lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. Upon vesicle tethering to the target membrane, which requires additional proteins, a SNARE-pin is formed. This is a very stable 4 parallel alpha-helical coil bundle consisting of 4 SNARE domains (usually one of each type: Qa, Qb, Qc, and R), of which at least one is anchored in the opposite membrane. The formation of the SNARE-pin is believed to bring the two membranes in close proximity and to provide the energy to drive membrane fusion. Through its interaction with the VFT (or GARP) complex, it may also contribute to vesicle recognition specificity and tethering. Regulation of SNARE-pin formation also seems to depend on the phosphorylation state of the protein, phosphorylation by TPK1 causing inhibition and dephosphorylation by SIT4 activation.
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein. Early endosome membrane; Single-pass type IV membrane protein. Late endosome membrane; Single-pass type IV membrane protein. Note=Probably shuttling between TGN and early/late endosome.
Sequence:
MNNSEDPFQQVVKDTKEQLNRINNYITRHNTAGDDDQEEEIQDILKDVEETIVDLDRSIIVMKRDENEDVSGREAQVKNIKQQLDALKLRFDRRIQESTQTTIPLEETVENSTLNTSMAENNDGGMSNPFQEQMLREQDVHLDGIHKTMQNLHIQAQTMGDELENQGQLLDNMDEGMDGVVNKLARGRRQLEWVYEKNKEKYDDCCIGLLIVVLIVLLVLAFIA
The following text describes a protein:
Function:
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular Localization:
Secreted, cell wall.
Sequence:
MASMAASVVFILLISTLLNAASVMPESHFKSYPHWRHDHKQHHQKDVAPGSGTSVAVTEACAATRYPASCLRALNSDPRSATAVPRELVAIAIGVAHRYATISQADSQTLAAQSATSGNINLISISKMCSEGTDLAAFHTQNSENAVNGPLLNDVQAWLSGALTFTTDCSAGLGQTSTALPFVSEMKGRLDASQEMISNALAMTDALVNYGPNTVLWKPPPLSKDHMLYETTSFVAQHELSAAVSTPKWLNVKDHNLLNGTLLASPSVTVDIYSAFSSIQRAVDLAPDWSTQRYVIYIKTGVYNEVVRIPKQKTNLMFLGDGTDKTIITGSLSDSQPGMITWATATVAVSGSGFIARGITFQNTAGPAGRQAVALRVNSDQSAFQNCAVVGFQDSLYTHSLRQFYKDVYVSGTVDFIFGNSAALFQNSQLVVRVGAPEATTSTVTAQGRTDSGQTTGLVFQDCSILGTPEYVALFQSNRQAHQAFLGRPWKTFSRTVFIRTYIDQIIDPSGWLPWNGNFALSTLFAAEYGTYGPGAATINNRVTWSSQLSTSQAQAFSVSSFIQGPSWLPATEIPFSP
The following text describes a protein:
Function:
Essential negative regulator of type I and type II interferon (IFN) signaling, as well as that of other cytokines, including IL2, IL4, IL6 and leukemia inhibitory factor (LIF). Downregulates cytokine signaling by inhibiting the JAK/STAT signaling pathway. Acts by binding to JAK proteins and to IFNGR1 and inhibiting their kinase activity. In vitro, suppresses Tec protein-tyrosine activity. Regulates IFN-gamma (IFNG)-mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular Localization:
Cytoplasmic vesicle. Nucleus.
Sequence:
MVAHSKVAADNAVATDARRRPDPSPSPPPITPVATRAGRPGPDARPRRPPAGASRHGAPAAPAAGGAAAPGPGDTHFRTFRSQADYCSITRASALLDACGFYWGPLSVNVAHEKLRDEPVGTFLVRDSRQKNCFFAISVKTATGPTSIRVNFQAGRFNLDGSGETFDCLFKLLEHYLSSPRKVLVTPLRRVRLRPLQELCRKSIVATFGRDNLGAVPLNPVLKDYLRSFPFKI
The following text describes a protein:
Function:
Mitochondrial aminoacyl-tRNA synthetase that catalyzes the attachment of tryptophan to tRNA(Trp).
Miscellaneous:
MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MSNKQAVLKLISKRWISTVQRADFKLNSEALHSNATVFSMIQPTGCFHLGNYLGATRVWTDLCELKQPGQELIFGVADLHAITVPKPDGEMFRKFRHEAVASILAVGVDPEKASVIYQSAIPQHSELHWLLSTLASMGLLNRMTQWKSKSNIKQSTNGDYLVNDSDVGKVRLGLFSYPVLQAADILLYKSTHVPVGDDQSQHLELTRHLAEKFNKMYKKNFFPKPVTMLAQTKKVLSLSTPEKKMSKSDPNHDSVIFLNDEPKAIQKKIRKALTDSISDRFYYDPVERPGVSNLINIVSGIQRKSIEDVVEDVSRFNNYRDFKDYVSEVIIEELKGPRTEFEKYINEPTYLHSVVESGMRKAREKAAKNLADIHKIMGF
The following text describes a protein:
Function:
Contributes to transmembrane potassium transport.
Miscellaneous:
MISCELLANEOUS: In the Saccharomyces cerevisiae heterologous expression system, localizes to the intracellular membranes of the yeast cells.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MKSGLFSMNDIFFLVNSIFKYFLILLNGSHLLKLLYSSKENIHIIEGLLCIITGVILKLSLIYIYCTYFMNIYIIKDYRRKNVLNIFNMNNNYKRNGNVIESDDFEYRKLIKKFFFKKVYYSIKKKHKRIELYMLKIYNSNFNYYFCNIRDMCYTIIWYISLYYWRRDTYNMIWGFNKIPTYIYNMLLILLSTSYIDLVMVIISYNKSKYYLMKSKLLIDIFFSAPCTYLFSKFIFVFEHQIDIYFMMGFLRNIKIFLNVSYVRIEHNSILTNTEIKIIRIVLGVLLLCNAFASTIYTIQAIHPYNLDNENFNYFLNSYLDYFYFSIISISTVGYGDIFPINKLSKVVCIIFIFWTFIWVPIQFNDLIISIFSKKKTYGKISMNNQKFILLIGDVEPQQLNVFLFESVAQGNKLKFHLLTTYPINIYDEQIKIADHFCISLYIKNFDLNEKENINLLYSINAQNAYYLFLFSNKFHNGHYNIDTKSFTRLLILKKFLHGKKNAVIELRSNCVSNIVRSIGCENFIIVNLKHSLIVKNIKYPGFITLILNLFTAYNYDISSYNFNDIASYPSLKYIGEFNRGSRTKIFSFIVHKNMVGLIFDKLFYKLYESLGIILVGIETNTTNYYINNKKHKNKNSYVDDNFTTMRKNNMKNKKKKSFKFIYLHLLKKYGHTNHYTQKKKKKKYDNIINHHGSKSKMEYSTQLRHNNKTIKIYDEYNTIETYQNYLNYETINNSRINIYNSDEKKKKYNDVSPTNNILTNYKNGKLHIEKRDDFDNNNNNNNNNIVKSRKKGRENKNDEIINVCININSDIKKKYNNNNNNNNNNDNDNNNIINDHDNYNIYNNLNSNLKCRCLPNTKKNKAQNVNNVTNNKDNDVSVKRIKTHLQDDNTIDNKKELKCYLNLLGKNYAIRDSDKCVVIANSRKVIKYLSKAKSLFWIFEIKSKKKDNISYDLKSVIKTKQTFNKYFTTNIKKKLPTTSIQNNVYVNKNAHIIAMNYHDLFNTYRISRIFTKNNYNYKRKNSRKKHLFRNLNGEFNETKLYHHCNNTHNIKTTDKKNMEKLDKLYFSTKLNSKSNTNIHIHNNNNNNNNNNEHYDDEIKTYYFNLTEKNSHLLLNYKKQLKKKNYINTCYSVNKSDESINKIKNMNSDNNNINSNNINSNINNNNNNNTKLNHTLKNRITFSYMEACEKYFPTENRNNKLLLIINCTCNIIQLIKMFNNKYKYNVIILTDEIPTMNIMDLFKYNVVFIKCKILDDYNLINSGLMNAEYILILPTEAKNINEINEIDMNTIIVTRKITHLLKKKKRTYYINNIITELINPSNVIFLEENKMIKLKDKKSSYDDFFPYVNSSQFYSSNIICETMLYNFMTHHKSFTDFSVCTNTLECLIKFLRIIYICDLSKYYDFSFKKIKTFRDLFYFLSKKNIITIGLYRKGDKKVPFYIYTKPNENCLLRFDDIVYIL
The following text describes a protein:
Function:
Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Microsome membrane; Single-pass membrane protein; Cytoplasmic side.
Sequence:
MVGSSEAGGEAWRGRYYRLEEVQKHNNSQSTWIIVHHRIYDITKFLDEHPGGEEVLREQAGGDATENFEDVGHSTDARALSETFIIGELHPDDRPKLQKPAETLITTVQSNSSSWSNWVIPAIAAIIVALMYRSYMSE
The following text describes a protein:
Function:
Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1. Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production.
Sequence:
MKNLRSPCFLFIFLLFSMLCALVTSSQRDYYTILGVGRTATTKEIKSAFRKLALKYHPDKNKEPDAEAKFRDIAEAYQVLSDKQKRQRYDQYGDDGLNDNMGGSSDGGNFHDHFRSHFNMHDFFKDFDDMFHEHKKHHKRPNMFTDFQSDDSASFFPELVIVEHEWSNYIDSFHFQNMEGSHSHQTFTSSKRKAIPYTTLFYLGSRQNCKTVTKTVNGVTTTYTTCTND
The following text describes a protein:
Function:
Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MESEQLFNRGYGRNSYNSITSASSDEELLDGAGVIMDFHTTEDDNLLDGDASPGSNYAMSNGGGGGGGASSSTHLLDLLEEPIPGVGTYDDFHTIDWVREKCKDRERHRKINSKKKESAWEFTKSLYDAWSGWLVVTLTGLASGALAGGIDIAADWMNDLKEGVCLSAMWFNHEQCCWGSNKTTFAERDKCPQWKTWAELILGQEQGPGSYIMNYFMFTFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNTSELIKELFTDCGPLESSQLCQYRSLMNGSQADPTGPDTASAATPGVYSAMWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDWFVFREWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAREVMRPRRSDPPLAVLTQDDMTLAELQGIISETSYNGFPVIVSKESQRLVGFALRRDITIAIENARRKQEGIVLNSRVYFTQHAPTLPADSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEHLEEIKQHVEPLTPPWYYYKKRYPPSYGPDGKPRPRVHNVQLAPSSSHYQEDEIEEEVRLLDNSSL
The following text describes a protein:
Function:
With S4 and S12 plays an important role in translational accuracy; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Domain:
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Sequence:
MEEINREEFQEVVVNIGRVTKVVKGGRRFRFNALVVVGNKNGLVGFGLGKAKEVPDAIKKAVDDAFKNLIHVTIKGTTIAHDIEHKYNASRILLKPASEGTGVIAGGSTRPIVELAGIKDILTKSLGSNNPYNVVRATFDALAKIKA
The following text describes a protein:
Function:
Plays a role in L-cysteine detoxification. Binds to the dlsT(yhaO)-yhaM operon promoter in the presence but not absence of L-cysteine; activates transcription from the dlsT(yhaO)-yhaM operon. No other DNA target was identified in strain K12 / BW25113. Thiosulfate does not activate its transcription function. Overexpression doubles hydrogen sulfide production in the presence of cysteine.
Sequence:
MLDKIDRKLLALLQQDCTLSLQALAEAVNLTTTPCWKRLKRLEDDGILIGKVALLDPEKIGLGLTAFVLIKTQHHSSEWYCRFVTVVTEMPEVLGFWRMAGEYDYLMRVQVADMKRYDEFYKRLVNSVPGLSDVTSSFAMEQIKYTTSLPIE
The following text describes a protein:
Function:
Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin.
Sequence:
MSEFPLVSPNVDSDRPPLGAAPRFFLGESNFSVYEEMARQLKEMGWCEVRSKGWLPTCDVILGDRFTIPYPLLRCECLPPTSRYSGSRWLNYFRGSHRLTLKASMARLLQKADSTCGEWMPRSYVLGGDQERRKDDREAFLEHAVRDPTQVWIIKPSSGCKGKDIVLTRSVAELEVFISELDPKCRRIYLVQQYVQRPLLYRGRKFDMRVWALLKSPYTIYAFTKGSCRTSSSPYDPDDIEDYLVHLTNHCLQEDAPEFGQYEEGNELWFEEVGAYLHEVYRKRVLEDRILPQIASIIIRTLLAARAELQVLENEPYQCFQLFGYDVIVDEGLSVMLLEINGSPGVASKYLQPLVREIIKLVDGGEALNEWDVDAVGFVKLWAEGDELPIGST
The following text describes a protein:
Function:
Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta; May play an integral structural role in elastic-fiber architectural organization and/or assembly.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MAMLVWDIIVSVTLLISPAFLSADQSGFRKLYVVQPGPSGTDGVHVSSISSLSGASGQPHSYNVELKASFGGQVRTRRMGHQQNPSIPIRQDAQSGRHTSSHHMKVSGVNVCGGQCCVGWSKTPGSQRCTKPNCTPPCKNGGMCLGPHMCVCKPGSKGKSCEQTTLPPSSHPTGPLNGHTNGGVPNGGHTNGYSNGHNVIPQRPIPQQIFPQGQGQVPLPLPGTNVGHLTLSMKPSVNGPIPYQPQIQNPVSMTMHQSKSQKFLVQQKNYHTHTQMQGVGPTLNRAIPLSVGHNPIHVGNHTGRIKVVFTPTICKMTCTNGRCQNSCQKGNTTTIISENGHATDTLTAPNFRVVVCHLPCMNGGKCSARDKCQCPPNFTGKFCQMASPNGHQGQHTVVNGQKTHVHSTHTLPLTYGTGQNQGMVNVHVKHPPEASVQIHQVSPVDSNGQVKNTQSSHSFTYHSSSQSIQHGHTHSGVIYPNQQTYLQYQPVTSKSQLGRCFQETTGMQCGKALPGLSKQDACCGTVGTSWGFHKCQKCPKKPSIPLIECPQGYKRLNGTRCIDIDECQLQGVCPNGNCINTVGSYRCICNPGFVPDPSLTSCFPETPALREEKGACFRFVGSGKQCLHPVSTQLSKQLCCCSVGKAWGPHCDRCPLPGTAAFKDICPGGMGYHVTPPYIYKPKPPNGHTQTDSQGYNNPTIRHQVPMDPPVPFPTLQQPVEALSITERQLPEVVEKVSPPAPVAIPPSNEGQDITPTQLAEIDECVVRPDICGAGICYNTAESYTCFCDDGYRTDSEGTTCVDVDECAENPSLCANGRCQNTPGGFLCVCELGFMPNERGSSCSDIDECQNRRACPSGLCYNTLGSFMCSPCPDGFEGKNGQCVDINECLDKRVCAHGQCSNLEGYFVCTCDEGFLPTPDGKSCTDIDECQDDNVCIQGHCQNTQGSFICNCEPGFKLSSSGDQCEDVDECLVIPQTCDGVGQCVNILGSYQCNCPQGYRQVNSTSCLDVDECEDDTQLCIPNGECLNTEGSFLCVCDAGFVSTRTGCQDVDECSLNENTCGSHGTCQNTIGSFICQCDPGFKDSQDGQGCVDVNECELLGNVCGEATCENREGTFLCLCPDDLQEFDPMLGKCISTPPVTTVERKECYFNLNDENLCDKVLASSMTKEECCCTLGAGWGDNCEVHPCPIPGTDQFSQMCPAGRGYLISGDPMSTTSSLAENTKADADECQLFGSEICKDGFCLNTAGWYECYCKSGLYYDESKLQCLDTDECQDEAKCRDGECMNTYGSYQCFCTPPMVLAMDNTHCILPDVAGQSEADLYSGVCWERVTENFSCANPIPNIHTSFTECCCLYGEAWGNDCALCPGKNTDSYAQMCNIRRPYGRDALVAGPIGVSPDYNPQPLNPDGTLPYIEDYDEPRNPYDAFEGLRAEECGVLNGCENGRCVRVQEGYTCDCFDGYTLDMSRMACVDINECSELNAKMSLCKNGNCINTQGSYKCVCLPGFILSAQHNYCVPHRQNATSTGTE
The following text describes a protein:
Function:
Ser/Thr-protein kinase involved in the mitotic exit network (MEN) and required after the metaphase to anaphase cell cycle transition. Phosphorylates CHS2 to regulate its dynamics and chitin synthesis at the division site during cytokinesis. Coordinates septin and actomyosin ring (AMR) functions during cytokinesis through the phosphorylation of HOF1. In complex with MOB1, phosphorylates CDC14 at sites adjacent to its nuclear localization sequence, thereby retaining CDC14 in the cytoplasm. Also binds to SWI5 and CLB2 mRNAs cotranscriptionally to regulate their decay. In the nucleus, the DBF2-MOB1 complex regulates passenger protein localization during anaphase. Mediates sorbic acid stress tolerance through promoting vacuolar H(+)-ATPase function, probably through phosphorylation of VMA1 and VMA2 subunits.
Miscellaneous:
MISCELLANEOUS: Present with 3500 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Bud neck. Nucleus. Note=Localizes on spindle ole body (SPB) for much of the cell cycle and migrates from there to the bud neck in late mitosis. SPB localization during anaphase coincides with activation kinase activity and depends on TEM1 and CDC15. In absence of BUB2, localizes to SPB in cell cycle stages other than anaphase and telophase.
Sequence:
MLSKSEKNVDLLAGNMSNLSFDGHGTPGGTGLFPNQNITKRRTRPAGINDSPSPVKPSFFPYEDTSNMDIDEVSQPDMDVSNSPKKLPPKFYERATSNKTQRVVSVCKMYFLEHYCDMFDYVISRRQRTKQVLEYLQQQSQLPNSDQIKLNEEWSSYLQREHQVLRKRRLKPKNRDFEMITQVGQGGYGQVYLARKKDTKEVCALKILNKKLLFKLNETKHVLTERDILTTTRSEWLVKLLYAFQDLQSLYLAMEFVPGGDFRTLLINTRCLKSGHARFYISEMFCAVNALHDLGYTHRDLKPENFLIDAKGHIKLTDFGLAAGTISNERIESMKIRLEKIKDLEFPAFTEKSIEDRRKMYNQLREKEINYANSMVGSPDYMALEVLEGKKYDFTVDYWSLGCMLFESLVGYTPFSGSSTNETYDNLRRWKQTLRRPRQSDGRAAFSDRTWDLITRLIADPINRLRSFEHVKRMSYFADINFSTLRSMIPPFTPQLDSETDAGYFDDFTSEADMAKYADVFKRQDKLTAMVDDSAVSSKLVGFTFRHRNGKQGSSGILFNGLEHSDPFSTFY
The following text describes a protein:
Function:
Controls the rotational direction of flagella during chemotaxis.
Subcellular Localization:
Cell inner membrane. Cell membrane; Single-pass membrane protein.
Sequence:
MTDASASLDTKPRRGRGLLRALVFLLLGAFLLAAGFGAGYFYFANPLSPAKDVLRLIERTPEADEPAADPDAPQKVPRPTPERESFVTSYYQFKEPLTTNLRASRRLLQAGIGLSTQYDQKVMDNVARNEVALRSDMLAIVGTFSEEELQDKAGRDRLAELRGAVNARLQQLEGFGGIEAVFFPSFILQ
The following text describes a protein:
Function:
Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
Sequence:
MFVGITYYTTPLLEIALIWVVLNYLLKFFWGTGAMDLVFGLLSFLCLFVLAEKLHLPVIRNLMLHVVNIAAIVVFIIFQPEIRLALSRIRLRRGKFVINMQDEFIDHLTACIYRMAERQIGALIVLENERLLNDLLNLSAVKINADFSEELLEAIFEPSSHLHDGAVLMRGETISYARVILPLAHDTTQLSRSMGTRHRAALGASQRTDALVIVVSEKTGAVSLARDGILTRGVKMDRFKAILRSILTRNERKTNPIISWMRKK
The following text describes a protein:
Function:
Regulates arginine biosynthesis genes.
Subcellular Localization:
Cytoplasm.
Sequence:
MRKRDRHQLIKKMITEEKLSTQKEIQDRLEAHNVCVTQTTLSRDLREIGLTKVKKNDMVYYVLVNETEKIDLVEFLSHHLEGVARAEFTLVLHTKLGEASVLANIVDVNKDEWILGTVAGANTLLVICRDQHVAKLMEDRLLDLMKDK
The following text describes a protein:
Function:
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Subcellular Localization:
Cytoplasm.
Sequence:
MNEILNTKDINVIGEFFIETWGCQMNEEDSEKLSGMLKKEGYIRTEERENADVIIFNTCCVRENAELKVYGNLGILKGLKSKNPNLIIAVTGCMMQQKGMAETIKKKFPFVDIIIGTHNLHNFPNYLNEVKKKDTSVLKIQEKENSIIENMPIDRKNSMKAFVTIMYGCNNFCTYCIVPYVRGRERSRTPENIEAEIKKLISEGYKEITLLGQNVNSYGKDLEPNVTFAELLKRVNNIEGLERVRFMTSHPKDLTDDVIEAIAKCDKLCEQIHLPVQSGSSEILKKMNRHYDREKYLDVVSKIKKLIPNVALSTDIIVGFPGETEKDFEETLSLVKEVEYDSAFTFLYSIRKGTPAAKFEDQVPEDVKHKRFNRLVEVLNEISAKKNKAYEGKIEEVLVEGTSKNDENKLMGRTRTGKLVNFIGDKDSIGELVNVKIIKANSFSLTGEEI
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein. Mitochondrion intermembrane space.
Sequence:
MGAHLVRRYLGDASVEPDPLQMPTFPPDYGFPERKEREMVATQQEMMDAQLRLQLRDYCAHYLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEFERERRLLQRKKRREKKAAELAKGQGPGEVDPKVAL
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MQLHYVFSHLQNSFRARKSLASVPNCNSVLELCAVLYHQGFLSSIQRGDIHGPDALPTITTRQNVATRRLWLGLKYFEGKPVLHYIRAVSKPSRKVNLTPSELLQFAKGRKVSFVNGLEPAEVGIVETKHGIMSIDDAIKNNLGGNVICRVK
The following text describes a protein:
Function:
Transcriptional regulator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters.
Sequence:
MDLKEVKGSEVEEMKTCSDCHTTRTPLWRSGPAGPKSLCNACGIKYNKKRRQLLGLDKGRSVSKKKRKISGEKIVEKIKDSH
The following text describes a protein:
Function:
Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Sequence:
MSHSSGIPASQELISAFGSANTGDVRLIKVVIKNDELVVDQKLNVQSDFETDLELAHSVLQKDSPCYILYKKDDKSIELTGYNWIFMFFVPDNAKVREKMTYAATRGNLKRELGASHFVDEIYSSNMNDFSKKGYQQHKLHQESEAPLTMEEQQRNDEKEQGLFVGGGGSGMHVHGISFPVDSDASTAVSNFINKKFNYIELSVNVDDEKIIFSSSSNIDIEAISSKISSTEPSFHFFRYSHQHEGENLDSIIYIYSCPDGSNGTKSAPVRKRMLFSSSKANVEQLVTSHNVKIDLKLEINSPSEISEESIINELHPPKVEEKKAFSKPSRPGRK
The following text describes a protein:
Function:
Non-catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met. NatB acetylates TPM1 protein and regulates tropomyocin-actin interactions. MDM20 is required for mitochondrial inheritance during budding and together with TPM1, is essential for the integrity and assembly of actin cables. Genetically interacts with CIN8.
Miscellaneous:
MISCELLANEOUS: Present with 5800 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSDKIQEEILGLVSRSNFKQCYAKLGQLQKQFPNALYFKILETYVKFKQSPGKFDYNKLLEEPYGLKGTTITGDTRSLEFLHNFFVELGKYDEALHVYERGNFKFPSYELSYHWFMKALEDSNYNQMSKASLQLAKYSDSGNLPKRAYYFWNAISILAVSRFQENTLSDPKKILLSRLARQSLLDLKPFQNVQEIIVYCLVLDELFPQSREISEEIVAITFANFDTSVNLYLKNFILKHTKLLNSPQKLFEVCSKLIEKGLDDYELITNLIDAAYKLSKSKDEVKQWIDENLGDSRNTRLARLKLDIMYTDSVSESSLSYYLSKYHNKPCCSIDLNHYSGHINIDMLKSIMSKYDPEDKDLIHHCNILELGLIGSDSINNYNKFKGTLEKKSVTDYSSCSTFLLEIVKDKCKKTNPELKDVLLCITILENYQAKDPHNFDTMCWLIVLYMYLGLVPDAYFHFINLKIKNVQTDSLDYMIFSRFSTLFPNKQSDFYSKTFHEHNNLYDTSLANLPRYIQVAFERNSYSKILGMLEMRDKLMKSYTRWTKTLENLQFSRLCNDKRGHLLQKLHEDWRSLEMTQSVSFSDNRDFSILDENFAQFLNRGKILEYANLNEESIFLTLIRELIIEALPNGEKTEQISALLKKLPSINLEELLNNNLTEVESASFLIFFEIYENNGKNLHDLISRLMKVPINAKQNWMVSHTYLTKMATLKTLDSLKRIKDKEIQKLIKNSLKELRSCCDDVFKGYSKALVQAYEELKKDECGNLLKELDVKAENVKNIKNSLLGIQKSVRNL
The following text describes a protein:
Function:
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Sequence:
MPPIIKRRVMRKIIIASQNPAKVNAVRSAFSTVFPDQEWEFIGVSVPSEVADQPMSDEETKQGALNRVRNAKQRHPGAEYYVGLEAGIEENKTFAWMIVESDQQRGESRSACLMLPPLVLERLRQAKELGDVMDEVFGTENIKQKGGAIGLLTRHHLTRSTVYHQALILALIPFINPEHYPSA
The following text describes a protein:
Function:
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Subcellular Localization:
Cytoplasm.
Sequence:
MSRVSEQPVDRITIPLLQRWKQDGRRLVMTTAYDAVAAPIPDPSIDISLVGDSGGNVCLGFENTPPVSVAMMNHHLEAAVRSKPRALLVADMSFLSFHVSVEETIRNAGGFLQRGAAAARLEGGGKRIEMVRAIVDCEIPVMGHLGLVPQSVNVMGGFKVQGRKVDEALRLLDDAHRLQEASCFALVLEGTPAELTARVSDSLTIPTIGIGSGPDCSEQVLCFMTCWAKPKVIAPNSFPPIRKAFSSSMMRFRAGQRMSAVARSPARKSPIGFPKALGRQLPTGRHPPQIITSVAELRRTLAKSRSANQRAGLCRRWAISTMATWR
The following text describes a protein:
Function:
Pyridoxal phosphate (PLP)-dependent decarboxylase involved in the biosynthesis of amidated D-glucuronic acid structures found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the decarboxylation of L-serine phosphate to ethanolamine phosphate. Less active with L-threonine phosphate. No activity with L-serine, L-threonine, L-aspartate or L-glutamate.
Sequence:
MLIKLNDYEKNITQKIKDLKNASGSHSPSIFTMAEQIPELNIKIDSCFLSNPYATALFLRYLKEELIDGQKLRSVLEFYPSQNSIIAKTVADFIGIDPKNVFIGNGAIEIIQAVMHNFVGKKIIVNIPTFSSYYEFAKSETNVVYYQLSKEDNYNLNIEHYLNFVKNENPDSVVLINPNNPDGGYINYEKLRYILSELKYVKNIIIDESFIHFAYENKDYNGINIEYLFKEFHNTIIIKSMSKDFGVAGIRIGYAIMSEDKIRGLLKNGYLWNSSGLSEYFLRLYVRKNFFDEYDKVRREYIQETQTFFRKLSGIKQFKVYPSMANFALVELLDGSSSTDFVAKMLIKYGIYMRTCNDKIGLEGEFIRIASRTLEENDMVLKSICDVFKE
The following text describes a protein:
Function:
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Domain:
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence:
MSSNKASFFTRLRRLCRLAVWLFKTGKNLRGIDGGCPESRNRAVIELGRGVLAALDIGLEVGRPAPEHPNGVLVAANHVSWLDIFAMSAVYPSSFIAKQEIKSWPVLGKMGQNAGTVFINRNSRRDIEPINRAVCETLQRGQNVSFFPEARTSSGLGLLPFKAALFQSAIDAGAKVLAVALRYYDETGKRTARPSYADVGLPTCLWRIVSMKKLTIRVDFVCVADAAESEDRYALKDKIEESIRAVVADDADIAV
The following text describes a protein:
Function:
Involved in adherence of spores to the host cell surface and in infection efficiency.
Subcellular Localization:
Cytoplasm. Spore wall. Spore polar tube. Note=Localized to the cytoplasm of sporonts and sporoblasts and to the spore wall and polar tube of mature spores.
Sequence:
MIKGLIYLFLFRCLEGRLADYEEESSDLGDYSLNGQTDEEYGKFPSHVLTEKETGPMDEIRCTNDDYTYNIKLNVHLQNYAIQAIADAAKPKLGMNLKERDAILSYFGTIANELNADLARLGAQIVIGLKHYKAEDFIDTNSFDTSCEIRDPVMDRLDSTFKQLKDVYQDSMGLRLFVWTCPQLTSSFETMKIMSNLNCGRIMGVLWQGADATRTSIKSTILEAISGVSELYLDGALPVDRVFSNVCRFCSKCVGVEPGVIGWKHPDVVKLIHAIPEEDTHEHGYDH