lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MTVQDAVDASEHYEIYNTDDIPSLYTIIIDTNPRAWAALNDVLPLTKALANILIFVNSHLAFNNSNQVALIASHTNRAVWLYPTAPDQNPGRHPQNPNEDIEMRDASFTSKQQSPPPANKYPLFAQIERSLLSSLRSLITDTTTEDITSTTTTQISGALTLALAHINKTALLFAPSNSATGPTPSSAGGKSSVSTTSGAGPGGGNAASLPGIGGGGLAGLHARILVVSVSDSSPSQYIPTMNAVFAAAHARIAIDTLALRGSATFLQQASYITRGTFIRAQEPRGLLQYLMFGFGSGSAPQGLAAAGNQRSQQQHGGHKGKEDKASEKALGAAAKGGAKHGGQKFLGSNASVADLLVTPSADSVDFRAACFCHRNVIDTGFVCSICLSIFCEVPEGGECLTCGTKLALGNYGRKLPVLPSKAAAPPGGGQANGKGTMLK
The following text describes a protein:
Function:
Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MNQDIKRLLKIKVDALKRLEKDYTLYKQEEISQYQKVERFKSDPTKDIYDVKKQEEILDETKRMIIDSVSRVTSYIVSLGEFLDEHKDKDDGSEIWIESYEIVDRLSTKFLNEQ
The following text describes a protein:
Function:
Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity.
Miscellaneous:
MISCELLANEOUS: UL16-binding proteins (ULBPs) are unusual members of the extended MHC class I superfamily. They do not contain the alpha 3 domain and lack a transmembrane domain.
Subcellular Localization:
Membrane; Single-pass type I membrane protein; [Isoform 4]: Secreted.
Domain:
MHC class I alpha-1 like and MHC class I alpha- like regions down-regulate the cell surface expression of KLRK1.
Sequence:
MRRISLTSSPVRLLLFLLLLLIALEIMVGGHSLCFNFTIKSLSRPGQPWCEAQVFLNKNLFLQYNSDNNMVKPLGLLGKKVYATSTWGELTQTLGEVGRDLRMLLCDIKPQIKTSDPSTLQVEMFCQREAERCTGASWQFATNGEKSLLFDAMNMTWTVINHEASKIKETWKKDRGLEKYFRKLSKGDCDHWLREFLGHWEAMPEPTVSPVNASDIHWSSSSLPDRWIILGAFILLVLMGIVLICVWWQNGEWQAGLWPLRTS
The following text describes a protein:
Function:
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 Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MAVGPVTGMFKRRIVTDFSVTMILGTLGACYWWFGYHKPAARQREEFYVKLAAEKNAE
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLSKYSIRSLTLLRFPRYKFSQQQQQQKEQQDEWDERTIEAEEANPTLENKEKAFSYFRLFSRIFWWTTSALFGYNLYLNNYKTDPTQELGYQKQINDAAKYCQDQYQAFYDFMTKPAIDKLLPDIPELPFGYEIPKTLVLNISGTLLHMDYVFGVGGEIKRRNGLQRFLEKLPKMYEVVILSDDETMFTQQITQKLDPTQIDICRESMVFEKGRYIRDLKYLNRPLNRVIVLDSDPERMYQYQDNGIFIKPFDGKQNDEVLKDVLLLLEHLSKPQVKDIRAELRKFGNFDPQIKYLDEVKAREINIKQTMNKGIFGIINQRKNPQFEQSRRQ
The following text describes a protein:
Function:
Seed storage protein. Has a protein kinase activity. Binds leginsulin.
Sequence:
MASILHYFLALSLSCSFLFFLSDSVTPTKPINLVVLPVQNDGSTGLHWANLQKRTPLMQVPVLVDLNGNHLWVNCEQQYSSKTYQAPFCHSTQCSRANTHQCLSCPAASRPGCHKNTCGLMSTNPITQQTGLGELGEDVLAIHATQGSTQQLGPLVTVPQFLFSCAPSFLVQKGLPRNTQGVAGLGHAPISLPNQLASHFGLQRQFTTCLSRYPTSKGAIIFGDAPNNMRQFQNQDIFHDLAFTPLTITLQGEYNVRVNSIRINQHSVFPLNKISSTIVGSTSGGTMISTSTPHMVLQQSVYQAFTQVFAQQLPKQAQVKSVAPFGLCFNSNKINAYPSVDLVMDKPNGPVWRISGEDLMVQAQPGVTCLGVMNGGMQPRAEITLGARQLEENLVVFDLARSRVGFSTSSLHSHGVKCADLFNFANA
The following text describes a protein:
Function:
Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate. When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for acetyl-CoA.
Miscellaneous:
MISCELLANEOUS: AccD6 is dispensable in nonpathogenic strains.
Sequence:
MTIMAPEAVGESLDPRDPLLRLSNFFDDGSVELLHERDRSGVLAAAGTVNGVRTIAFCTDGTVMGGAMGVEGCTHIVNAYDTAIEDQSPIVGIWHSGGARLAEGVRALHAVGQVFEAMIRASGYIPQISVVVGFAAGGAAYGPALTDVVVMAPESRVFVTGPDVVRSVTGEDVDMASLGGPETHHKKSGVCHIVADDELDAYDRGRRLVGLFCQQGHFDRSKAEAGDTDIHALLPESSRRAYDVRPIVTAILDADTPFDEFQANWAPSMVVGLGRLSGRTVGVLANNPLRLGGCLNSESAEKAARFVRLCDAFGIPLVVVVDVPGYLPGVDQEWGGVVRRGAKLLHAFGECTVPRVTLVTRKTYGGAYIAMNSRSLNATKVFAWPDAEVAVMGAKAAVGILHKKKLAAAPEHEREALHDQLAAEHERIAGGVDSALDIGVVDEKIDPAHTRSKLTEALAQAPARRGRHKNIPL
The following text describes a protein:
Function:
N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN), preferentially DAP-type PGNs. Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments.
Subcellular Localization:
Secreted.
Sequence:
MNTSTAISFVAALVLCCLALSANALQIEPRSSWGAVSARSPSRISGAVDYVIIHHSDNPNGCSTSEQCKRMIKNIQSDHKGRRNFSDIGYNFIVAGDGKVYEGRGFGLQGSHSPNYNRKSIGIVFIGNFERSAPSAQMLQNAKDLIELAKQRGYLKDNYTLFGHRQTKATSCPGDALYNEIKTWPHWRQN
The following text describes a protein:
Function:
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
Sequence:
METRLQELRARLQEIDDLNSAAAVLGWDQSTYMPPGGAAARARQLATLSRLAHMKSTDPELGRLLAELMPYAEQLPYEHPDAALIRVAQRNYERMTRLPTDLVSEIAAHTAASYHAWTQARPANDFATMLPYLERTLELSRRVADCFPGYEHPADPLIDFSDYGMRASVIRDLFARLRAGLTPIIRAIVAQPPIDDSCLRQYYPRNDQLAFGEQIIRRFGYDFERGRQDLTHHPFATKFSVGDVRITTRINEHDLGDGLFSTLHESGHAMYEQGIEPAFEATPLCNGVSAGVHESQSRLWENLIGRSRPFWEHFYPELQQTFPQQLGNVPLDTFYRAINRVQPSLIRTDADEVTYNLHVMIRFDLELALLEGTLKLRDLPDAWNARYAEDLGVTVPDYRDGVLQDVHWFGGLIGGAFQGYTLGNILSAQFLAAARAAHPAIDDEIGRGEFATLHGWLRENIYRHGSVFTPTELIERAAGGPMQIEPYLTYLRTKYSAIYGIDLSS
The following text describes a protein:
Function:
Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers. Involved in membrane fusion downstream of the lipid mixing step mediated by mymk. Acts by generating membrane stresses via its extracellular C-terminus, leading to drive fusion pore formation (By similarity).
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Domain:
The AxLyCxL motif is required for myoblast fusion.
Sequence:
MPAVFLLLRSLVVRLFGSRLAASGVQLLRRILTTATGHLGTVLRNIWERISSQQSKEAILGCVLCLLNMHKKVDN
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of lysine and hydroxylysine residues in collagen and elastin, resulting in the formation of covalent cross-linkages, and the stabilization of collagen and elastin fibers (By similarity). Essential for the elastic fiber homeostasis and for their maintenance at adult age (By similarity).
Subcellular Localization:
Secreted, extracellular space. Secreted, extracellular space, extracellular matrix.
Sequence:
MALARGSRQLGALVWGACLCVLVHGQQAQPGQGSDPARWRQLIQWENNGQVYSLLNSGSEYVPAGPQRSESSSRVLLAGAPQAQQRRSHGSPRRRQAPSLPLPGRVGSDTVRGQARHPFGFGQVPDNWREVAVGDSTGMARARTSVSQQRHGGSASSVSASAFASTYRQQPSYPQQFPYPQAPFVSQYENYDPASRTYDQGFVYYRPAGGGVGAGAAAVASAGVIYPYQPRARYEEYGGGEELPEYPPQGFYPAPERPYVPPPPPPPDGLDRRYSHSLYSEGTPGFEQAYPDPGPEAAQAHGGDPRLGWYPPYANPPPEAYGPPRALEPPYLPVRSSDTPPPGGERNGAQQGRLSVGSVYRPNQNGRGLPDLVPDPNYVQASTYVQRAHLYSLRCAAEEKCLASTAYAPEATDYDVRVLLRFPQRVKNQGTADFLPNRPRHTWEWHSCHQHYHSMDEFSHYDLLDAATGKKVAEGHKASFCLEDSTCDFGNLKRYACTSHTQGLSPGCYDTYNADIDCQWIDITDVQPGNYILKVHVNPKYIVLESDFTNNVVRCNIHYTGRYVSATNCKIVQS
The following text describes a protein:
Function:
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Subcellular Localization:
Cytoplasm.
Sequence:
MKHPGIFLIGLTGGIACGKSTVLAMLAALGARTIDADRVTHRLQQPGTPVYQAIVAAFGPQILTAPGGAIDRRKLGNIVFNDQAALKRLESIVHPAVRTEIQRFLAEVANAGGYATRLRPVERPIVVIDAIKLIESGWADECDQVWVVTCPPEQQIERLMTTRGMSLAEAQARIAAQPPQESRFSRAHVIIDNSGSQARTRAQVEAAWQQALVASHGA
The following text describes a protein:
Function:
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
Subcellular Localization:
Nucleus.
Sequence:
MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYSNQSVEDLLLQGNGTAGGNILVGGAASPMAQSVSQSPAQHDVYTVTEAPDSHVQEVPNSPPYYEEQNVLTTPMVREQEQQKRQQLKENNKLRRQAGDVILDAGDILVDSSSPKAQRTSIQHSTQPDVMVQPMIIKSEPENSSGLMDLMTPANDLYSVNFISEDMPTDIFEDALLPDGVEEAAKLDQQQKFGQSTVSSGKFASNFDVPTNSTLLDANQASTSKAAAKAQASEEEGMAVAKYSGAENGNNRDTNNSQLLRMASVDELHGHLESMQDELETLKDLLRGDGVAIDQNMLMGLFNDSDLMDNYGLSFPNDSISSEKKAPSGSELISYQPMYDLSDILDTDDGNNDQEASRRQMQTQSSVLNTPRHEL
The following text describes a protein:
Function:
The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling.
Subcellular Localization:
Secreted.
Sequence:
MSNAHFSQWHLCHVLKGAMRCISCSHTLSLLLCVLTLTPTSSGAGPETLCGAELVDTLQFVCGDRGFYFSKPTGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSKAARSVRAQRHTDVPRKVSTPGQRAEKATERRTSQHSDKTKNKKRPLPGHSHSSFKVRIHLHCYLIKKNQCSVFIMCIIFHKFLLIEIIV
The following text describes a protein:
Function:
Involved in the resistance to DNA-damaging agents.
Miscellaneous:
MISCELLANEOUS: Present with 2130 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MNIDCLCRWVVLPLLRYPLLVALVLRWSLSDSISICLTIYTLLINAFLIANSYIKRSGQVAWKSLREFKNGIVLITGGSKGLGRAIVSQLLQDYSNLTILNVDICPSSVRNTRVKDLICDLSDDEEVAALLNLLKRKYKNEIRLIVNNAGVRANFTGFNGMERDNLDKIFKINTFAPLQFIQELAPSRHSTRQCYIVNIASILGILTPAKVAAYAASKAALIAFHQSYSFELQNEGVRNIRTLLVTPGQLNTEMFAGFKPPRQFFAPVIDITTLAAKIVRYCELGQRGQLNEPFYCSFAHLLMCVPYSLQRIVRSFSRIDCCLPDE
The following text describes a protein:
Function:
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that acts in conjunction with A1 to repress transcription both of homozygote-specific genes and of genes necessary for the white-opaque switch, a prerequisite for mating.
Miscellaneous:
MISCELLANEOUS: The C.albicans mating-type-like (MTL) locus contains, in addition to the genes for the regulatory proteins (MTLA1, MTLA2, MTLALPHA1 and MTLALPHA2), a and alpha idiomorphs of a phosphatidylinositol kinase (PIKA and PIKALPHA), a poly(A) polymerase (PAPA and PAPALPHA) and an oxysterol binding protein-like protein (OBPA and OBPALPHA). MTLALPHA2 is not represented in the genomic sequence of strain SC5314 because that haploid assembly includes the mating type a allele of this locus; MISCELLANEOUS: Most C.albicans strains are heterozygous at the MTL locus and do not readily undergo white-opaque switching and mating, but mating occurs in hemi- or homozygous strains. Mating takes place in opaque cells, produces tetraploid progeny and seems to occur rarely, if at all, in nature. Conservation of mating capacity is rather thought to be due to the simultaneously regulated white-opaque switch, which seems to play an important role in host commensalism.
Subcellular Localization:
Nucleus.
Sequence:
MNSHSEALFEINQRLSSHIRTMSNFPVFDPQKITNDVEANIKRMTSILKSKRLTREDEDLMKMINDCSKVLHEMLLERIMLQQDSIQFFTEKEASDSPFSNSADTIDEDDDKKIKSRRLTKKQLLVLEGWFQKHKNHPYSQKDQTNLLIKSTKLSKSQVQNWISNRRRKEKNTKVSPELAALLLTG
The following text describes a protein:
Function:
May be involved in the recruitment of DRP2A to the accessory protein complex and in the negative regulation of its GTPase activity.
Subcellular Localization:
Cytoplasmic vesicle, clathrin-coated vesicle.
Sequence:
MDAFRRQASKLRDQVAKQQLAVIKQFSGTGYESSDVMVIDELEMQRHHQLDKLYRSTRSAKEFQRDIVKAAEAFTTIGLRHIEAGTKLSEDCCRYGNENSQNIDENILAKAAAIYGDARKHVDKEQEDFNKLLASQVLDPLRAMVAGSPLEDARHLAQRYSRMRQEAETHATEVSRRQARVREAPIPENVAKLQLAEAKMQELKANMAVLGKEATAALAAVESQQHRLTFQRLVAMVEGEKNYHLRIAAILSDIEAEMVTEKQHKESAPPAIPTENGSEKTSYFLAEVIHPFSAASEKELDLDKGDYIVVRKVSQTGWAEGECKGKAGWFPMAYIEKRQRLPTTNFAAEVY
The following text describes a protein:
Function:
Required for homeostasis of heavy metal ions such as cadmium, cobalt and copper. Controls metal ion transport and prevents metal hyperaccumulation by negatively regulating the SMF1 and SMF2 metal transport systems. Under manganese-replete conditions facilitates trafficking of SMF1 and SMF2 metal transporters to the vacuole where they are degraded.
Miscellaneous:
MISCELLANEOUS: Present with 3070 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum. Vacuole. Membrane; Multi-pass membrane protein.
Sequence:
MPEQELLIGQEMNTLHAGSSTDGINVGNAGRTRDTQTGVEGETEIGSDEEDSIEDEGSSSGGNSTTERLVPHQLREQAARHIGKIGRHFNILDRLFKKRTQQSSDIQQGAMFDGVFSNLSAKPDTTETEGNNEQDIPPTYDEAAADMAPSYYGMDLNNSDIYYDEICIEGLPVGNIANLLWNIIVSTSFQFIGFLITYILHTSHAAKQGSRFGLGLTFIGYGYSMIPNDVTSKVGKNKSLNRMELEDPNEFDDVRLNSQSTTQDKFESHLNHGLDEEKQNIPWLAVFVAFLGLFITLKSIYDYIQVKKLEKKYLNQSQNQA
The following text describes a protein:
Function:
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MADAARARRLAKRIAAIVASAIEYEIKDPGLAGVTITDAKVTADLHDATVYYTVMGRTLHDEPNCAGAAAALERAKGVLRTKVGAGTGVRFTPTLTFTLDTISDSVHRMDELLARARAADADLARVRVGAKPAGEADPYRDNGSVAQSPAPGGLGIRTSDGPEAVEAPLTCGGDTGDDDRPKE
The following text describes a protein:
Function:
Functions as a transcriptional regulator of the adaptive response to hypoxia. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Cytoplasmic in normoxia, nuclear translocation in response to hypoxia.
Domain:
The oxygen-dependent degradation (ODD) domain is required for cytoplasmic localization in normoxia.
Sequence:
MVSLIDTIEAAAEKQKQSQAVVTNTSASSSSCSSSFSSSPPSSSVGSPSPGAPKTNLTASGKPKEKRRNNEKRKEKSRDAARCRRSKETEIFMELSAALPLKTDDVNQLDKASVMRITIAFLKIREMLQFVPSLRDCNDDIKQDIETAEDQQEVKPKLEVGTEDWLNGAEARELLKQTMDGFLLVLSHEGDITYVSENVVEYLGITKIDTLGQQIWEYSHQCDHAEIKEALSLKRELAQKVKDEPQQNSGVSTHHRDLFVRLKCTLTSRGRSINIKSASYKVIHITGHLVVNAKGERLLMAIGRPIPHPSNIEIPLGTSTFLTKHSLDMRFTYVDDKMHDLLGYSPKDLLDTSLFSCQHGADSERLMATFKSVLSKGQGETSRYRFLGKYGGYCWILSQATIVYDKLKPQSVVCVNYVISNLENKHEIYSLAQQTAASEQKEQHHQAAETEKEPEKAADPEIIAQETKETVNTPIHTSELQAKPLQLESEKAEKTIEETKTIATIPPVTATSTADQIKQLPESNPYKQILQAELLIKRENHSPGPRTITAQLLSGSSSGLRPEEKRPKSVTASVLRPSPAPPLTPPPTAVLCKKTPLGVEPNLPPTTTATAAIISSSNQQLQIAQQTQLQNPQQPAQDMSKGFCSLFADDGRGLTMLKEEPDDLSHHLASTNCIQLDEMTPFSDMLVGLMGTCLLPEDINSLDSTTCSTTASGQHYQSPSSSSTSAPSNTSSSNNSYANSPLSPLTPNSTATASNPSHQQQQQHHNQQQQQQQQQQHHPQHHDNSNSSSNIDPLFNYREESNDTSCSQHLHSPSITSKSPEDSSLPSLCSPNSLTQEDDFSFEAFAMRAPYIPIDDDMPLLTETDLMWCPPEDLQTMVPKEIDAIQQQLQQLQQQHHQQYAGNTGYQQQQQQPQLQQQHFSNSLCSSPASTVSSLSPSPVQQHHQQQQAAVFTSDSSELAALLCGSGNGTLSILAGSGVTVAEECNERLQQHQQQQQQTSGNEFRTFQQLQQELQLQEEQQQRQQQQQQQQQQQQQQQLLSLNIECKKEKYDVQMGGSLCHPMEDAFENDYSKDSANLDCWDLIQMQVVDTEPVSPNAASPTPCKVSAIQLLQQQQQLQQQQQQQQNIILNAVPLITIQNNKELMQQQQQQQQQQQQEQLQQPAIKLLNGASIAPVNTKATIRLVESKPPTTTQSRMAKVNLVPQQQQHGNKRHLNSATGAGNPVESKRLKSGTLCLDVQSPQLLQQLIGKDPAQQQTQAAKRAGSERWQLSAESKQQKQQQQQSNSVLKNLLVSGRDDDDSEAMIIDEDNSLVQPIPLGKYGLPLHCHTSTSSVLRDYHNNPLISGTNFQLSPVFGGSDSSGGDGETGSVVSLDDSVPPGLTACDTDASSDSGIDENSLMDGASGSPRKRLSSTSNSTNQAESAPPALDVETPVTQKSVEEEFEGGGSGSNAPSRKTSISFLDSSNPLLHTPAMMDLVNDDYIMGEGGFEFSDNQLEQVLGWPEIA
The following text describes a protein:
Function:
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSDFLAYLTSAPSRPHGSANITDKCYDHQLRDLIAYLKQPGVAPSTADINGYLEAISPAVHSLSYLYLLRIRIQQLQEKTAVGVPNDLQPGGTLWNQTVKFLRSFDPIQIRYVGHEWRELVDSVANAALSVSKPILAVKMIRDALERLNTAGVFTSLHLMLVKLALLSSSYTYVLPVLDKLLCHFPSDTQNAHAGILLCSEHEPSTVFFTDSSGFSANLTYRDHLQFYMYSGMVYMALKKWDQASHCLGIVISAPTANSVSKIMVEAYKKWVLANLLGHGKLFSVPNLVAPHVTRVYQSLSKPYISLAEAFEKRDFQRLRTEISLGQTIWRADKNSGLVYQVFEAYDKFLIIKLGKTFSALTMPDVLQRASSCSKGSRDIEEFVVSLVMTKELRAKLSHSPGNETTTMLRFPLSSQSHALREEHIRFRLIQKEAALNTISRAITQTKITLETSHENLQVIAKNQKLAGSSERSGVVGSTEADGGGDLDEDLMGDGR
The following text describes a protein:
Function:
Auxillary component of the NALCN sodium channel complex, a channel that regulates the resting membrane potential and controls neuronal excitability.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTRGAWMCRQYDDGLKIWLAAPRENEKPFIDSERAQKWRLSLASLLFFTVLLSDHLWFCAEAKLTRARDKEHQQQQRQQQQQQQQQRQRQQQQQQRRQQEPSWPALLASMGESSPAAQAHRLLSASSSPTLPPSPGDGGGGGGKGNRGKDDRGKALFLGNSAKPVWRLETCYPQGASSGQCFTVENADAVCARNWSRGAAGGDGQEVRSKHPTPLWNLSDFYLSFCNSYTLWELFSGLSSPNTLNCSLDVVLKEGGEMTTCRQCVEAYQDYDHHAQEKYEEFESVLHKYLQSEEYSVKSCPEDCKIVYKAWLCSQYFEVTQFNCRKTIPCKQYCLEVQTRCPFILPDNDEVIYGGLSSFICTGLYETFLTNDEPECCDVRREEKSNNPSKGTVEKSGSCHRTSLTVSSATRLCNSRLKLCVLVLILLHTVLTASAAQNTAGLSFGGINTLEENSTNEE
The following text describes a protein:
Function:
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Subcellular Localization:
Cytoplasm.
Sequence:
MKDLLTRRFVLNSKEVREGDVFVAVKGKRFDGHDFIDEALRNGAYAIIAERKTVNSDRIFLVESSVDTLAKLAREKLGNFSGTVVGVTGSSGKTTTKEILYNLLKNKRSVFKTPGNMNTEYGLPLSILNDYKGEEILVLEMAASRPGDIAHLCKIAPPDVAVLLNVGSAHLEFFGTRERIMETKMEIIKHSKENAIAVTLFDDPDLRKEVPRYRNTLFFGKEGGDSVLKDWWYYEGSTIAEFEAFDSLFTVKLSGYWNGGQLLNIAASLCVMRTLGETVDIFDLASLKTVPGRFNVREKKGVLIVDDTYNASPEAFQTSIEALLRFPGKKFAVVGAMKELGERSKEFHEELGERLNVLDGVYVFLSEPEAEWIKSKKIILKSDDPEKIAKDLATRVKKGDVVLFKASRAVRIERVLEMFEKELEKR
The following text describes a protein:
Function:
Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon. Possesses both phosphatase and kinase activities. The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity.
Sequence:
MPHKRCNGEVAGEDAAERGPRTLRAEGALNAIVAGPVPQERLRVILEQALVFAGASFAALYAPGDDRELLCLVESAGVPRSLYGVRDSYPASGGSPVADAHRAGEAVWIGPEEFAGSAESRHVPSSGFSLAVLPVRGDGGGCLLALTERPDGFDTDDRTCLEAIAEAMTCPAPAETAARAETGDLQPDAFTLTMDSGRVEVGDGILRLFGLAPGEFDGKVETLLGLTVPEDLPSLMSVTESDHMTIGERELEFRVLQPTGPPKWLRLSGRLLPGGEGRPALLVGTVADASTLRPDVTDVARVQRLAAALATAGTVRDVSQAVVAALRRPLRADRIALAELENDRLVVTVLDPPDPESWPELWRLEWRTEWPDAPVRAMPTLAAALREGRARIWPAGTGDLEPALADVGPGGLAVLPLPAGGRMAGACLIGWDTPHDFGPDERALLTASAGLAGQALMRAHAFDAEHELVGMLQRQLLPRRLPKLPGAVAVARYLPSTAGLELGGDWYDVIPLPDHHVALVIGDVQGHSAGAATLMGQMRTALRAYAVEGHPPDVVVSHANRLLTGMETDLFATCVYVDLDMEEGSAWCVRAGHLPPVLRHPDGSTEIAEVEGGPPLGVVTQADFPMSPLRLRPGTLIALTTDGLVETPESDIDEGMDRFAHALAVSAPDHLGLVADALLGNARRNDDVALLLVRYDGMALRPLRESWSVWRLPEAVRHARRFTRRTLRTWGVPDDDIDGVLLIVSELVTNALVHTDGKVRLDLTLIGGRLRVAVADASPRTPVKPTSIGWEATGGRGILLVEAMSATWGTLPVSGGKQVWSEIPVGGG
The following text describes a protein:
Function:
May play a role in apoptosis. May act as a tumor suppressor.
Sequence:
MGATMVKPLVKNGNILDALPSQATLHVVMLGLDSAGKTTALYRLKFDQYLNTVPTIGFNCEKVQCTLGKAKGVHFLVWDVGGQEKLRPLWRSYTRCTDGILFVIDSVDTERMEEAKMELMRTAKCPDNQGVPVLILANKQDLPNACGAMELEKLLGLNELYNPVPNISMPSSSDSSPTINLIGCRVSNQSITDKSLEEKKESHLHSSMIHIKPALESKDHNSTLSGGALTAFIYPQSHNNSAVLDQKNPQDVKNGFHNKKMNRSSSNSVQFRGWYIQPTCAITGEGLQEGLDALYDMILKRRKINKSNKRNL
The following text describes a protein:
Function:
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAASMVRRLWPLVASRGLRLRGGYACNQSPRRSFATERRDRNLLYEHAREGYSALPQLDMEPLCAYPEEAARTLDLRKGELRSDDLPAIISTWQELRQLQEQIQSLEEEKRAVAEAVRALVVTQDNDQVQQDPRYQSLRARGREIRKQLVLLYPKEAQLEEWFYLRALRLPNQTHPDVPVGDESQARVLHVVGDKPAFSFQPRGHLQLAENLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTLQKLIHRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPSRFEDLNLAGTAEVGLAGYFMDHSVAFRDLPIRMVCSSTCYRAETDTGKEPRGLYRVHHFTKVEMFGVTGPGLEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLSAYRKFDIEVSPSGPRGGKEGDTVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPALQPYLGTDRITAPTHVPLQYIGPNQPQRTRPQGQAASG
The following text describes a protein:
Function:
Appears to partially substitute for Brp function in retinal biosynthesis during bacteriorhodopsin production. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGASPVALTPLTARARRTLARPALALGWVAISIAALPAITGVSLSPTARYAPLVASAVVFGMPHGAIDYLALPRAVTGTVTVRWLAVVGVLYLVLGGGYAAAWFFAPVPAAFAFVAITWLHWGQGDLYPLLDFLDVDYLDTRPRRAATVLIRGGLPMLVPLLGFPERYRSVVDAFAAPFGGSVGDLAVFDPRVRLWLGVAFAAATVAVLAAGRRRTHSPGAWRVDAAETLLLWVFFFVVPPVFAVGVYFCVWHSVRHVARAIAVDGSVHPSLRAGDILGPLARFGVEAAPMTAAALALGGVLWWAVPNPPTTLESGAALYLVLIAVLTLPHVAVVTWMDRVQGVL
The following text describes a protein:
Function:
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization:
Nucleus.
Sequence:
MASTSTDAGPADKVARLRVVNLEKQDSRVVKPKRQPRVNLAAKSLTKEERAQLKYAQFEPMYQLWLQYALQMMPEVSTKGKPEGDRLLRMEWLGAMLMVTEADNPSMVGLVGIVVLETKLTMQLITKKDKYLSKVYSSDLVIPKAGSVFQTAFRGKVLTLFGDAMRLRPSQRGRKSRLRQKLPFSLR
The following text describes a protein:
Function:
Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Subcellular Localization:
Secreted.
Sequence:
MHLAIKSLFVSLLGASVLASPLPSNALVERNAPLNEFLSALLSHLPAIDGTIDAVSGVITDFDQLLADLTGARTTQNGYIGVCTDYTVLFARGTSEPGNVGVLVGPPLSEAFEQAVGAKALSFQGVNGYNADVAGYLAGGDAAGSKSMASLASEVLSKCPDTKLVMSGYSQGCQIVHNAVEQLPAADASKISSVLLFGDPYAGKAFPNVDASRVHTVCHAGDTICNNSVVILPPHLTYAVDVTNAVQFAVAAAN