lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May play a role in intracellular calcium sensing and homeostasis. May act as a negative regulator of plasma membrane calcium-transporting ATPases preventing calcium efflux from the cell.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTEHEESGNGTNCRERHHHDGTTPRLLAPDNQGDEMYLGENEEDVGMISFKSSMRDDLDHVPCGKLRQFWALHKGLLLALLSCFAQACGSIGVKMLAGKIPPTEIASIRLLSYFVFCNISMVYFKISLRVTKKQLPWLLLRVTCGTTAMCLLFYAYQNIPIGDTSAIIFSSPIFTGIFAWILLGEKFTLVDMALALLTLVGIVLIARPSFLFGNFAEPSGDGNTLLGIIAALVGAIFASMVFVLIRKLGGISVHPLTQIWFFGLIGFILTTMLTAVLGIWVVPRCGRDRFVLIVVGVLGFVAQILMTYAFKLEKATYVAVMKSNNVILSFLFEFAIFGTVPFWLSIIGALLVMSSSLGITVKKWKASKSKKDKEDEDIRNVDQESDNEDEN
The following text describes a protein:
Function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MAEEITSQLKKNLLDEENGTSSHVVEGAADADADAELSPPSQKGDDAKEVSKKKKKKSKSKKKKELLQQTDPPSISVINLFPSGDFPEGEIQQYKDDNLWRTTSEEKRELERLQKPLYNSVRRAAEVHRQVRKYIKGILKPGMLMTDICETLENTVRKLISEDGLQAGIAFPTGCSLNWVAAHWTPNSGDKTILQYDDVMKLDFGTHVDGYIVDCAFTVAFNPMFDPLLEASREATNTGIKEAGIDVRLCDIGAAIQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAGKSVPIVKGGEQTKMEEGEFFAIETFASTGKGYVREDLECSHYMKNFDVGHIPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIVQPYPPLCDVKGSYVSQFEHTILLRPTCKEVISKGDDY
The following text describes a protein:
Function:
[Capsid polyprotein VP86]: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the immature VP70 virion; [Core protein VP33]: Self-assembles to form an icosahedral capsid with a T=3 symmetry, about 43 nm in diameter; [Spike protein VP38]: Forms the spikes at the surface of the virion (By similarity). Plays a role in the attachment to target host cell (By similarity).
Subcellular Localization:
[Capsid polyprotein VP86]: Virion. Note=Immature capsid; [Core protein VP33]: Virion. Note=Capsid; [Spike protein VP38]: Virion. Note=Capsid.
Domain:
[Spike protein VP38]: Contains the core attachment region and the P2 globular region; [Capsid polyprotein VP86]: Contains a lipid disrupting region that is exposed after trypsin treatment; [Capsid polyprotein VP86]: The highly basic N-terminus region binds to the viral RNA genome.
Sequence:
MAEKPQQKAVASAAKQLAKEVVKLDKITKSNGKQHPQKNVPARKWRPRQAKPNNRRVTHKIKRELHKQGLEGPASRFRVTVSATIGKVGPNKEQGPELQIATFLHPSLVKEPNDGSNFGPLQAAAAQWGLWRISDLEVRFTPLVGSSAVTGSVTRASLNLTQSPGATSWGGLGARKHLDVPTGVSKVWKLRRGDLTGPRQTWWVTDTNEEGGQSCGPMLEVHGLGKTTSTYKDSDWTGDLFIVELHGTWEFSNYNAKPALGMLERVTDQTNVELGVDTEGQITMTIPENSPMARHMGERFERASASNASSVGETIWQIVDEGAGLASSVAPAPFGWLIKGGWWFVKKILGRAANAGSQYLVYASLADAQNGKPAMSTSRGYVREVKQTILSSTQLNAPNTGPGASQPALAAYEMFPYFPHGEPAVGQPFYLMSTVSTGVYREAMPVWVKYNYPGAPSNQAPFEVTIGQTTYQAQTYFKLTEPVAYGADIPEVTSEVKPALNGWYTLDTLPAIGTFQAIFTLPGTKSKYGDVVAASHFSITPQLMLVAYLVRVTTALPNALRGSPWSDNADNSILYYTPLVNAYAAATSDANPIQFTPNRACVSECRSHCGHPTIVAADVGEYILALVWCRGNGFSAGVINSYGALADTSFNLDSLRADSNGVMTLLNRAVPYSSLCALRMTRGVPPTSDDELVARILGQLQTRLKFAAGSGSSSEDDLSDDDDFECLRSTPLQQIYEGVRGLRGHAEAVAVVKSLQSRGHAE
The following text describes a protein:
Function:
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MAVAVAKLLISAMAVFMLVSASFATSEVPFMVVHKKATLNRLKSGAERVSVSYDIYNQGSSSAYDVTLTDNSWDKKTFEVVNGNTSKSWERLDAGGILSHSIELEAKVKGVFYGAPAVVTFRIPTKPALQEAYSTPLLPLDILADKPPTKPLDVAKRLLAKYGSLVSVISMVVCFIYLVATPKSNVSKASSKKKR
The following text describes a protein:
Function:
Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.
Subcellular Localization:
Cytoplasm.
Sequence:
MKDPSRSSASPSIINEDVIVNGHAHEDDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQLSDLVIGDGSSLEDLVVKSNLNPNAKEFVPGVKYAVR
The following text describes a protein:
Function:
Acts as a coactivator during transcriptional activation of nuclear genes related to mitochondrial biogenesis and cell growth. Involved in the transcription coactivation of CREB and NRF1 target genes.
Subcellular Localization:
Nucleus.
Sequence:
MCLSDSSWDLPPSPFLEASSPKIPGWRTPRSWPRWGQLSPLQRSDGEEEEDARLSRDRVIAVDPSIDNTEDFPMHLACPEEEEEEEAAPVGEESISSLSELVRAMHPYCLPSLSVCLDSPGEEPEEQAEELMLAEGGMVLEILGQGSMAGEALEIPVVLRHLPPSSQPIEDLDSDLTQQLLECDMEAEVPTRVGQSFQKEPTAPGKLEDGREKELTCSALPQEEVIPASVNSPKGPSADVSSDAQKGQRGHRNRRKKSEVQLLPDRDKDRTCVQKLRKSRSQSIPDSQSSEQPLGVYRVAQSAGGRRKLRTTVVEPKIVSSLGNPDFTEPGSTPQSALVKEEPLTLCPSNGKMSLSSANGDHSQTPEPSFEVTSSQSERISSPSKTEHSANTVPQEAKPRPLSLSEYWQRRQQRQTGDQVPEPQTPTGKWPSIPVTPTELAEIPCLIVPSKTAEQPTAPGVARQRTAQPPGPKPCSVASPETDLPLPAKHKSLVRQSVPPTMPIPPTVPPVVPMSPAVPPTVTLPLTMPRPPALPPTMPPMVQLPSSGQVMPDLLRPPLPPPRLPRPPDSYAQFAPVPSWPRYPSVPPSVNYPCLPPPVSGTPNAYPGPSTPAVPWVLPPAPVTAYGSDHSYGPMGWGPGPQPPYWPAVPPTPLPPPPPPPPPPPPPPLVKSIPLPSQVPDSFSTGIPESVPASSAVSVIPPPSLVPTSQEGPQAALSRAEGKQGPAPQQSLRTLSPRSKPKLATPGSPDARKKGAPVEDPVVQKGQPLPEGPAPQKAQPEAKESEHSESPSVPADSAVSVPKQCQVTKMTPVHPSRLRRLSFLTPPHSQGSEDVVQAFISEIGIEASDLSSLLEQFEKSEVKKECIPLGPADTLALGNSGVDNSQEKRPLDRLQAPELANVAGLTPPATPPHQLWKPLAAVSLLAKPGSPDSPTQDRVLKPVGNIDAQRPAAARLRGRVPGPSPVHVGSGDHDYCILSPTVTTGPELGSRWNVKRHQDITIKPILSLGPSAALPACPAMCQKQQLDHRTSEELEATPPAPTSAPAQQSSVLLSPEASPGRNDDTRTHPGPLAKQPVHCYQKACAPSSPPVRGWAGRSSRSCSNGASEASSSSSSSRSRSRSHSHSRSRSRSRSISPPPKRWRRYRSHCSRSTRSSSRSSCDSWGHSRRRSSSSSSSSSSSSSSSSSSSSSSSSSSSSRSQSRSPSPRRRSNRRRRYDYYDSQDHYQRQKILQKERAIEERRVVFIGKIPGCMTRSELKHRFSVFGEIEECTIHFRFEGDNYGFVTYRYAEEAFAAIESGHKLRRAGEQPFDLCFGGRRQFCKRNYADLDSNWEEFDPAPVKSKFDSVDFDTLLKQAQKNLRR
The following text describes a protein:
Function:
Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTSVIDAAPVKPAFRLTRAFQGLERVVVPALLIAGWEAFARSGMLPPALLPAPSAVLHALGDWVFGFDETTQTYSGHWLRDALASALRVFGGFALASALGILAGVAIGWSRLFEKTLEPTLQMLRPIPPVSWIPLAIIWFGIADKPAIFLVFLGAFFPVLMNSIHGVKTVDHNLVRAGAMMGASQRQMLTDIVLPAALPSIFAGLRIAVGSAWMLTVTAEMVAVKSGLGYVLWDSYYFLRYDIVLAAMISIGLLGYLSDLGLKAIMARTLRWQQTTTVQGRAG
The following text describes a protein:
Function:
NAD-dependent protein deacetylase.
Sequence:
MTSVYESLLSDYPDKGVIGKPEIRDTETEIIEKLRTLYNHFVQAKQTGKPIFVLIGAGVSTGSKLPDFRGKQGVWTLQAEGKHAEGVDFQVARPGVSHKSILALHKAGYIKTIITQNVDGLDRKVGIPVEDLIEVHGNLFLEVCQSCFSEYVREEIVMSVGLCPTGRNCEGNKRTGRSCRGKLRDATLDWDTEISLNHLDRIRKAWKQTSHLLCIGTSLEIIPMGSLPLDAKSKGIKTTTINYQETAHEKIVETAIHADVKLILYSLCNALGVNVDLGDDLPDEVPIPLKIS
The following text describes a protein:
Function:
Ceramide hydroxylase involved in the hydroxylation of sphingolipid-associated very long chain fatty acids. Postulated to hydroxylate the very long chain fatty acid of dihydroceramides and phytoceramides at C-2.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAATSSSSSSKMQLFSVDDVAKHNTATDCWLIHRGNVYNVTDFVEDHPGGDDLIIKYAGKDMGEIMDDPQEHSHSDSAYELLDEYIIGRLPATDAEKHALQQRTAQGGYSGKDDSIVITEDFHPEETDFSSDYKAHKFLDLNKPLMPQMLRANFSKQFYLEQVHSPRHLKHPARFFDQDYLEVFTRTPWYVVPMVWLPIASIIFFRSITQFASNLASTPLNATNWYEAATKPTQFDASVWSIAVTQTAICWAIGVVIWTLLEYTIHRFLFHIDNILPDKPAFLTLHFLLHGVHHFLPMDRLRLVMPPLLFLVLSYPFTQLAHTLFPHAIANGIISGSFSMYVVYDCMHYALHHTKLPEYMREMKKYHLEHHYKNFELGFGVTSKVWDYVFGTQL
The following text describes a protein:
Function:
Catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for the biosynthesis of several classes of glycoprotein.
Sequence:
MVRYDDAGGAAATTPTQLLESLGSFMRRCLFRVLAVGPIPHHFAFIMDGNRRYAKKLNVEEGAGHKEGFSSLISVLKYCYELGVKYVTIYAFSIDNFQRKPAEVQNLMDLLLEKINELLKEQSIVNLYGIRVYFIGNLKFLSEPVRVAAEEVMMATARNSKVVLLVCLAYTSADEIVHAVQESFKNKSDESLAVNANQVSNGVINGAEKVEKIYSLTVPSIEESCKEKASRVCNGAIERVKGTEDINGATVCTDGVSCDYKSEAQALRAGRIGNGVTEGFEEKQGNNPIINLVDVEKHMYMAVAPDPDILMRSSGETRLSNFLLWQTSNCLLDSPAALWPEIGLWHLVWAVLKFQRNHSFLEKKKKQL
The following text describes a protein:
Function:
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Domain:
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence:
MEGGFGSDFGGSGSGKLDPGLIMEQRMTDKCFRKCIGKPGGSLDNSEQKCIAMCMDRYMDAWNTVSRAYNSRLQRERANM
The following text describes a protein:
Function:
Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
Sequence:
MGIWTWTLIALRRESHRLFAVMAGARPGHPRSLAKKDVDARDKRGHGVERSVRCRYSGSMSPKSALKAKSEPSQPETASRPLALLAWYDRHRRHLPWRAASGEASDPYRVWLSEIMLQQTTVKAVGPYFEKFVARWPDVTALGQASQDDVLRMWAGLGYYSRARNLHACAVAVTREHGGVFPDTEERLRALPGIGPYTAAAIAAIAFDRRTMPVDGNIERVVSRLFAVEEELPQSKPLIQQLAATLLADARAGDSAQALMDLGSSICTPKKPACSLCPLNDDCIARAQGTQESFPRKTPKKSGTLRRGAAFVVTRGDELLVRSRPEKGLLGGMTEVPGSDWLAGQEDATAKQQAPALKGLSRWQRRVGVVTHVFTHFPLELVVYTAKAEARTRAPAGMRWVPIATLPGEALPNVMRKVIAHGLRLPPAPSS
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MGNSLQRPTENRGRQEEEGNGSSFTCEICIEPMAANKKFKNKNLCTHPFCQECIAKYIQVMVQDNNTAKIECPGLNCQKNLDPFSCKPMIPSSLFSKWCDLLCEDYVRGYERSYCPNRNCMALVVNECERKGRMKKAQCPNCKHWFCFRCKLKWHGGYHCEESGNLRDRNDIAFGQLAERMKWARCPGCGHCVQRKNGCHVMQDSVLL
The following text describes a protein:
Function:
Effects nucleoid occlusion by binding relatively nonspecifically to DNA and preventing the assembly of the division machinery in the vicinity of the nucleoid, especially under conditions that disturb the cell cycle. It helps to coordinate cell division and chromosome segregation by preventing the formation of the Z ring through the nucleoid, which would cause chromosome breakage.
Subcellular Localization:
Cytoplasm, nucleoid.
Sequence:
MKHSFSRFFGLGEKEQEPEIAEHDTNKEEILEIPVNAIVPNRFQPRTIFSDEKIKELAMTIHTHGIIQPIVVRHTEEEGQYELIAGERRWRAVQSLEWEKIPAIIKDFSDTETASVALIENLQREELSSIEEAHAYARLLELHDLTQEALAQRLGKGQSTIANKLRLLKLPQPVQEAIMEKKITERHARALIPLKQPELQVTLLTEIIEKSLNVKQTEDRVVKMLEQGQRKPKPRRKAFSRDTRIAMNTIRQSLSMVEDSGVKLNTEEEEFEEYIQLTIRIPK
The following text describes a protein:
Function:
A humoral factor that may play a role in stress tolerance.
Subcellular Localization:
Secreted.
Sequence:
MGLSIGSLLICVFLGIVPFATANTNSSSYEEHRNYLLNIFHNPFVNDSIKEKNIPQLIAFYQRYPTDVPLSDADRQQFERFIHDYREYRAVLVDGAPPQGGSFGNIFGHFLGRVGTRYISSLFNKKREERKSNHAYIIEDYN
The following text describes a protein:
Function:
Gamma subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain. GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s). When activated by GABA, GABAARs selectively allow the flow of chloride across the cell membrane down their electrochemical gradient.
Subcellular Localization:
Postsynaptic cell membrane; Multi-pass membrane protein.
Sequence:
MAPELLLLLCLSWGVHARSRKVEEDEYEDSSSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDEHSCPLIFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTALGITTVLTMTTLSTIARNSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTTTKKKTSLLHPDSSRWIHERISLQAPSNYSLLDMRPPPPAMITLNNSVYWQELEDTCVYECLDGKDCQSFFCCYEECKSGSWRKGRIHIDILELDSYSRVFFPTSFLLFNLVYWVGYLYL
The following text describes a protein:
Function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MWSWLLHRITGVILVVGLLYHFILMHFMGHDNYSYNAVMQRLSEPSWKIFNIVFLFSALYHGFYGLNGVVTEYVRNNSLKRILKFMAFTVPIGLAFYGFKIVFF
The following text describes a protein:
Function:
Transcription factor involved in the regulation of seed size. Possesses transactivation activity in yeast.
Subcellular Localization:
Nucleus. Cytoplasm.
Domain:
The NAC domain includes a DNA binding domain and a dimerization domain.
Sequence:
MAMTPQLAFSRMPPGFRFQPTDEQLVVDYLQRRTAAQPCVTPDITDIDVYNVDPWQLPAMAMYGSDHDRYFFTMAAREAQARRTTPSGFWKPTGTKKTIFVVAGGHEVPTAVKRRFVFYLGHHQPSGSSNNNKTSWIMHEYRLMNSPRAAVPSSSSVNRLPTDDLTEEMVLCRISNKDLPKPPFIHNGLLQFSSVGLNGDGYNYLILDHLEPPAMEYPNVDIGNVDDAAAADDDPGDLDEEIDDSMQRNHGG
The following text describes a protein:
Function:
Plays a role in development of both male and female reproductive tissues.
Subcellular Localization:
Nucleus.
Domain:
The cysteine-rich domain CRC binds zinc in vitro.
Sequence:
MDTPDKNRISAVSFCNFEDSPVFQYINDLSPIEPVKPGRPENILHSLVFTSPSSSSSLFCSPQLNSYRDSRFFIKRHRSLDLSSPVVLIGETLKNSPDALWEEKLKCRPEKLENVSEPKPFKEQISLAIELANSLKHGRDGCDIQMVSCDEVPMDADDEIGSGGGSRELSDELCRQSFDPLDFDADSDGVLHTDEMEAESGFGKEVIMFDVADIQNYEQQIPRTTDPRFYSLASEPQQFSIYCNNSNYVEEREGSCSVQVAAGAPDINLSCSSKVAAIDSTAEAEDKEDKDLQPSGKQRSVRRRCLTFDMGGSHKRIPLRDSTNDLPLDSTSINKAPSPQNCLDTSKQDTDEILPIPRTIGLHLNGFVNPSVSSGRKKKKIKDGQAFPSTTFHYNIEDEFSTPVSTKRDLVVFSDVKIMEPPERSVEGECFDQLMAMENRQLSQGLDELGSCKRCKCRKSQCLKLYCECFSAGLFCGEPCSCQNCFNKPIHEDLVMKSREVIKARNPLAFAPKVVSTSDTVIDLWVENSKTPASARHKRGCNCRKSGCSKKYCECFMMGVGCSSNCRCMGCKNTFGHTNEQCAGDSDVVTINDEAKHYGDHGDASRQNEEILTSERNRLLLPGSVAFRSLTSLSNLSEL
The following text describes a protein:
Function:
Transcriptional repressor. Together with PHD finger-containing proteins (e.g. PHD1, PAIPP2/PHD2, AIPP2/PHD3, PHD4, PHD5 and PHD6), cooperates to form a BAH-PHD bivalent histone reader complex able to read histone H3 lysine 27 trimethylation (H3K27me3) and low-methylated H3K4 histone marks in order to regulate transcription, especially to prevent early flowering; H3K27me3 reader of this complex. CPL2 is subsequently recruited to form a BAH-PHD-CPL2 complex (BPC) in order to silence several H3K27me3 and low-methylated H3K4 enriched loci, including AGO5, via the phosphorylation state-dependent inhibition of Pol II release from the transcriptional start site (e.g. Ser5P-Pol II dephosphorylation). The BPC complex represses flowering by inhibiting the expression of several genes, including AGL6, FT, FUL and SOC1. Prevents the accumulation of intronic heterochromatin-containing genes (e.g. IBM1, At3g05410 and RPP7). Seems to not be involved in vernalization establishment, by contrast to orthologs in grass plants.
Subcellular Localization:
Nucleus.
Domain:
The BAH domain (129-248) recognizes specifically histone H3 lysine 27 trimethylation (H3K27me3) hallmarks, binding affinity being proportional to H3K27 methylation level.
Sequence:
MVLSRRFAQVSSDEEDDVPITRSKGRNSASPEESLGKRRKRKTVKLYEDFEEKEADRKKKRKGNKEDEDMAEGDDDQAEEETNPEAEEEEDEEEEEKPDDACPVGDSVNVTGKGKGKRTHFNQFAYDGNTYDLEVPVLLVPEDKSQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKRGGGNWQSSDTRELFYSFHRDEVPAESVMHRCVVYFVPAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLTDKDYEDSKQREIDVLVKKTMNVLGDLPDLESEDMLVDQENVLKAKRSFRKVNISPVDVRREEDASLKAETPGSGAGISSEHYAILEKFDSLTGDAHRDKCLGKLLEAVQHICYIPENKQAGDEAKVGSDASHLEQDEKDTKPENGKDEKFLWPDAAVPQVCALENASHASLASDFQKYNQKMRTLVFNLKNTALLARRLLNGELEPATILNMSPTELKEGLTADETTKKEPDDADRMQMTSVRCSRCSQLTVGLRDIIQAGHGDRYQLECVDCGYSWYASRDEVSTLTIVTDKPAQGTEKEDIEKNLTSPRETNKPKDEALKTNDSNADNNPEASKKPE
The following text describes a protein:
Function:
Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs (acp3U(20)).
Subcellular Localization:
Nucleus.
Sequence:
MKRARKVYSDDDEERCKKVVDFIRSLRFSIPLYRLREQNDRRLCPKCGRRRQYYCYDCLIVVHPESQPPPLKLPLNVYVILHPGETRGKSTSLAASTISPDLHIIDYPHVPTDLEPKATLLLYPSTDSTELESLENLDSCKNVVFIDGTWQQSKAMARDERLSKFRHVRIKAQTSLFWRFQNNDPTYLATVEAIYYFLREFISQNNKRRAGCQPPYYNGDVDDILYYYINQYIAVQQRYCKSELEYTTRHFDSYIIRCFSWDQLVAKPSESAPVVNHRTS
The following text describes a protein:
Function:
Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MAQEPNPFKHVTFMDTNCAAKAAMVTVAGGAMGFLMALFMNAVEMRDMDYGRTKQSTRYVLRRDINKMFGMAKGFAIFGAFYSIFECQLEKLRIRDDATNSFLSCMFSSMVLAAESVGWKGLMMSGLGGGMFGGVIL
The following text describes a protein:
Function:
Forms chloride channels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane.
Sequence:
MVPTASTMNNKALLQARQTRDKRLMSNSTTSARVAQALQSRGNEVIYNIETETDPLSDSSRKAEENNNNNTGDPASAKGGEKQQTAAVEATVIEVDKNIKNGSPATNEQPANEAYRPTILKQYLVPLWILLAYLAAFGLSRAFYNLALSYDDKMAFDMWAAYFNSLPSNLNTIWFLGMVLNQMLSKRTTATIQNVLPGTTHVMELFERALKKGIPERHQHVERFSRYILLMWLMTARQFSKPLEMEYSSWAKIQETLGLNDAEIKSLQRKEKKGEPLALVAYDWSKVFLAEMDDKKFLTSPGEVAQMYQTVYLLKKNCGTAMKFSNRELVPRIMLWISWAVLHLFGWISVLGLQTEIEWEGKSEKWYFPSQFSLPYFLVCFAYAASQIVSHPFDNNEDEDMVQTLNQKIENRKRFLRVYDKKCVEDLIME
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Sequence:
MKESMDDMEEDMGTSSKGEKLPNEFDMEIDFDGDDDEDDGEFMDLTSLGDLGEGFLEDFCKKAATLFFNEYGLISHQINSYNDFIHNGLQMAFDSFDDLVVEPGYDPSKKGENEWRYASVRFGKVTVDRPSFWAGSDGGEHNMFPRHARLQNMTYSARMKVNVTVEVYTQKVVSSDEFRTGKDHFVDKVVLSTDSRDIIIGRMPVMVKSDLCWMQTVEKGDCDFDHGGYFLIKGAEKVLIAQEQSCLKRLWISNTQGWTVAYKSEVKRNRLIVRLEPVGPSKDENLKEGKKGLTVYFLSTEIPLWILFFALGIKSDKEVIDLIDYNMEDASIMNIIFGSIHDADDKCEGFRKERNALDYLVKQIQGTKFPPGEDEDCISLYLFPTLHSPRQKARFLGYMVKCLLQAYSGKRKCDNRDSFRNKRFELAAELLDRELKVHIAHARRRMSKVLQKDLYGDRDVRPIEHYLDASIVTNGLSRAFSSGAWSHPFKRMERISGVVANLGRTNPLQTMVDLRKTRQQVLYTGKVGGARYPHPSHWGRVCFLSTPDGENCGLVKNLAATGLVSTNISEPLIDILFDCGMEKIVDDAHTKLNGKHIVFLNGEWVGVCEDSHLFVTELRRLRRRKRLPQQVEIKRDDQQREIRIFSDAGRILRPLLVVENLTKIKAFKGGNYTFQSLLDKGIIEFVGTEEEEDCNTAWSVKLLLAGADGKQPVQYTHCELDMSFLLGLSCGIIPFANHDHARRVLYQAQKHCQQAIGFYTTNPNIRVDTVSHQLHYPQRPLFRTVTSDCLGKSRHQRGYNGMLPKPELYNGQNAIVAVNVHLGYNQEDSLVMNRSSLERGLFRSEHSRSYKADVDNKELLDKWRKFDDTINFGKVQSKFGRVDSLDDDGFPFIGANLQSGDIVIGRCAESGADHSIKLKHTERGMVQKVVLSSNDEGKNFAVVSLRQVRSPSLGDKFSSMHGQKGVLGFLESQENFPFTRQGIVPDIVINPHAFPSRQTPGQLLEAALGKGIACGGSMRYATPFSTLSVEAITNQLHRAGFSRWGNEKVCDGRTGEMVHSLIFMGPTFYQRLIHMAEDKVKFRNTGPVHPLTRQPVADRKRFGGIKFGEMERDCLIAHGASGNLHERLFTLSDSSQMHVCQSCKNVANVIQRGVRGGHKIRGPYCRICESADDIVKVNVPYGAKLLYQELFSMGINLKFETQLC
The following text describes a protein:
Function:
Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Sequence:
MKTHFITFLLLVGMSLGISSRLHAQSSYQPGEENLKAREEFQDNKFGIFLHWGLYAMLATGEWTMTNNNLNYKEYAKLAGGFYPSKFDADKWVAAIKASGAKYICLTSRHHDGFSMFDTQYSDFNIVKATPFKRDIIKELAAACSKQGIKLHFYYSHLDWTREDYPWGRTGRGTGRSNPQGDWKSYYQFMNNQLTELLTNYGPVGAIWFDGWWDQDGNPGFNWELPEQYAMIHKLQPGCLIGNNHHQTPFAGEDIQIFERDLPGENTAGLSGQSVSHLPLETCETMNGMWGYKITDQNYKSTKTLIHYLVKAAGKNANLLMNIGPQPDGELPEVAVQRLKEMGEWMNQYGETIYGTRGGAVAPHDWGVTTQKGNKLYVHILNLQDKALFLPLADKKVKKAVLFKNGTPVRFTKNKEGVLLEFTEIPKDIDYVVELTID
The following text describes a protein:
Function:
Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5-trisphosphate. Necessary for proper organization of the trans-Golgi network (TGN) and post-Golgi secretion in root hairs. Together with PI4KB2, required during polarized root hair expansion and pollen tube elongation. Functions redundantly with PI4KB2 upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway.
Subcellular Localization:
Cell membrane. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Associated to tip-localized membranes in growing root hairs.
Domain:
The PPC (Plant PI4K Charged) region is involved in membrane targeting and phospholipid binding.
Sequence:
MPMGRFLSLVRGDSAESPREITSQSNIIGDTGSNGWLIRFFDSAFFCEWIAVSYLYKHPHAGVRDYLCNRMYTLPLSGIESYLFQICYMMVHKPSPSLDKFVIDICGKSLKIALKVHWFLLAELEDADDNEGISRIQEKCQIAATLMGEWSPLMRPQNEVSTPGSKNQVLNRLLSSKQKLFSLKLSPPTQKSLSFSPSPGTNVQDDGSQLPAEDNKIFKKLIPSPKVRDALMFRKSADKDDEESEKEGFFKRLLRDSKGEGDEPIPNSEGFFKRLLKDNKSEDEDITNSSEGFFKRLLSSKGESEELTSSSDGLFKRLLRDNKGDEEELGANSDSFFKRLLRESKNEDEESNPNSEGFFKKLFRDSKPEDDKVPKEVDDEDKDGFLKKLFREKNDDKRHGSEKNEANGTVYADKKSGEEDEREGFFKKFFKEKSDDKKDIVKVDDGNESEGDESPEFSLFKRLFRIHPEDAKPTSENENSSNGLVESSPGTENFFRKLFRDRDQSVEDSELFGSKKHKEKRPGSPKQRDDTPSGKPPLPNNTASQFRKGAYHESLEFVQALCETSYGLVDIFPIEDRKIGLRESLAEINFHLSEAEITGGICFPMGRGVFRVVHIPEDECILLNSREKAPYMISVEVLKAETPSAKESSNSQKLSKGGIPLANGDAFLQKPPPWAYPLWTTQEVYRNSADRMSLSTAQAIDQAMTPKSEVKVKLVNVSLSVEDRTSALESFGDPIDDVLGEAPRTGLNNDLEWVRVVVTADPGLRMESIPDPSVPRKKEHRRVPSTVAMEEVRAAAAKGEAPPGLPLKGAGQDSSDAQPRANGGMLKEGDALSGELWEGKRDRIRKASIYGKLPGWDLRSIIVKSGDDCRQEHLAVQLISHFYDIFQEAGLPLWLRPYEVLVTSSYTALIETIPDTASIHSIKSRYPNITSLRDFFVAKYKENSPSFKLAQRNFVESMAGYSLVCYLLQVKDRHNGNLLLDEEGHIIHIDFGFMLSNSPGGVNFESAPFKLTRELLEVMDSDADGVPSEFFDYFKVLCIQGFLTCRKHAERIILLVEMLQDSGFPCFKGGPRTIQNLRKRFHLSLTEEQCVSLVLSLISSSLDAWRTRQYDYYQRVLNGIL
The following text describes a protein:
Function:
Probably plays a role in ammonia secretion that neutralizes the medium at pH 5.5, although it does not play a direct role in ammonia transport. The OmpA-like domain (196-326) binds M.tuberculosis peptidoglycan. Overexpression in M.bovis or M.smegmatis gives channels with average conductance value of 1,600 +/- 100 pS, but this may not be physiologically relevant.
Subcellular Localization:
Secreted, cell wall. Cell outer membrane. Note=Does not have a cleavable signal sequence.
Sequence:
MASKAGLGQTPATTDARRTQKFYRGSPGRPWLIGAVVIPLLIAAIGYGAFERPQSVTGPTGVLPTLTPTSTRGASALSLSLLSISRSGNTVTLIGDFPDEAAKAALMTALNGLLAPGVNVIDQIHVDPVVRSLDFSSAEPVFTASVPIPDFGLKVERDTVTLTGTAPSSEHKDAVKRAATSTWPDMKIVNNIEVTGQAPPGPPASGPCADLQSAINAVTGGPIAFGNDGASLIPADYEILNRVADKLKACPDARVTINGYTDNTGSEGINIPLSAQRAKIVADYLVARGVAGDHIATVGLGSVNPIASNATPEGRAKNRRVEIVVN
The following text describes a protein:
Function:
Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.
Subcellular Localization:
Membrane.
Sequence:
MQFKSLLLIAGATILSPFLVEAQTWTICNPLNQTCPNDPALGTNHTFYFNTSSTVTDYYNITAGTLAYGNDGAEFTIAKQGQSPTIQSKFFIFFGQVSVVMKAATGVGIVSSIVLESDDLDEVDWEFIGGNNTHAETNYFGKGNTTAYDRAIWYPTPSDPTANFHNYTVDWTAERIQWWIDDSLVRTLAYADALGGKNFPQTPMTVRLGIWSGGDPKGNSEGTIEWAGGVTDFSKTPFTMYVKSAAIQDYSTGSEYQWTDKTGDWQSIKVISGNSTVAKAITENATPKLTLSEKWHRLSKGVKLTIYCLCGAVAAALISLFLFTFFRQRRNGRLEREAYNQLIEKQQQDNQIEMNNKGFGGFDDASGGLGDDHGTGYVGPVGSASANALATGSPVVQAGQHGPRSPTMVEHSGEMSPQTAEFPQQPRFGSTTNGGSYVKM