lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MEAAIVGQRQKSDDESGGDGNNKDSNSIAPSAIAINSKKKQTTKDIVTTQGAQFISESLIGETQTKDLDKPSAVHQRGIVPLCNGLDIIQQSLFGTTVTLCCGILQRLDYASTECQALVLVPTHDLAHETQNVIGVLGQFLSAKAHAFCGGTSAHEDQQILSTGVQVAVGTPCHVLGMLQGRALCPDHIRMFVLDEADEVLRGFKDQIHGIIQFLPTKTQFGFFSASMSHEALEMCRKYMNKPVEIIVPRDEELEGINVKQFYVNVEKEDCKLDKLCGLFDTMEITRSIIFVNTRHHAKSLTEKIRGKGYTVSAIHGGIHQRARDKAVQEFQSGSSRILITTDLRGIDVLRAPAAIFYDLPTQPVCYLRHVQSGQHGRKGVAISFITSTDERVFSTIQKFCNTQIEELPSNVADLL
The following text describes a protein:
Function:
MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MARKKKKKHEDEHVDESWLVPYADILTLLLALFIVLYASSSIDAAKFQMLSKSFNEVFTGGTGVLDYSSVTPPENESDGIDEVKKEKEEKEKNKKEKEKAADQEELENVKSQVEKFIKDKKLEHQLETKMTSEGLLITIKDSIFFDSGKATIRKEDVPLAKEISNLLVINPPRNIIISGHTDNMPIKNSEFQSNWHLSVMRAVNFMGLLIENPKLDAKVFSAKGYGEYKPVASNKTAEGRSKNRRVEVLILPRGAAETNEK
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.
Subcellular Localization:
Cytoplasm. Secreted, cell wall.
Sequence:
MPEGRHVAIIGAGAVGVISAIEALREGHRVTLIDPGEPGGEQAASYGNAGWLSSHSVIPPAEPGIWKKVPGYLMDPLGPLAIRWSYLPKALPWLIKYLLSGWTEARVEKTAFALRDLLKDAPLLHRKLAEEAGVPELIERNGVMHAFPSRGNFDNDLGWRLRKKVGVAWLELNADEMRQREPDLHPRYSFGVVVEEAGRCRDPGAYVAALANHALASGAKLVRAKATGLKLSGNKLVAVVTETGEIACDAAVVAAGARSKQLTASVGDPLPLETERGYHVMIENPETGPRSSIMASDAKMVVNWTNKGLRAAGTVEIAGLEAAPNWKRAEILRDHLFSMFPKLPRDIPASRIKTWFGHRPSMPDGLPCIGHARASRDIVYAFGHGHVGLVGSARTGRLVAQLLSGKQPEIPLAPFSPTRFL
The following text describes a protein:
Function:
Removes N-terminal dipeptides sequentially from polypeptides (By similarity). Essential for control of distal tip cell migration.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MENDNYDVEEQGCSVFNGKHGYFARSCCVVFILIICVIFVFSVIFTFMQNPINLNSDNGFNQTSGNTSSLEATTLKPKFSSLMTTTRRFTFEQLFSGKQFLVDYYDYIWLPDGSFVQMNDDFTIRKQMKKIPLGSSVAEPFFNNGEYVKALSSNMKYAYGSKKVNELWRHSAEYLYHIVKINNKTVSTEQWHVGPEENSLIQAFYWNPNASSNDFVYVHNYNLYYQKDPEKPDGAIQLTVGGSTFNRFGLANWLYEEEILEASSAVWWSPSGRYVSYLRFDDREVNRIFLPKYTDDDSYVEYFELPYPKAGVQNNTLVTQYIWDSENHKIVETAPPNELSAANGDYYVLTNKWITMPRNGSDLGEERLVTVWANRDQNHVYFSLCNEQDCVMALSFQFSIDNRQLWVSPKDVRGVFPTETGFLTVLPHKHDDGNIYNHVAHVELDGTGTGKITKWIGENFDVILVLGYSSKIDALTFSAYGDGVGEFSTYIVREAMYSNKKTTLQKVTDQFEDCKTLGSQSADPTGQRIVVQCEKPFDNTRLYLVDVVDTTKKIMLEGGTKAVIPFDVPNMKFGKLKLPSGIDGHYMMLTPANLLDGAKIPLLLDIYGGPDSKQVFQKTPTAHAIQIVSQYDIAYARIDVRGTGGRGWDVKEAVYRKLGDAEVVDTLDMIRAFINTFGFIDEDRIAVMGWSYGGFLTSKIAIKDQGELVKCAISIAPVTDFKYYDSAYTERYLGQPAENLQGYINTNVIPHARNVTNVKYLLAHGERDDNVHYQNSARWSEALQQNGIHFTQLVYANEAHSLSHKLFHLYGEVQRFLMNDCFKSNLDLL
The following text describes a protein:
Function:
Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated.
Subcellular Localization:
Nucleus.
Sequence:
MTPEPRTRKSTRLHLKQTSSESVNTRRRTRKPIIISDSEEENVPETEKSPFKKPPNTPYKTKSRTPPEDRTVTPPKQRKMSENNENLQTPPSTPTILLERLSLLSPNEKSNRKKLFQEDDLYQNARRALHSSCPTNLPGREKELGDLKQFILQHLDEGTSGTLYISGPPGTGKTASLNLVLEDPQISSGIEHVYVNCTSIKSSGSIFSRIAKDLGIKASGKSEKDYVGAIEKFLQKGHRTILLVLDEIDQLESKKQSVLYTIFEWPANPNSRLILIGIANALDLTDRILPRLQARCELKPQLMHFAPYTKQQIVEIFTNRLKNANVLDIFSPIALQMLAGKVAAISGDVRRALDIGRRVIEMSDKKKRGECVLKSVENLATELEEKKLESVDMRQVVQVLNRVYGTTQSLDEEVEDSFPLQQKIIVCSLLLILKKAKNKDVTIGRLHDVYRRVCAKRNIQVVDQGEFVGLCSLIETRGMVKIIKKKDPRMNKVSLVWDEGEVSATLRDKQLMSMILQDDSCLGKM
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular Localization:
Cell projection, growth cone. Cytoplasm, perinuclear region.
Sequence:
MSDGGAGRLRRQLESSGFEARLYVKQLSQQSDGDRDLQEHRQRIQALAEETAQSLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPASSSSSSAASGQPSEEPGSDAPAPPAEDGRQRTLTTLLEKVEGCRPLLDTPGQRLVYNGDLVEYEADHMAQLQRVHGFLLSDCLLVATWLPQRRGVYRFNALYPLDGLAVVNVKDNPPMKDMFKLLMFPEGRIFQAENAKVKREWLEVLEEAKRALAGERRLRQQEAAAPRPPPPPADPFDDDDDDDRRRPERRRREAEAGPAAPDWVRELPEDLDVCIAQRDFEGAVDLLDRLDRHLRAGPPALPELRARVDERVRQLTDVLVFELSPGRSLRGGPRATRRAVSQLIRLGQGTKACGLFLRNRAAAVRGAIRQLRIEGSTLLYIHKLCRVFFTGLLETAREFETDFAGAHGGGCYSALVVWARAAVGLFVDAFSGRVFDGKESLSTAAECVKVAREHCRRLGALGLDLTFVLHALLLKDIRGALRGYKEIVVEAAKHRNSEEMWRRMNLLTPEALAKLREEMRQCGVGPGFEQYAGQDACWVGLSYTVVAFTKQTVGFLDEALKLYCPELHTVLLESLVEVILVALQHVDYSLRCEQDPDKKAFILQNATFLYQAVLPAVERRFEDGVGRPARQLQDLRSGAWLVRVNPESTTSVV
The following text describes a protein:
Function:
Metastasis suppressor protein. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Intracerebroventricular administration induces an increase in serum LH and FSH levels in prepubertal male and female as well as in adult animals.
Subcellular Localization:
Secreted.
Sequence:
MISLASWQLLLLLCVASFGEPLAKMAPVVNPEPTGQQSGPQELVNAWQKGPRYAESKPGAAGLRARRTSPCPPVENPTGHQRPPCATRSRLIPAPRGSVLVQREKDMSAYNWNSFGLRYGRRQVARAARG
The following text describes a protein:
Function:
Transcriptional regulator that binds CpG, CpNpN and CpNpG (N is A, T, or C) islands in promoters regardless the DNA methylation status. Plays probably a role in gene silencing.
Subcellular Localization:
Nucleus.
Domain:
The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
Sequence:
MKEEEEIGKPAKPKAKKDVAPGRLIDTYAAQCDNCHKWRVIDSQEEYEDIRSKMLEDPFNCQKKQGMSCEEPADIDYDSSRTWVIDKPGLPKTPKGFKRSLVLRKDYSKMDTYYFTPTGKKLRSRNEIAAFVEANPEFRNAPLGDFNFTVPKVMEDTVPPDPKLGSPFPSTTTTTSEKSSVKQSHN
The following text describes a protein:
Function:
Regulatory protein of the MTREX-exosome complex involved in the synthesis of the 60S ribosomal subunit. Participates in an early cleavage of the pre-rRNA processing pathway in cooperation with NVL. Required for blastocyst formation, is necessary for RNA transcription, processing and/or stability during preimplantation development.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAATSARWNHVWVGTETGILKGVNLQRKLAANFTPSGQPRREEAVNALCWGTGGETQILVGCADRTVRHFNAEEGTFQSQRYCPGGEGTFRGLAQADDGTLITCVDSGILRVWCENDKEASSDPLLELKVGPGVCRMRQDPTHTHVVATCGKENALKVWDLQGSEEPVFRAKNVRNDWLDLRVPIWDQDIQFLPGSQKLVTCTGYHQVRIYDPASPQRRPVLEATYGEYPLTAMTLTPEGNSVIVGNTHGQLAEIDFRQGRLLGCLKGLAGSVRGLQCHPSKPLLASCGLDRVLRIHRIRNPRGLEHKVYLKSQLNCLLLSGRDNWEDEPQEPQEPNLVPPEDTETDELWASLEAAAKRKLPDLDQKQGNEGDNLGRRKQRSNESLLITVLWRRLSMFSRRGSSRSGKQDNQMQERKREGSHKEPEKG
The following text describes a protein:
Function:
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Miscellaneous:
MISCELLANEOUS: Present with 220 molecules/cell in the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MIFNPVISNHKLSHYIHVFCTFTTFCILGTETRQAITALSTYTPAFVTAPTVLWSNCSSCMLMGIMQSLNAYTWMKDHQVLFLGVTTGYCGALSSFSSMLLEMFEHSTNLTNGNIANHTKLPNRAYGIMEFLSVLLVHLMVSMGSLIFGRQLGKEVIVAYGSSSFSKPYTPPSDTVKENAGDVDTQEMEKNILEFKFKTPAPFFKKFFDVVDKLAYALAFPLIILFVVLCAYYENYSRGKWTLPCLFGIFAGFLRYWLAEMFNKTNKKFPLGTFLANVFATLLIGIFTMVQRGKKHFSTDIPIVNSLNSCHIVSALISGFCGTLSTISTFINEGYKLSFINMLIYYTVSIGISYCLLVITLGSYAWTRGLTNPIC
The following text describes a protein:
Function:
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular Localization:
Plastid, chloroplast. Mitochondrion.
Domain:
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence:
MGGLQLVESPIALRLVSAASRPRRRLSLATFGHGLRPFRGCNGMICVSKARQTHVEVSSTYLYKLTSPKKVKFSTRSTSASVQPMTQDITEDMHKDYPISGDEIRTRFLNFYASRGHKILPSASLVPDDPTVLLTIAGMLQFKPIFLGKEPRSVPCATTSQRCIRTNDVENVGKTTRHHTFFEMLGNFSFGDYFKKEAIVWAWELTTKEYKLPPERLWISVFKDDDEAFSIWHDEVGVPKEHIKRLGEDDNFWTSGITGPCGPCSEIYYDFHPERGSESADLGDDSRFIEFYNLVFMQYNKKDDGSLEPLKQKNIDTGMGLERMARILQQVPNNYETDLIFPIIQKAANLAMISYAKADDATKTNLKIVGDHMRAVVYLISDAVLPSNIGRGYVVRRLIRRVVRIGRLLGIKGAGEGNPDGAFLPGLAKIVIELSNQIDPDVTGRMPHILEELKREELRFVQTLERGEKLLDQFLASALLNASTNGDRPCLAGKDVFLLYDTYGFPVEITAEVAEERGVSLDMNGFHIEMENQRRQSQAAHSTVKLSVGNEVELAESVPDTEFLGYDMLSANAIIKGLLQNGEPVTEVAEGSDVEIMLDRTPFYAESGGQIGDNGFLRCKGVEDSKDTAIVEVKDVQKSLGNIFVHKGTIKEGKIEVGLEVNAIVDPRLRQRAKVHHTATHLLQAALKNVIGQETSQAGSLVAFDRLRFDFNFHRPLFEHELMKIEELINQWINDSTLLQTKVMPLLDAKKAGAIAMFGEKYGEQVRVVEVPGVSMELCGGTHVSNTSEIRGFKIISEQGIASGIRRIEAVAGEAFIEYVTTRDNSMRHLCSVLKVKAEDVTGRVENILEELRIARNEVSALRTRVAILKATALVNKAFIVGTTNIRVVVESMDDTDADSLRNAADYLVDSLQDPAAVVLGSCPGDGKVSLVAAFTPSVVKMGIQAGKFIGGIAKLCGGGGGGKPNFAQAGGRKPENLSNALEKARVELIAALDGKTS
The following text describes a protein:
Function:
Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module.
Sequence:
MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV
The following text describes a protein:
Function:
Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation.
Subcellular Localization:
Nucleus.
Domain:
The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence:
MKMQSPKMEQEEVEEERMRNKWPWMKAAQLMEFRMQALVYRYIEAGLRVPHHLVVPIWNSLALSSSSNYNYHSSSLLSNKGVTHIDTLETEPTRCRRTDGKKWRCSNTVLLFEKYCERHMHRGRKRSRKLVESSSEVASSSTKYDNTYGLDRYNESQSHLHGTISGSSNAQVVTIASLPSARSCENVIRPSLVISEFTNKSVSHGRKNMEMSYDDFINEKEASMCVGVVPLQGDESKPSVQKFFPEVSDKCLEAAKFSSNRKNDIIARSREWKNMNVNGGLFHGIHFSPDTVLQERGCFRLQGVETDNEPGRCRRTDGKKWRCSKDVLSGQKYCDKHMHRGMKKKHPVDTTNSHENAGFSPLTVETAVRSVVPCKDGDDQKHSVSVMGITLPRVSDEKSTSSCSTDTTITDTALRGEDDDEEYLSLFSPGV
The following text describes a protein:
Function:
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, throughout development (By similarity). Required for ubiquitination of histone H2A. Plays a role in the formation of the male-specific genital sensilla (simple sense organs) known as rays. Required for normal migration of the hermaphrodite specific neurons (HSN) and for extension of some neuronal processes. Represses vulval fates in hypodermal cells that do not normally contribute to vulval development.
Subcellular Localization:
Nucleus. Nucleus, nucleolus.
Sequence:
MTRKRPALAEPVSSSRSRVTRRSTTGAPSSKKKRSPEPESDADSEDDYDGPSTSQTKKLKRGNSSTNRGKAANKTKRGSFQVKQEIMDDDENEEKIDGEVENGITSREHSPDPSTFKKTAKLQTKKKKKKESPPETPPTSPSPSPSRSVSPSTTKSDISSKKGRKAVVNSVSKVKIEKESTPVKTNGRNLPPKRKKKPVEEETAEEIKLRERAERKARRIEEAKNRPKLTIEQKLAKLRKKKERRERRKEQEKEESMRQKYGQRKIKAEASKWNFGPISSINQRRRDEMMAYFPKANFLAEDGVPKVMNNFRRATVKYNMEVLNPFITCGICDGYIVDATTIIDCMHTFCKSCLLTYFESDNNTCPTCGTFIHGSHPTHYVTYDRAVNELVNQFVPKMENNELDVRKTFLRDCREALGIDTAAEDRERKERLERERITGTNRCYPLERPRFSHHRDDCQVTVNLLPGTANLPLITRPYVRCSEMTTMNTLKKFLSLQIWDDQSRYSDLDMFCDGQLMGKDFSVRFVWMMKRRGQPKSEPLIIRYHMTRT
The following text describes a protein:
Function:
E3 ubiquitin ligase that plays a role in various biological processes including neural stem cell differentiation, innate immunity, inflammatory resonse and autophagy. Plays a role in virus-triggered induction of IFN-beta and TNF-alpha by mediating the ubiquitination of STING1. Mechanistically, targets STING1 for 'Lys-63'-linked ubiquitination which promotes the interaction of STING1 with TBK1. Regulates bacterial clearance and promotes autophagy in Mycobacterium tuberculosis-infected macrophages (By similarity). Negatively regulates TLR3/4-mediated innate immune and inflammatory response by triggering the autophagic degradation of TICAM1 in an E3 activity-independent manner. Plays an essential role in oxidative stress induced cell death by inducing loss of transmembrane potential and enhancing mitochondrial reactive oxygen species (ROS) production during oxidative stress conditions. Ubiquitinates XIAP and targets it for proteasomal degradation. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2 (By similarity). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation. Positively regulates dendritic branching by promoting ubiquitination and subsequent degradation of the epigenetic factor CDYL (By similarity). Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-41' to initiate autophagy (By similarity).
Subcellular Localization:
Cytoplasm. Note=Localized in cytoplasmic bodies, often located around the nucleus.
Sequence:
MAAAAAASHLNLDALREVLECPICMESFTEEQLRPKLLHCGHTICRQCLEKLLASSINGVRCPFCSKITRITSLTQLTDNLTVLKIIDTAGLSEAVGLLMCRGCGRRLPRQFCRSCGVVLCEPCREADHQPPGHCTLPVKEAAEERRRDFGEKLTRLRELTGELQRRKAALEGVSRDLQARYKAVLQEYGHEERRIQEELARSRKFFTGSLAEVEKSNSQVVEEQSYLLNIAEVQAVSRCDYFLAKIKQADVALLEETADEEEPELTASLPRELTLQDVELLKVGHVGPLQIGQAVKKPRTVNMEDSWAGEEGAASSASASVTFREMDMSPEEVAPSPRASPAKQRSSEAASGIQQCLFLKKMGAKGSTPGMFNLPVSLYVTSQSEVLVADRGNYRIQVFNRKGFLKEIRRSPSGIDSFVLSFLGADLPNLTPLSVAMNCHGLIGVTDSYDNSLKVYTMDGHCVACHRSQLSKPWGITALPSGQFVVTDVEGGKLWCFTVDRGAGVVKYSCLCSAVRPKFVTCDAEGTVYFTQGLGLNVENRQNEHHLEGGFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKEILHFPKGGGYSVLIREGLTCPVGIALTPKGQLLVLDCWDHCVKIYSYHLRRYSTP
The following text describes a protein:
Function:
Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.
Subcellular Localization:
Secreted.
Sequence:
MWAQLLLGMLALSPAIAEELPNYLVTLPARLNFPSVQKVCLDLSPGYSDVKFTVTLETKDKTQKLLEYSGLKKRHLHCISFLVPPPAGGTEEVATIRVSGVGNNISFEEKKKVLIQRQGNGTFVQTDKPLYTPGQQVYFRIVTMDSNFVPVNDKYSMVELQDPNSNRIAQWLEVVPEQGIVDLSFQLAPEAMLGTYTVAVAEGKTFGTFSVEEYVLPKFKVEVVEPKELSTVQESFLVKICCRYTYGKPMLGAVQVSVCQKANTYWYREVEREQLPDKCRNLSGQTDKTGCFSAPVDMATFDLIGYAYSHQINIVATVVEEGTGVEANATQNIYISPQMGSMTFEDTSNFYHPNFPFSGKIRVRGHDDSFLKNHLVFLVIYGTNGTFNQTLVTDNNGLAPFTLETSGWNGTDVSLEGKFQMEDLVYNPEQVPRYYQNAYLHLRPFYSTTRSFLGIHRLNGPLKCGQPQEVLVDYYIDPADASPDQEISFSYYLIGKGSLVMEGQKHLNSKKKGLKASFSLSLTFTSRLAPDPSLVIYAIFPSGGVVADKIQFSVEMCFDNQVSLGFSPSQQLPGAEVELQLQAAPGSLCALRAVDESVLLLRPDRELSNRSVYGMFPFWYGHYPYQVAEYDQCPVSGPWDFPQPLIDPMPQGHSSQRSIIWRPSFSEGTDLFSFFRDVGLKILSNAKIKKPVDCSHRSPEYSTAMGAGGGHPEAFESSTPLHQAEDSQVRQYFPETWLWDLFPIGNSGKEAVHVTVPDAITEWKAMSFCTSQSRGFGLSPTVGLTAFKPFFVDLTLPYSVVRGESFRLTATIFNYLKDCIRVQTDLAKSHEYQLESWADSQTSSCLCADDAKTHHWNITAVKLGHINFTISTKILDSNEPCGGQKGFVPQKGRSDTLIKPVLVKPEGVLVEKTHSSLLCPKGKVASESVSLELPVDIVPDSTKAYVTVLGDIMGTALQNLDGLVQMPSGCGEQNMVLFAPIIYVLQYLEKAGLLTEEIRSRAVGFLEIGYQKELMYKHSNGSYSAFGERDGNGNTWLTAFVTKCFGQAQKFIFIDPKNIQDALKWMAGNQLPSGCYANVGNLLHTAMKGGVDDEVSLTAYVTAALLEMGKDVDDPMVSQGLRCLKNSATSTTNLYTQALLAYIFSLAGEMDIRNILLKQLDQQAIISGESIYWSQKPTPSSNASPWSEPAAVDVELTAYALLAQLTKPSLTQKEIAKATSIVAWLAKQHNAYGGFSSTQDTVVALQALAKYATTAYMPSEEINLVVKSTENFQRTFNIQSVNRLVFQQDTLPNVPGMYTLEASGQGCVYVQTVLRYNILPPTNMKTFSLSVEIGKARCEQPTSPRSLTLTIHTSYVGSRSSSNMAIVEVKMLSGFSPMEGTNQLLLQQPLVKKVEFGTDTLNIYLDELIKNTQTYTFTISQSVLVTNLKPATIKVYDYYLPDEQATIQYSDPCE
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MQNGGASSDQNGSISSVPRDTSRPLTEDELDRYSRQMIVPGMGKEAQLRLINAKVLIIGAGGLGCPAAQYIAGAGIGTIGIADGDTVERSNLHRQVGHSTSRIGQSKVSSLITHLRGLNPLPTYVAHTTHITPLNAADLISQYDLILDCTDNPATRYLISDVCVLLCKPLVSAASVQTSGQIIVLNCPPTPQGQLDGGPYPPCYRCCFKKPPPANAQLSCGEAGILGPVVGLMGVAQAGEAIKILASALHIPTTTTTTTSPPAQGVPRAAPVVEPTLLLYSYSLTSFLSPFTFRALKMAPRKKNCFACGEGSKQRLTLEGVKNGEPNYDFFCGLGGGGPEKGVLSEEERITPREFVERVQGKDGNGKGKKYVVLDTREKEHFSFGSIEGAVNLPFGKLLSKAAQLKRSGETPKVGDILPPEIQVRDGHGDKDIPIYVVCRRGLDSQEAVEKLKEMGLDNGGSRKIVDIAGGMKAWKEQVDPSFPYL
The following text describes a protein:
Function:
Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MGLRFAHLAGGVARAAFSRRGPHLSAACAHRVLAPLASPGEPSGGNWLIPARGHGGHSHHHGEESGEASEKIFRLGLAADVVLTVGKAITGYLSGSTAITADAAHSLSDIVLSGVALLSYKAAKVPRDKDHPYGHGKFESLGALGISSMLLITAGGIAWHSFEVLQGVMSSAPDIIGNTSQMNHNHGSGGHNHAIDLEHPVLALSMTTLAISIKEGLYWITKRAGEKEGSGLMKANAWHHRADAISSVVALVGVGGSIVGLPYLDPLAGLVVLGMILKAGVQTGYESTLELVDAAVDPSLLEPIKETIVKVDGVKGCHRLRGRKAGTSLYLDVHIEVYPFLSVSAAHDIGETVRHHIQKTHNQVAEVFIHIDPSYSMGANVDKKRILENLERRNSDVIPRQRSAEAMVSDIISSHLPKKMCLEHLMLHYLQGRVLLQVQVSMSPEILIRDAMDIAKKAEEEIMKADASICQVSVQLRLGQQIEQLQLAASKSGANDLLPPFGFRCRGGSKI
The following text describes a protein:
Function:
Required for flagellum motility.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MQGANLKVLPSTRAAAKELVDPLDITNVGWSTLEPKFDELMQLMDAPSSGINALAARSAHREKVGAVIEQLLTRAQDESRRLLVEGNGEAAAEAGVKTLRLKERFYGKGSVKLVPAHFHLARTNQFLKRYGNAEEILSLAHFIILQNPDEADATIKAELHQTFGLLYAADNKLDVSVKHLTCATYYLSVMNGPEHVLTTFAYFDLANVFATKACMEAAMALYDTVKNIWLKHLRRVLKDIVDETMAAKLVKRYDDDEVTHEVGHASARAFGKENLADVSKMLFGIFSIQKERLTISHPTTARAQFLLGLYLLWVNKNDEAAEHLLSARTTSQKFYGERHPIVQDIEDWCIWFEIPFRGVAAEQ
The following text describes a protein:
Function:
Immunoglobulin-like receptor which plays an inhibitory role in degranulation of mast cells. Negatively regulates IgE-mediated mast cell activation and suppresses the type I immediate hypersensitivity reaction.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MWSHLNRLLFWSIFSSVTCRKAVLDCEAMKTNEFPSPCLDSKTNVVMKGQNVSMFCSHKNKSLQITYSLFRRKTHLGSQDGKGEPAIFNLSITEARESGPYKCKAQVTSCSKYSRDFSFTIVDPVTAPVLNIMVIQTETDRHITFRCLSVNGSLPINYTFFENHVAISPAISKYDREPAEFNLTKKNPGEEEEYRCEAKNRLPNYATYSQPVTMPSTGGDSCPFCLKLLLPGLLLLLVVIILILAFWVLPKYKTRKAMRNNVPRDRGDTAMEVGIYVNILEKQAKEESVPEVGSRPCVSTAQDEAKHSQELQYATPVFQEVAPREQEACDSYKSGYVYSELNF
The following text describes a protein:
Function:
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins smb1, smd1, smd2, smd3, sme1, smf1 and smg1 that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (By similarity). In the cytosol, the Sm proteins smd1, smd2, sme1, smf1 and smg1 (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone saf5 that controls the assembly of the core snRNP (By similarity). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from saf5 forming an intermediate (By similarity). Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of smd3 and smb1 to complete assembly of the core snRNP (By similarity). Within the SMN complex, smn1 acts as a structural backbone and together with yip11/gem2 it gathers the Sm complex subunits.
Subcellular Localization:
Nucleus.
Sequence:
MDQSQKEVWDDSELRNAFETALHEFKKYHSIEAKGGVSDPDSRLDGEKLISAARTEESISKLEEGEQMINQQTETTLEGDTHIQQFADNKGLSDEKPETRAAETHQEFMEVPPPIRGLTYDETYKKLIMSWYYAGYYTGLAEGLAKSEQRKD
The following text describes a protein:
Function:
Involved in vesicular protein trafficking.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MKYNIVHGICLLFAITQAVGAVHFYAKSGETKCFYEHLSRGNLLIGDLDLYVEKDGLFEEDPESSLTITVDETFDNDHRVLNQKNSHTGDVTFTALDTGEHRFCFTPFYSKKSATLRVFIELEIGNVEALDSKKKEDMNSLKGRVGQLTQRLSSIRKEQDAIREKEAEFRNQSESANSKIMTWSVFQLLILLGTCAFQLRYLKNFFVKQKVV