PAOx) . Cannot use tyrosine (Tyr), tryptophan (Trp) and valine (Val) as substrates .
Expressed in seedlings. |
C7968_PRUMU | Prunus mume | MSLPYLFLDSEVTPPISLSLAFIIFMFLVKFILKTHNKNSVPVVPLPPGPSPWPIVGSLPEMWRNRPAHRWIHSLMKKLNTDIACIRLGNVHVIPVTSPEIAREFLKKNDAVFASRPVTMATKTLSSGYLTTVVGPWGDQWRKMRRVLVAEAFNPSRVHWLLGKRNEEADNLVKFLYNQCSANQNGAVVNVRIAAQFYSGSIMRKMIFNRTYFGKGREDGGPGVEEEEHVSALLTLLTYAYAFCVSDYLPWLRVFDIDGHEKKVRKAMNIVKKHQEPIVNERLQEWRDGKRNEPDDLLDVFISLKDANGQPLLSDEEIKAQTTELQLSTVDSPFNIAEWALTEMLNQPEMLKKAEEELDRVVGKKTLVQESHVPHLPYIRACAKEVMRLHPVGPFNLPHVSIADAEVAGYFIPKGSNVILSRLELGRNPRVWEEPLRFNPERHLNIAVDQQVDLEENDLRFVSFSTGRRGCMGVGLGSTIVVMLLARLLQGFSWSLPPDVDKIDFTEDQIYLKKASPLLAQAKPRLPASVYPI | Catalyzes with low efficiency E and Z isomers of indole-3-acetaldoxime from tryptophan (Trp).
Subcellular locations: Membrane
Confined to buds. |
C79D1_MANES | Manihot esculenta | MAMNVSTTIGLLNATSFASSSSINTVKILFVTLFISIVSTIVKLQKSAANKEGSKKLPLPPGPTPWPLIGNIPEMIRYRPTFRWIHQLMKDMNTDICLIRFGRTNFVPISCPVLAREILKKNDAIFSNRPKTLSAKSMSGGYLTTIVVPYNDQWKKMRKILTSEIISPARHKWLHDKRAEEADNLVFYIHNQFKANKNVNLRTATRHYGGNVIRKMVFSKRYFGKGMPDGGPGPEEIEHIDAVFTALKYLYGFCISDFLPFLLGLDLDGQEKFVLDANKTIRDYQNPLIDERIQQWKSGERKEMEDLLDVFITLKDSDGNPLLTPDEIKNQIAEIMIATVDNPSNAIEWAMGEMLNQPEILKKATEELDRVVGKDRLVQESDIPNLDYVKACAREAFRLHPVAHFNVPHVAMEDTVIGDYFIPKGSWAVLSRYGLGRNPKTWSDPLKYDPERHMNEGEVVLTEHELRFVTFSTGRRGCVASLLGSCMTTMLLARMLQCFTWTPPANVSKIDLAETLDELTPATPISAFAKPRLAPHLYPTSP | Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Can use L-valine or L-isoleucine as substrate, but not L-leucine, L-phenylalanine, L-tyrosine, D-valine or D-isoleucine.
Subcellular locations: Microsome membrane
Expressed in the epidermis, the next two cortex cell layers, the endodermis and the pericycle of leaf petioles. Strong expression around the laticifers among the phloem cells and in parenchymatic cells between the protoxylem and the metaxylem cells. In the leaves, preferentially expressed in the mesophyll cells adjacent to the epidermis. |
CALR_PRUAR | Prunus armeniaca | MAFRVPNSSLLSLILLSLLAIASAKVFFEERFEDGWDKRWVTSEWKKDENLAGEWNYTSGKWNGDPNDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYIKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILNYNNTNNLIKKDVPCETDQLTHVYTFIIRPDATYSILIDNLEKQTGSLYSDWDLLPAKKIKDPEAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGEWKPKKIKNPNFKGKWKAPLIDNPEFKDDPELYVYPNLKYVGIELWQVKSGTLFDNILITDEPEYAKQLAEETWGKQKDAEKAAFEELEKKLQEEESKEDPVDSDAEDDDNEAEDGEESDSESKPDSTEESAETEAEKHDEL | Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Subcellular locations: Endoplasmic reticulum lumen |
E13B_PRUPE | Prunus persica | MTKSNSSSVGRLLSLISIVLLLGQLVVGSLATKQHTGAPIGVCNGMVGDDLPPQAEVVALYKTNNIPRMRLYDPNPAALEALRGSNIKLLLGVPNENLQYIALSQANANAWVQNNVRNYANVKFKYIAVGNEVKPSDSFAQFLVPAMRNIQEAISLAGLAKKIKVSTAIDTGVLGETFPPSIGSFKSEYNALLYPIIRFLVSHQSPLLVNLYPYFAYSGNTQDIRLDYALFTAPSVVVQDGNFGYRNLFDAMLDGVYAALEKAGGGSLKVVISETGWPSAAGTATTIDNARTFISNLIQHVKEGTPRRPGRPIETYIFAMFDENRKTPELEKHWGLFSPTKQPKYQISFN | Is thought to be an important plant defense-related product against fungal pathogens. |
IF5A_MANES | Manihot esculenta | MSDEEHHFESKADAGASKTFPQQAGTIRKNGYIVIKNRPCKVMEVSTSKTGKHGHAKCHFVGIDIFNGKKLEDIVPSSHNCDVPHVNRTDYQLIDISEDGFVSLLTETGNTKDDLRLPTDENLLSQIKDGFAEGKDLVVSVMSAMGEERICSLKDIGPKN | Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). |
NDHK_MANES | Manihot esculenta | MNSIEFPLLDRTTQISVISTTSNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKISREIYEDRIRSQPGKRCFTTNHKFNIERTTHTGNYDQELLYQSPSTSKIPPETFFKYKRSVSSNELVN | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
NLTP3_PRUDU | Prunus dulcis | MASSGQLLKLVCLVAVMCCMAVGGPKAMAAVSCGQVVNNLTPCINYVANGGALNPSCCTGVRSLYSLAQTTADRQSICNCLKQAVNGIPYTNANAGLAAGLPGKCGVNIPYKISPSTDCKSIK | Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity). |
NU4C_MANES | Manihot esculenta | MNSFPWLTIFVVLPISGGSLIFLFPHRGNKVIKWYTIFICIFELLLMTYAFSYYFQLDDPLIQLTEDYKWIQFFDFYWRLGIDGFSLGPILLTGFITTLATLAARPITRDSRLFHFLMLAMYSGQIGLFSSQDLLLFFIMWELELIPVYLLLSMWGGKKRLYSATKFILYTAGGSVFLLMGALGIALYGSNEPRFHFETSANQSYPVALEIFFYIGFLIAFAVKSPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLVRINMELLPHAHSIFSPWLIIVGVMQIIYAASTSPGQRNLKKRIAYSSVSHMGFIIIGICSISDMGLNGAILQIISHGFIGAALFFLAGTGYDRIRRVYLDEMGGMATSMPKIFTTFSILSLASLALPGMSGFFAELIVFFGIITGQKYLLMSKILITFVMAVGMILTPIYLLSMLRQMFYGYKLFNAPNSYFFDSGPRELFVSISILLPVIGIGFYPDFVFSLSVDRVEAILSNYFYR | Subcellular locations: Plastid, Chloroplast thylakoid membrane |
NU6C_MANES | Manihot esculenta | MDLPGLIHDFLLVFLGLGLILGGLGVVLLTNPIYSAFSLGLVLVCISLFYILSNSHFVAAAQLLIYVGAINVLIIFAVMFMNGSEYYKDFNLWTVGSGVTSLVCTSIFVSLITIIPDTSWYGIIWTTKTNQIIEQDLISNGQQIGIHLSTDFFLPFEFISIILLVALIGAIAVARQ | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PER7_DAUCA | Daucus carota | NYPTQDSTMDKTFANNL | Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. |
PER8_DAUCA | Daucus carota | NAPPNLTLR | Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. |
PER9_DAUCA | Daucus carota | GQNFTSDKDLYTDSR | Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. |
PSAI_DAUCA | Daucus carota | MTTFDFPSVLVPLVGLIFPAMAMASLFLHVQNNKTV | May help in the organization of the PsaL subunit.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBB_MANES | Manihot esculenta | MGLPWYRVHTVVLNDPGRLLSVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWSITGGTITNPGIWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPVSPAWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLVDGDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPVTVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGAFQKLGDPTTRRQVV | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBI_MANES | Manihot esculenta | MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGREE | One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBZ_DAUCA | Daucus carota | MTLAFQLAVFALIATSSILLIGVPVVFASPDGWSSNKNVLFSGTSLWIGLVFLVGILNSLIS | May control the interaction of photosystem II (PSII) cores with the light-harvesting antenna, regulates electron flow through the 2 photosystem reaction centers. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
RK2_MANES | Manihot esculenta | MAIHLYKTSTPSTRNGAVDSQAKSNTRNTRKNLIYGQHRCGKGRNARGIITARHRGGGHKRLYRKIDFRRNEKDIYGRIVTIEYDPNRNAYICLIHYGDGEKRYILHPRGAIIGDTIISGTEVPIKMGNALPLTDMPLGTAIHNIEITLGKGGQLARAAGAVAKLIAKEGKSATLKLPSGEVRLISKNCSATVGQVGNTGVNQKSLGRAGSKCWLGKRPVVRGVVMNPVDHPHGGGEGRAPIGRKKPATPWGYPALGRRSRKRNKYSDNLILRRRSK | Subcellular locations: Plastid, Chloroplast |
RK33_DAUCA | Daucus carota | MAKGKDVRITVILECTGCVRNGVNKVSTGISRYITEKNRHNTPNRLELRKFCPFCYKHTMHGEIKK | Subcellular locations: Plastid, Chloroplast |
RPOC2_DAUCA | Daucus carota | MEVLMAERANLVFHNKVIDGTAMKRLISRLIDHFGMAYTSHILDQVKTLGFQQATATSISLGIDDLLTIPSKRWLVQDAEEQSFILEKHHHSGNVHAVEKLRQSIEIWYATSEFLRQEMNPNFRMTDPFNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRKDCGTARGISVSLGNGMMSENIFIQTLIGRVLADDIYMGTRCIATRNQDIGSGLVNQFITFRAQPIYIRTPFTCRSTSWICQLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGIAEHVRAPSNGKIKFNEDLVHPTRTRHGHPAFVCSIDLYVTIESEDILHNVNIPPKSFLLVQNDQYVESEQVIAEIRAGTSTLNFKEKVRKHIYSDSEGEMHWNTDVYHAPEFTYGNVHLLPKTSHLWILLGEPRRSDLISLSIHKDQDQMNARSFSVKKRSISNLSVTNDQVRHKFFSSDFFGKKEEEHPDYSELNRIVRCNLRYPTIPYADYDLLAKRRRKRFIIPLQSIQERENELMPPSGISIEIPINGIFRINSILAFFDDPRYRRKSSGITKYGTIEVDPIAKKEDLIEYRGVKEFKPKYQIKVDRFFFIPEEMHILPGSSSIMVRNNSIIGIDTQIALTTRSRVGGLVRVEIKKKRIELKIFSGDIHFPGETDKISRHSGVLIPPGTGKTNSKESKKGKNWIYVQRITPTNKKYFVLVRPVVTYEITDGINLVRLFPPDLLQEMDNVQLRVVNYILYGNGKPIREIYNTSIQLVRTCLVLNCTQDKKSSYIEETRTSFVEIGINGLSRDFIKIDLVKSPISYTAKRNDPSRSGLIYENGSDCTNINPFSSRFFYYSNARIKESLNQNQGTIHTLFNRNKEYQSLIILSSSNCFRMGPFNNVKYHNVIKESIKKDPPIPIRNLLGPLGTALKTANFYPFSHLITYNQILVINYLQLDNLKQTFQVIKYFLMDEIGKIYNYDLCSNIILNPFNLNWYFLQHNYCEGMSTIMSLGQFICENVCIAKNGPHLKSGQVLIVKMDSVVIRSAKPYLATPGATVHGHYGEILYEGDTLVTFIYEKSRSGDITQGLPKVEQVLEVRSIDSISMNLEKRVEGWHECITRTLGIPWGFLIGAELTIVQSRIALVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEDGMSNVFLPGELIGLLRAERMGRALEEAICYRAVLLGITKASLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGMIPVGTGFEGLVHSSRQHTNLSLETKNNNIFEGEMRDILFHHRKFFDSCFSKNFHDTSEQSFIGIGFNDS | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular locations: Plastid, Chloroplast |
RR14_MANES | Manihot esculenta | MARKSLIQREKKRQKLEQKYHLMRRSSKKEISKVPSLSDKWEIHGKLQSPPRNSAPTRLHRRCFSTGRPRANYRDFGLSGHILREMVHACLLPGATRSSW | Binds 16S rRNA, required for the assembly of 30S particles.
Subcellular locations: Plastid, Chloroplast |
RR7_DAUCA | Daucus carota | MSRRGTAEEKTAKSDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRAVKKIQQKTETNPLSVLRQAIRGVTPDIAVKARRVGGSTHQVPIEIGSTQGKALAIRWLLAASRKRPGRNMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Subcellular locations: Plastid, Chloroplast |
RS4_PRUAR | Prunus armeniaca | MARGLKKHLKRLNAPKHWMLDKLGGAFAPKPSSGPHKSRECLPLILILRNRLKYALTYREVVSILMQRHILVDGKIHFCIRLSDVVSIPKTNENFRLLYDTKGRFRLHSIRDEESKFKLCKVRSVQFGQKGIPYINTYDGRTIRYPDPLIKANDTIKLDLETNKITDFIKFDVGNVVMVTGGRNRGRVGVIKNREKHKGSFETIHVQDATGHEFATRLGNVFTIGKGTKPWVSLPKGKGIKLTILEEAKKRQAAAQTAATA | Subcellular locations: Cytoplasm |
RS8_PRUAR | Prunus armeniaca | MGISRDSMHKRRATGGKKKAWRKKRKYELGRQPANTKLSSNKTVRRIRVRGGNVKWRALRLDTGNFSWGSEAVTRKTRLLDVVYNASNNELVRTQTLVKSAIVQVDAAPFKQWYLQHYGVEIGRKKKTAAAKKDTPEEGEATTEEAKKSNHVAIKLEKRQQGRTLDAHIEEQFGGGKLLACISSRPGQCGKADGDILEGKELEFYMKKLQRKKGKGAGAAA | null |
TBA_PRUDU | Prunus dulcis | MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPGDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESAEGEDDEGDDY | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular locations: Cytoplasm, Cytoskeleton |
TOP1_DAUCA | Daucus carota | MKSNPGITVIKQNASNVMEKTLKEEGQSRSNSEDSDDDKPLSHKLSSGALNGNSHHIRMGSNLSCPSPYTSPKPRIIKGPEDEMLLSSELQLNAGASNAESSDSDESKPLASELEDPSSSLNKRPLIQPKNSDPSPSKKAKLSEPSAPTNRKLKTAEQEEAAADDDPSISNRNKKSTTPASKVSDKKKRPDVSASVNKVDFSKSLKVPLVLVKGRNGQPLVHNGVIFPPLYKPHGVKMLYRENPVDLTPEQEEVATMFAVMLETEYMTKPKFRENFMSDWRKILGEKHIIQNLEDCDFTPIYEWHQREKEKKKQMSTDEKKAIKEGKDETRKEKYMWAVVDGMSREKVGNFRVGTTRVVQRSWRASKDPQVKKNVYSQIDITINIGKDAPIPEPPIPGERWKEIRHDNTVTWLAFWNDPINPKEFKYVFLAASSSLKGKVTREKYEKSRKLKDYIEGIRAAAYTKDFASKDSKKRQIAVATYLIDKLALRAGNEKDDDEADTVGCCTLKVENVETKRPNILKFDFLGKDSIRYQNEVEVEPRVFSAIEQFRSGKEGGDDLFDQLDTSKLNAHLKELMPGLTAKVFRTYNASITLDEMVRCKLLSRETKGGDVAEKVVVYQHANKEVAIICNHQRTVSKSHSAQMVRLNEKIEELKGLLKELQEDLTRVNKGKPPLKNSDGKPKRNLNLKRYKGKLLKLIQKLRKWSETRRLSVTKKIAQTNTKIEKMERDKETKEDLKTVALGTSKINYLDPRITVAWCKRHDVPIEKIFNKSLLAKFAWAMDVVLIFRF | Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Subcellular locations: Nucleus |
CYF_DAUCA | Daucus carota | MQTRKTFSWIKEQINRSISVSLMIYIITRPSISIAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQTVLPDTVFEAVVRIPYDMQLKQVLANGKRGTLNVGAVLILPEGFELAPADRISPEMKEKIGNLSFQSYRPNKKNILVIGPVPGQKYSEITFPILSPDPATTKEVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATSAGIVGKIIRKEKGGYEITIADASDGRQVVDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLASVILAQIFLVLKKKQFEKVQLSEMNF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
INVB_DAUCA | Daucus carota | MDTYHFLPSRDLEHASSYTPRPDSPETRHEPDPDRSKTNRRPIKIVSSVLLSTLILSFVIFLLVNPNVQQVVRKKVSKNSNGEDRNKASKSPEMLGPPSRGVSQGVSEKSFRQATAEPSYPWTNDMLSWQRTSFHFQPQENWMNDPNGPLFHMGWYHLFYQYNPDSAIWGNITWGHAISRDLINWLHLPFAMQPDQWYDINGVWTGSATVLPDGKIVMLYTGDTDDLVQVQNLAYPANLSDPLLLDWIKYPDNPVMFPPPGIGSTDFRDPTTAWIGRDGKWRITIGSKVNKTGISLMYKTTDFITYELLDNLLHAVPGTGMWECVDFYPVSVTGSNGLDTSVNGPGVKHVLKSSLDDDRHDYYALGTYDPINDKWTPDNPELDVGIGLRLDYGKYYASKTFYDQDKERRLLWGWIGETDSESADLLKGWASVQSIPRTVVFDKKTGTNILQWPVKEVESLRSRSYEIDDVELKPGSLVPLKISSAAQLDIVASFEVDEEAFKGTYEADASYNCTASEGAAGRGILGPFGILVLADDPLSELTPVYFYIAKGVDGNAKTYFCADQSRSSTASDVDKEVYGSDVPVLHGESLSMRLLVDHSIVESFAQGGRTVITSRVYPTRAIYSAARVFLFNNATGVSVTASVKAWQMASATLKPFPFDQL | May participate in the regulation of the hexose level in mature tissues and in the utilization of sucrose stored in vacuoles.
Subcellular locations: Membrane, Vacuole, Vacuole lumen
May be released into the lumen of the vacuole from the tonoplast through a proteolytic processing. |
NU2C1_DAUCA | Daucus carota | MIWHVQNENFILDSTRIFMKAFHLLLFDGSLIVPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPVISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATMKYLLMGGASSSILVHGFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSPAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLETLAILSMILGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNDGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLYLFWCGWQAGLYFLVLIGLLTSVVSIYYYLKIIKLLMTGRTQEITPHVRNYRRSPFRSNNSIELSMIVCVIASTIPGISMNPIIAIAQDTLF | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
NU2C1_MANES | Manihot esculenta | MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATTKYLLMGGASSSILVHAFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSLAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMIVGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNGGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVLIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIELSMIVCVIASTIPGISMNPIVEIAQDTLF | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
NU3C_MANES | Manihot esculenta | MFLIYEYDIFWAFLIISSVIPILAFLISGVLSPISKGPEKLSSYESGIEPIGDAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGLSVFIEALIFVLILIVGSVYAWRKGALEWS | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PCNA2_DAUCA | Daucus carota | MLELRLVQGGLLKKVLESIKDLVNDANFDCSASGFSLQAMDSSHVALVAVLLRSEGFEHYRCDRNISMGMNLGNMAKMLRCAGNDDIVTMKADDDGDVITFMFESPTQDKISDFEMKLMDIDSEHLGIPESEYEAIVRMPSAEFARICKDLSTIGDTVVISVTKEGVKFSTRGDIGTANIVCRQNTSVDKPEDATIIEMQETVSLTFALRYMNSFTKATPLANQVTISLSSELPVVVEYKIAEMGYIRYYLAPKIEEEDEAANYAQPAQNSAAAATSNNGTKKNEGNNKVDSKKRAIKSEFVDDSEAATDAQPQAKAKTKTEAGEDDDVEVMDTKPKNEPDDGDEVMETKPKTESNGEVEVMDIE | This protein is an auxiliary protein of DNA polymerase delta and may be involved in DNA replication as its carrot homolog, typical PCNA. The larger PCNA is perhaps processed thus bestowing on it exactly the same function as its homolog.
Subcellular locations: Nucleus |
POR_DAUCA | Daucus carota | MALQAASFLPSSFSINKEGKANVSLKETSLFGVTFSDSLRTDFSSLRTRRGCRQISQTGAIRSQAVATTPSVNRATGEGKKTLRKGSVIITGASSGLGLATAKALAETGKWHVIMACRDFLKAERAAKSAGMPKENYTIMHLDLASLDSVRQFVETFRRSERPLDVLVCNAAVYFPTAKEPTYTADGFELSVGTNHLGHFLLSRLLLDDLNKSDYPSKRLIIVGSITGNTNTLAGNVPPKANLGDLRGLAGGLNGMNSSAMIDGAEFDGAKAYKDSKVCNMLTMQEFHRRYHEETGITFASLYPGCIATTGLFREHIPLFRTLFPPFQKYITKGYVSEAESGKRLAQVVSEPSLTKSGVYWSWNKDSASFENQLSEEASDVEKARKVWEVSEKLVGLA | Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Subcellular locations: Plastid, Chloroplast |
PSAA_DAUCA | Daucus carota | MIIRSPEPEVKILVDRDHIKTSFEEWARPGHFSRTLAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQLWRASGITSELQLYCTAIGALIFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLDWSKYSDFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYKTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIIVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWACIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPSATAPGATTSTSLTWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIVQGRAVGVTHYLLGGIATTWAFFLARIIAVG | PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBC_MANES | Manihot esculenta | MKTLYSLRRFYHVETLFNGTLSLAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICILGGIWHILTKPFAWARRALVWSGEAYLSYSLGALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBH_DAUCA | Daucus carota | MATQTVENVSRSRPKPTTVGGLLKPLNSEYGKVAPGWGTAPLMGVAMALFAIFLSIILEIYNSSVLLDGISMN | One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBL_DAUCA | Daucus carota | MTQSNPNEQDVELNRTSLYWGLLLIFVLAVLFSNYFFN | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface and is required for correct PSII assembly and/or dimerization.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSBN_MANES | Manihot esculenta | METATLVAISISGLLVSFTGYALYTAFGQPSQQLRDPFEEHGD | May play a role in photosystem I and II biogenesis.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
RBL_PRUDO | Prunus domestica | VGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEESQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFVEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEF | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Subcellular locations: Plastid, Chloroplast |
RBS_MANES | Manihot esculenta | MASSMLSTATVASINRVSPAQATMVAPFTGLKSTPVFPTTRKTNSDITSITSNGGKVQCMKVWPTLGMKKFETLSYLPPLTREQLASEVEYLLRSGWIPCLEFELEHGLVYREHARVPGYYDGRYWTMWKLPMFGCTDAAQVLKELDELIKHHPDGYARIIGFDNVRQVQCISFLAYKPPGA | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Subcellular locations: Plastid, Chloroplast |
RR7_MANES | Manihot esculenta | MSRRGTAEEKTAKSDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRAMKKIQQKTETNPLSVLRQAIRGVTPDIAVKARRVGGSTHQVPIEIGSTQGKALAIRWLLGASRKRPGRNMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Subcellular locations: Plastid, Chloroplast |
UP06_DAUCA | Daucus carota | YGLAADHVLDAR | null |
UP07_DAUCA | Daucus carota | YGLAADNVLDAR | null |
YCF3_DAUCA | Daucus carota | MPRSRINGNFIDKTFSIIANILLRIIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEAMRLEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAIRQGDSEIAEAWFDQAAEYWKQAIALTPGNYIEAHNWLKITRRFE | Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
ACCD_DAUCA | Daucus carota | MERWWFDSILFKKGFEHRCGLSKSMGGLGPIENTSESEDPNRNDMKKNSHSWGSRDNSSYSNVDYLFGVKDIWNFISDETFLVVDRNGNSYSIYLDIEKHIFEIDSGHFFQSGLESSFYSYWNLSYLNNGSKTDDPHDDHYMDDTQYSWNNHINSYIDIYLESQIFIDTYIVSGSDNYSNSYISRSVCGESESKGSNISTSTNGSTIIESSNDLDITQKYRHLWVQCENCYGLNYKKILKSKMNLCEQCGYHLKMSSSDRIELSIDPDTWDAMDEDMVSLDPIEFHSEEEPYKDRIDSYQRKTGLTEAVQTGIGQLNGIPIALGVMDFQFMGGSMGSVVGEKITRLIEYATNQLLPLIIVCASGGARMQEGSLSLMQMAKISSALYDYQSNKKLFYVPILTSPTTGGVTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPEGSQAAEYLFQKGLFDLIVPRNLLKSVLSELFQLHAFFPLNKNSIEH | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Subcellular locations: Plastid, Chloroplast stroma |
ACT1_DAUCA | Daucus carota | MADGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGIITLKYPIEHGIVSNWDDMRIWHHTFYNELRASPEEHPVLLTEAPLNPKANREKMTQIMIETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDGLMKILTEKSICHYTTAEREIVRDMKEKLAYVALDYEQELETAKRRSAVEKNYELPDGQVITIGAERFRCPQVLFQPSMIGMESAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSDLWIGGSILASLSTFQQMWISKGEYDESGPSIVHRKCLLAG | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
Subcellular locations: Cytoplasm, Cytoskeleton |
ATPI_MANES | Manihot esculenta | MNVLSCSINTLTLRGLYDISGVEVGQHFYWKIGGFQVHAQVLITSWVVIAILLGSAIVAVRNPQTIPTGGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWAGALLPWKIIQLPHGELAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFSKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPSVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CLPP_DAUCA | Daucus carota | MPIGVPKVPFRSPGEEDASWVDVYNRLYRERLLFLGQEVDSEISNQLIGLMVYLSIENDTKDLYLFINSPGGWVIPGVAIYDTMQFVRPDVQTICMGLAASMGSFILAGGEITKRLAFPHARVMIHQPASSFYEAQTGEFILEAEELLKLRETLTRVYVQRTDKPLWVVSEDMERDVFMSATEAQAYGIVDLVAVVE | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Subcellular locations: Plastid, Chloroplast stroma |
COX2_DAUCA | Daucus carota | MSFTGIFHFFTNSPCDAAEPWQLGSQDAATPMMQGIIDLHHDIFFFLILILVFVSRILVRALWHFHSKKNPIPQRIVHGTTIEILRTIFPSIIPMFIAIPSFALLYSMDEVVVDPAMTIKAIGHQWYRTYEYSDYNSSDEQSLTFDSYTIPEDDPELGQSRLLEVDNRVVVPAKTHLRIIVTSADVPHSWAVPSSGVKCDAVPGRLNQISISVQREGVYYGQCSEICGTNHAFTPIVVEAVSRKDYGSRVSNQLIPQTGEA | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular locations: Mitochondrion inner membrane |
CWP02_DAUCA | Daucus carota | QLAELKYVI | Subcellular locations: Secreted, Cell wall |
CWP03_DAUCA | Daucus carota | DLSNLLSRVPNERSN | Subcellular locations: Secreted, Cell wall |
CWP04_DAUCA | Daucus carota | GVREDTYPDVVXTA | Subcellular locations: Secreted, Cell wall |
CWP05_DAUCA | Daucus carota | AEYPNDVNLTVYWDP | Subcellular locations: Secreted, Cell wall |
CWP06_DAUCA | Daucus carota | SEVGALVFQPKTRF | Subcellular locations: Secreted, Cell wall |
DC104_DAUCS | Daucus carota subsp. sativus | MGVQKTEAEVTSSVSAEKLFKALCLDIDTLLPQVLPGAIKSSETLEGDGGVGTVKLVHLGDASPFKTMKQKVDAIDKESFTYAYSIIDGDILLGFIESINNHFAYVPNADGGCTVKSTITFNTKGDAVVPEENIKFANDQNRAIFQAVEAYLIAN | Expressed in roots (at protein level) (, ). Expressed in roots . |
GLNA1_DAUCA | Daucus carota | MASLTDLINLDLSDTTDKFIAEYIWIDAVGGLRSKARTLSGPVDDPTKLPKWNFDGSSTGQGPGDDSEVIIYPQAIFKDPFRRGNHILVMCDTYTPAGEPIPTNKRCNAAKIFSHPDVAAEVPWFGIEQEYTLLKKEVNCPIGCPTGGYPGPQGPYYCGIGADKAFGRDIVDAHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAGDELWVARYILERITEIAGVVVSLDPKPIPGDWNGAGAHTNYSTKSMRNEGGFEIIKKAIAKLETKHAQHIAAYGEGNERRLTGKHETASIHKFSWGVANRGASVRVGRDTEKEGKGYFEDRRPASNMEPYVVTSMIAETTIL | Subcellular locations: Cytoplasm |
GLNA2_DAUCA | Daucus carota | MAQILAPSVQWQMRFTKNSTEVSSMTSKMWGSLFLKQNKKAPARSSTKYRALAVKSEDGTINRMEDLLNLDVTPYTDKIIAEYIWIGGTGIDVRSKSRTISKPVEHPSELPKWNYDGSSTGQAPGDDSEVILYPQAIFKDPFRGGNNILVICDTYTPQGEPIPTNKRHKAAQIFSDAKVLGEVPWFGIEQEYTLMQQDVNWPLGWNVGGYPGPQGPYYCAAGADKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEFQVGPSVGIEAGDHIWCARYLLERITEQAGVVLTLDPKPIDGDWNGAGCHTNYSTKSMREEGGFEVIKKAILNLSLRHKEHISAYGEGNERRLTGKHETASIDSFSWGVADRGCSIRVGRDTEKEGKGYLEDRRPASNMDPYVVTGLLAETTLLWEPTLEAEALAAQKLSLNV | The light-modulated chloroplast enzyme, encoded by a nuclear gene and expressed primarily in leaves, is responsible for the reassimilation of the ammonia generated by photorespiration.
Subcellular locations: Plastid, Chloroplast |
GRP7_DAUCA | Daucus carota | MGSKIFLLLGLSIAFALLISSEVAARDLSETTTEGASLDGGHHGGGGGGHYSGGGGHGGSHHGGGGHGGCHHYCHGSCCSAAEAKALEAAQVKPQN | May be connected with the initiation of embryogenesis or with the metabolic changes produced by the removal of auxins. |
GRP9_DAUCA | Daucus carota | MGSKIFLLLGLSIAFAILISSEVAARELAETAAKTEGYNNGGGYHNGGGGYNNGGGYHNGGGGYNNGGGYHNGGGGYNNGGGYHNGGGGYNNGGGHHNGGGGYNNGGGHHGGGGSCYHYCHGRCCSAAEAKALEATTAQVKPQN | Subcellular locations: Membrane |
KCY_PRUAR | Prunus armeniaca | MWRRVTSVSHLFSHSKSTKFNQGASTFKIWETFTSESEIPTPSKGSPFVTFVLGGPGSGKGTQCAKIVEAFGFTHVSAGDLLRREIASGSAYGSVILSTIREGKIVPSQVTVELIQKEMESSDNYKFLIDGFPRSEENRKAFEQTIGAEPDVVLFFDCPEQEMVKRVLNRNQGRVDDNIDTIKKRLEIFDELNWPVINYYSQRGKLHKINAVGTVDEIFEKVRPIFAPLSK | Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Subcellular locations: Cytoplasm, Nucleus |
NDHI_DAUCA | Daucus carota | MFSMVTEFMNYSQQTVRAARYIGQGFMITLSHASRLPVTIQYPYEKLITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLEKDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPMSIINDYTTRTILNLPMK | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
NDHK_DAUCA | Daucus carota | MNSIEFPLLDRTTQNSVISTTSNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTISGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKISREIYEDRIKSQRENRCFTTNHKLKVGRSIHTGNYDREFLYQPTSTSEIPPETFFKYKSSVSSHELVN | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
NLTP_DAUCA | Daucus carota | MGVLRSSFVAMMVMYMVLATTPNAEAVLTCGQVTGALAPCLGYLRSQVNVPVPLTCCNVVRGLNNAARTTLDKRTACGCLKQTANAVTGLNLNAAAGLPARCGVNIPYKISPTTDCNRVV | Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Expressed in protoderm cells of somatic and zygotic embryos, and transiently expressed in epidermal cell layers of leaves, flowers and seeds. |
NU2C2_MANES | Manihot esculenta | MIWHVQNENFILDSTRIFMKAFHLLLFDGSFIFPECILIFGLILLLMIDSTSDQKDIPWLYFISSTSLVMSITALLFRWREEPMISFSGNFQTNNFNEIFQFLILLCSTLCIPLSVEYIECTEMAITEFLLFVLTATLGGMFLCGANDLITIFVAPECFSLCSYLLSGYTKKDVRSNEATTKYLLMGGASSSILVHAFSWLYGSSGGEIELQEIVNGLINTQMYNSPGISIALIFITVGIGFKLSLAPSHQWTPDVYEGSPTPVVAFLSVTSKVAASASATRIFDIPFYFSSNEWHLLLEILAILSMIVGNLIAITQTSMKRMLAYSSIGQIGYVIIGIIVGDSNGGYASMITYMLFYISMNLGTFACIVLFGLRTGTDNIRDYAGLYTKDPFLALSLALCLLSLGGLPPLAGFFGKLHLFWCGWQAGLYFLVLIGLLTSVVSIYYYLKIIKLLMTGRNQEITPHVRNYRRSPLRSNNSIELSMIVCVIASTIPGISMNPIVEIAQDTLF | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PER4_DAUCA | Daucus carota | ANLFTSDQDLYTDSR | Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. |
PER5_DAUCA | Daucus carota | YLGPTADSTMDQTFANN | Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. |
PSAJ_DAUCA | Daucus carota | MRDLKTYLSVAPVLSTLWFGSLAGLLIEINRFFPDALTFPFF | May help in the organization of the PsaE and PsaF subunits.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
PSK_DAUCA | Daucus carota | YIYTQ | In presence of 2,4-D, stimulates proliferation of the cells, but does not stimulate differentiation into the somatic embryos.
Subcellular locations: Secreted |
RK14_DAUCA | Daucus carota | MIQPQTLLNVADNSGARELMCIRIIGASNRRYAHIGDVIVAVIKEAVPNMPLARSEVVRAVIVRTCKELKRDNGMIIRYDDNAAVVIDQEGNPKGTRIFGAIARELRQLNFTKIVSLAPEVL | Binds to 23S rRNA.
Subcellular locations: Plastid, Chloroplast |
RK16_MANES | Manihot esculenta | MLSPKRTRFRKQHRGRMKGIAFRGNRICFGRYALQALEPAWITSRQIEAGRRAMTRNARRGGKIWVRIFPDKPVTLRPTETRMGSGKGSPEYWVAVVKPGRILYEMGGVAENIARKAISIAASKMPIRTQFIISG | Subcellular locations: Plastid, Chloroplast |
RK22_DAUCA | Daucus carota | MLKKLTKIKTEVYALGQHISMSAHKARRVVDQIRGRSYEETLMILELMPYRACYPILKLVYSAAANANYNMDSNESNLVISKAEVSEGTATKKLKPRARGRSFTIKRPTCHIAIVVKDISLDEYQYLGVDFIDSFRCSKKLQSKKKYTAMSYHDMYTNGGIWDKK | This protein binds specifically to 23S rRNA.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Subcellular locations: Plastid, Chloroplast |
RK36_MANES | Manihot esculenta | MKIRASVRKICEKCRLIRRRGRIIVICFNPRHKQRQG | Subcellular locations: Plastid, Chloroplast |
RL4_PRUAR | Prunus armeniaca | MAAAAAAARPLVTVQSLEGDMATDQTQTVALPDVMKASIRPDIVTFVHSNISKNSRQPYAVSKKAGHQTSAESWGTGRAVSRIPRVPGGGTHRAGQGAFGNMCRGGRMFAPTKIWRRWHRKINVNQKRYAVVSAIAASAVPSLVLARGHKIETVPELPLVVSDSIEGVEETSAALKVLKQIGAYSDAEKAKDSHSIRPGKGKMRNRRYINRKGPLIVYGTEGAKLVKAFRNIPGIDIINVERLNLLKLAPGGHLGRFVVWTKSAFEKLDSIYGSFDKVSEKKNGYVLPRSKMVNADLARIINSDEVQSVVSPIQEGSKRAPLKKNPLRILNTMLKLNPYAKTARRMSLLAEAERVKAKKEKLDKKRKPISKEEASTIKAAGKAWYQTMISDSDYTEFDNFTKWLGVSQ | null |
RPOC1_DAUCA | Daucus carota | MIDQYKHQQLRIGSVSPQQISTWANKILPNGERVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNYRVIGDKKKDRKSCEQCGVEFVDSRIRRYQMGYIKLACPVTHVWYLKRLPSYIANLLDKPLKELEGLVYCDFSFARPIAKKPTFLRLRGLFEYEIQSWKYSIPLFFTTQGFDTFRNREISTGAGAIREQLADLDLRIIIDSSLVEWKELGEDGPTGNEWEDRKVGRRKDFLVRRMELAKHFIRTNIDPKWMVLCLLPVLPPELRPIVQIDGGKLMSSDINELYRRVIYRNNTLTDLLTTSRSTPGELIMCQEKLVQEAVDTLLDNGIRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLYQCGLPREIAIELFQTFVIRSLIRQQLASNIGVAKSKIREKKPIVWEILREVMRGHPVLLNRAPTLHRLGIQAFQPVLVEGRAICLHPLVRKGFNADFDGDQMAVHVPLSFEAQAEARLLMFSHINLLSPAIGDPISVPTQDMLIGLYVLTSGNRRGICVNRYNPSNHRNQNKRIYENNYKYTKEKEPFFCNSYDAIGAYRQKRINLDSPLWLRWRLDQRVIAAREAPLEVHYESLGTYYDIYGQYLIVRSIKKEILSIYIRTTVGHISIYREIEEAIQGFCQAC | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular locations: Plastid, Chloroplast |
RS27A_DAUCA | Daucus carota | MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGGKKRKKKTYTKPKKTKHKHRKVKLAVLQFYKVDESGKVQRLRKECPNGECGAGTFMANHFDRHYCGK | Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Component of the 40S subunit of the ribosome.
Subcellular locations: Cytoplasm, Nucleus |
RS3A_DAUCA | Daucus carota | MAVGKNKRISKGKKGGKKKATDPFAKKDWYDIKAPNVFQNKNVGKTLVSRTQGTKIASEGLKHRVFEVCLADLQGDEDQAYRKIRLRAEDVQGKNVLTNFYGMDFTTDKLRSLVRKWQTLIEAHVDVKTTDSYTLRMFCIGFTKKRANQQKRTCYAQSSQIRQIRRKMVEIMRNQASSCDLKELVAKFIPESIGREIEKATSSIFPLQNVFIRKVKILKAPKFDIGKLMEVHGDYSEDVGVKLERPIEETMVEGETEVVGA | Subcellular locations: Cytoplasm |
TBB2_DAUCA | Daucus carota | MREILHIQGGQCGNQIGSKFWEVVCDEHGIDPTGQVLSESDLQLDRINVYYNEASGGRYVPRAVLMDLEPGTMDSVKTGPHGQIFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCECLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSGHQLVENADECMVLDNEALYDICFRTLKLSTPSFGDLNHLISGTMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRTLTVPELTQQMWDSKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQILNVQNKNSSYFVEWIPNNVKSSVCDIPPRGLSMSSTFIGNSTSIQEMFRRVSEQFTAMFRPKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEDDYDDGEGSTGD | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular locations: Cytoplasm, Cytoskeleton
Found in areas of rapidly dividing tissues. |
UGTK4_MANES | Manihot esculenta | MGSISPQKPPHAILVPYPAQGHVNPLMQLGKLLHARGFYITFVNTEHNHRRLIRSRGQEFIDGLPDFKFEAIPDGLPYTDRDATQHVPSLSDSTRKHCLAPFIDLIAKLKASPDVPPITCIISDGVMAFAIDAARHFGILEIQFWTTSACGFMAYLHHIELVRRGIVPFKDESFLHDGTLDQPVDFIPGMPNMKLRDMPSFIRVTDVNDIMFDFLGSEAHKSLKADAIILNTFDELEQEVLDAIAARYSKNIYTVGPFILLEKGIPEIKSKAFRSSLWKEDLSCLEWLDKREPDSVVYVNYGCVTTITNEQLNEFAWGLANSKHPFLWIVRPDVVMGESAVLPEEFYEEIKDRGLLVSWVPQDRVLQHPAVGVFLSHCGWNSTIECISGGKPMICWPFFAEQQTNCKYACDVWKTGVELSTNLKREELVSIIKEMMETEIGRERRRRAVEWRKKAEEAISVGGVSYNNFDTFIKEVILQQQTQ | UDP-glucosyltransferase catalyzing in planta synthesis of cyanogenic glucosides. Able to glucosylate acetone cyanohydrin and 2-hydroxy-2-methylbutyronitrile, forming linamarin and lotaustralin. Accepts also to some extent, a wide range of potential acceptor substrates, including simple alcohols, flavonoids, isoflavonoids and other hydroxynitriles such as p-hydroxymandelonitrile, mandelonitrile, (E)-4-hydroxy-2-methylbut-2-enenitrile and (E)- 2-(hydroxymethyl)but-2-enenitrile.
Expressed in the cortex, xylem and phloem parenchyma, and in specific cells in the endodermis of the petiole of the first unfolded leaf. |