lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 8739 (MIC=50 ug), against Gram positive bacteria S.aureus ATCC 6538 (MIC=3.1 ug), methicillin-resistant S.aureus ATCC 43300 (MIC=12.5 ug), B.subtilis ATCC 6633 (MIC=12.5 ug) and against fungus C.albicans ATCC 90028 (MIC=50 ug).
Subcellular Localization:
Secreted.
Sequence:
MFTLKKSMLLLFFLGTINLSLCQEERDAEEERRDEDNAKMEEIKRGILGTVFKAGKGIVCGLTGLC
The following text describes a protein:
Function:
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Sequence:
MKNQDLVEYLRSCGVCEICQLRYLKARGAEYRNINETLQKLDVKLNENVENEELVISEGSQPSKRARLGVCSTCLGLFSKDFQNELLSSILASDFAKYDCQKIVLAICLPMSLQLRQLAMWFALRRRFGPSIDENNPPDVPIKEAVKLILHPIICEKLAKVYDANGLMINIDLTHSLEGEEVEKLVKLNKEAFPAKASHQKRIEISRGLLEKQYQPSKVKAETYEKYFQIPCSNVEESIKLTSIDLQGPLICVAGRYRKLSRELSHTPWILNGQRLMEDSIEEIIIRHVGPHFTEKLGKITFMSSGREDVDVRCLGKGRPFVLEIPNAKRSCLTKDEAFAMERAVDASGMVSIHHLQVVPREELTHIKTGEEQKKKFYRALCALQEPVSVKILEQLQISASFNIQQKTPIRVLHRRPLHTRPRTIYSVTAKVHRGNPKALIIDIVTQAGTYIKELVHGEFGRTTPSLSSIIGKPMDIQALDVVGIDLDWPHEVDNSKHKE
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). Involved in the control of cell division patterns during the early lateral root primordium development. Acts downstream of auxin signaling. Regulated by ARF7 and ARF19 in response to auxin. Co-acts with LBD16 and LBD18 to control lateral root development. Involved in the determination of floral meristem identity and suppression of bract growth. Required for proper conversion of secondary inflorescences to flowers. Acts together with NPR5/BOP2 and NPR6/BOP1 to promote expression of LFY and AP1, two central regulators of floral meristem identity.
Subcellular Localization:
Nucleus.
Sequence:
MSTSKTLDHNKPFETSQTQMGFALIHQNTSANTTTTTTTGERRGRRSKQAEPGRFLGVRRRPWGRYAAEIRDPTTKERHWLGTFDTAHEAALAYDRAALSMRGTQARTNFVYTPTDVHTILTNPNLHSLIVSPYNNNQSFLPNSSPQFVIDHHPHYQNYHQPQQPKHTLPQTVLPAASFKTPVRHQSVDIQAFGNSPQNSSSNGSLSSSLDEENNFFFSLTSEEHNKSNNNSGYLDCIVPNHCLKPPPEATTTQNQAGASFTTPVASKASEPYGGFSNSYFEDGEMMMMNHHEFGSCDLSAMITNYGAAAASMSMEDYGMMEPQDLSSSSIAAFGDVVADTTGFYSVF
The following text describes a protein:
Function:
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MLGTLGLWTLLPAAAQVSPNRRTCVFFEAPGVRGSTKTLGEVVDAGPGPPKGIRCLYSHCCFGIWNLTHGRAQVEMQGCLDSDEPGCESLHCDPVPRAHPSPSSTLFTCSCGTDFCNANYSHLPPSGNRGAPGPQEPQATPGGPIWMAQLLLGVFLVLLLSIIILALLQRKACRVQGGSDPEPEPGSGGDCSEELPELAELRFSQVIQEGGHAVVWAGRLQGEMVAIKAFPPRAVAQFRAERAVYQLLGLQHNHIVRFITAGQGGPGPLPSGPLLVLELYPKGSLCHYLTQYTSDWGSSLRMALSLAEGLAFLHGERWQDGQYKPGIAHRDLSSQNVLIREDRSCAIGDLGLALVLPGLAQPPALAPTQPRGPAAILEAGTQRYMAPELLDKTLDLQDWGTALQRADVYSLALLLWEILSRCSDLRPDHRPPPFQLAYEAELGSNPSACELWALAVAERKRPNIPSSWSCSATDPRGLRELLEDCWDADPEARLTAECVQQRLAALAYPQVASSFPESCPQGCPENCPAAPASAAFPCRPQQSSCLLSVQQGSGSKS
The following text describes a protein:
Function:
Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD-diaminopimelate-alanine bonds in high-molecular-mass murein sacculi.
Miscellaneous:
MISCELLANEOUS: In E.coli there are three murein endopeptidases: two are penicillin sensitive (DacB and PbpG), the other (MepA) not.
Subcellular Localization:
Periplasm.
Sequence:
MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQMAAAGQTAQND
The following text describes a protein:
Function:
Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEIFAFVPLAVLTALCVVISLFVKREKLVVFWLLWSGLIHIILEGSYGFFAHEVTKASTVSFTEKMLELVPLENAWNPHWYAQLYSQYAKYDLRYAIQDPMVVFFCFLELVQGAACFLLVICVIKQARIRHALQIFLCSIQGLGTVFYFITPYIYGLWEQQISSDPFELWVYVVGLNGLWLLVPIILTIQSFIAINKQFSIVESTTKDAKFISRKPKTA
The following text describes a protein:
Function:
Required for proper export of mRNAs from the nucleus to the cytoplasm.
Subcellular Localization:
Nucleus envelope. Nucleus. Cytoplasm. Nucleus, nuclear pore complex. Note=Part of the cellular SEH1 pool is not permanently associated with the Nup107-160 complex.
Sequence:
MAKSMATLDSGTTCSSWNQSGDRLAAGSLNGKLSIYESSTSSSSTFSCTSKVRVSESSIVKIVWLPSEYGDAVACVCEDGSLSIWEELSEDAHGLEWKLCKSMKNKSSQVLDVQFGVSRKSLKMVAAYSDGYLRVFELLNPLELKNWQLQAEFQNVIDSLSTLGKPSSLSASVSWNPMKGEEQEPSFVLAFNSDSPHLNSSKIWEFDEAHNRWLAVAELALPEDKGDPVYALSWAPNIGRPYEVVAVATHKGIGIWHVGLAPDLEGRLPVKKVSSLSGHQGEVWQMEWDMSGMTLASTGSDGMVKLWQSNLNGEWHEQATLEPVPS
The following text describes a protein:
Function:
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. In contrast to what is usually observed in eukaryotes for which one enzyme synthesizes the whole tRNA CCA terminus, in S.pombe, cca1 specifically adds two cytidine residues to a tRNA substrate lacking this sequence while cca2 specifically adds the terminal adenosine residue thereby completing the CCA sequence.
Subcellular Localization:
Cytoplasm.
Domain:
The B/A element (residues 122-124) is present in cca2 but not cca1 and is thought to position tRNA-NCC for terminal A addition; The absence of a C-terminal alpha-helix in cca2 as compared to cca1 might allow for binding of the tRNA-NCC substrate, or prevents binding of the tRNA-N or tRNA-NC substrates; The ERhxxExxxhh motif (residues 234-244) has been suggested to serve to distinguish between A-adding and CC-adding proteins as A-adding enzymes have a small amino acid in the first position while CC-adding enzymes have an E in the first position.
Sequence:
MYSRIVLNDVEKKVVNLLKKTADFIESKSSSSSSLEVRLAGGWVRDKLLGLSSDDLDVTLNKVTGVDFANSIFEYVHSLDSDSVIPYKDALGKLTVNPDQSKHLETATLSLFDLDIDFVGLRAESYDDKSRIPSVTPGTVETDALRRDFTVNTLFFNIRTEKIEDITKRGYKDLQTKVLVTPISPLQSFLEDPLRILRGIRFASRFEFTIDPSVVSAIQDPKVCKAFEKKVSKERVGEEIEKMLKGANAKLALQLLYSTNTYQFTFDTLPAEKEFQIPKALEATESLFQSLALTFPKLMKLSEDEKIGLWLYVALIPWSSQTVMVKKKQFYIPAIIAKDKLKLRSTYVNQLNQCCTFNPIFDELVNDTSTKNCSSIGSLIRQLNKSWEVVFLTSVIYSCCKTPAASVSNTFSSYKSLYDFIYDKNLQNAYNMKPLLDGKQIMKNVGVKPGPQLKETMDNMISWQFKHPEGSVEDCVAYLQSLKI
The following text describes a protein:
Function:
Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids. Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor. Can functionally replace FadD under anaerobic conditions.
Miscellaneous:
MISCELLANEOUS: Probably starts on Met-1; overexpressed protein starting at Met-19 has lower activity, forms aggregates during reaction and is unstable in storage at -80 degrees Celsius; MISCELLANEOUS: The enzymatic mechanism is a two-step reaction that proceeds via the intermediate formation of an acyl-adenylate (acyl-AMP) intermediate.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Note=Partially membrane-associated.
Sequence:
MHPTGPHLGPDVLFRESNMKVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLTQDVCEEIE
The following text describes a protein:
Function:
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Localization:
Nucleus.
Sequence:
MGDEDAPPATAGPSDKQKRPSYFNPKPPAIVPALIACHPHAPIVVVAIGAALRVLNYETGEALLLSDATIPRRHREAIRAIAFHPSGALFASGGDDKLVKVWDTATWTCRKTVSGPKKISSVVFSADARWLCFSDKYGIVHVTSTGGPGDAVDSAEAGIKQLLAHCSSIITSLAMSPDGRFIASADRDYKLRVSVFPATPLAGAPEIQSFCLGHTSYLTAALFLPGGLLVSAGGDGTLRLWQPQMGELLQTLRLAGEQEIAPVESVMSLDEGDSASESSGRAIVALALAPDGVSLAAALEGCSEVVFVHMVGEPPALVVAQRLSLGGRAPPTSLAFDAGGRVWRVAGAVQEIETGDAVVTEEALAAKEAAAAAAAASAAVQVELLQRRETGVSARERSAEPVGHGAGEEAASAAAVYEVGELPGGSAAQGVLEGSQADAQAAAEAAKAATEAMRNLLGKRMYTEAEKIDRKRNRNDQKPPRGKS
The following text describes a protein:
Function:
The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue.
Sequence:
MAGNSDPLTPRAKIAVTAGKAVAAASRAAGRGSGSVIGGRVALKLDPDLLGRLAGHLDVTLVSATNGKTTTTRLIAEALKAAGPVVSNALGANMPAGITSALAGGADARYGVIEVDEKYLVGVAQATDPKCIALLNLSRDQLDRAAETRMLAENWREGLAGSKAVVVANADDPLVVWAASSSPNVIWVAAGQMWKDDAWSCPSCGGVMQRPGDDWFCGECGFRRPTPSWALSGDHVLDPHGSAWPIHLQLPGRANKANAASSAAVAAVFGVPPQVALERMYQVQAVAGRYDVVQFQGRDLRLLLAKNPAGWLETFSLIDPPPAPVILSVNARGADGTDTSWLWDVDYTRLSGHPICVVGDRKLDLAVRLEVANQQFQVCEDLDQAVQLCPPGRIEVIANYTAFQDLRRRVGN
The following text describes a protein:
Function:
FMRFamides and FMRFamide-like peptides are neuropeptides. AQTFVRF-amide inhibits the activity of dissected pharyngeal myogenic muscle system (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MSLSGFEFSSIIAVLLLLIQLSSAAVLPVDYASQYGVASADEMTALPEEGSLFAERPAKRAQTFVRFGKRAQTFVRFGKRGQTFVRFGRSAPFEQ
The following text describes a protein:
Function:
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released.
Sequence:
MEFKFNVLDVIRKPISIFSSTELPKSQQALEKIVEIIDEVGIASAKAQGLRAPVTSILKLKHNPNQRIYIMRTDFDAKHNTKTGDQDSTDTLQSHQSKSIQLIDSRKQVVVGLLKVGLKKLFLVDEFGRQIEINALCVLDFYIHESSQRLGYGKRLFEYMLAIEFCSASELCYDRPSSKFLAFLKKHYDLHELLMHCFHGTTAIPQSNYFTVFKQFGLGLLELDSKGRPKPPLKLNPILKNTKHAHPTHPTPILRSEGLLQKFQHMTKNAPPITVKQLPSGNSINNPYDIMNIGSLTDKSAAQNNLNITSLYNTGSTKKFETQEHALLYQTQEIQPFKKQSKHEDNLHANNHDIFPPNSTFKETNMLNRSHHSKDKLSKLEVLSDEPHQHYNHSHHSHHHTHGHHTHHTLAKTVEHQTAQAQNEFTKNDIRYKNSTQHMGENENHAFLENPCSPKSQGTKSSSRFNRTQVVEKVASQAMVQEGTRQAGVLSRNDSKDILHLSEIGPYDSRVKKQHLDSIPIDPIDGPIDWTTTPHAGQTVSATMACFKTSPEIGIQEKERKARIRMLMQTERLPLLSPSALGNACVMPKPYLSGIALLAGGLGSFEKNYINTQRSEKHRQRLVKQSHNTKDF
The following text describes a protein:
Function:
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Subcellular Localization:
Cytoplasm.
Sequence:
MVKFSIEKKTILGRLGKIDSWGPVDVNHATPSCMTYLRAGHIPHLTWDVAENQLKLSQTPIYQMTLPSLISNAKIIEKFGKGVAKFVGMGALESPAIHLSPFDPLGKLPSGYNDSKSIAIWTANGKVSLDVKTYRNTVNSFGCGSFETLVDYDLPRDAGHKKLLKAVDRTTTFNEQIFKQDEKIDGERIVALGGGFSKYHRRKCAVDIGLAENTAAYTVEFHEFVEGMETDEMEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFAIKLAEEGHAFCLADDYPTSSKYEVVDFKDQEKFADDFTPVFDGCGCYTCTKYTKGYLQHLLNTKELLASILLVIHNMSEYDRMFKLIRKSLENSEGL
The following text describes a protein:
Function:
Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MMSDFSEELTKLAGAEDNPETSEFSKTRMHFPWLQKHIEAVVTGGKKRKDFAQTTSACLSFLQEALLKHQWCRAAEYMHSYLQTLEDSDTYRKQAAPEIIWKLGSEILFYHPKSNVETFSSFADRMKNIGVLNYLKISLQHALYLLHHGMLEDANRNLSEAETWRYGEKSASQEVLIKLVQAYKGLLQHYSWSKKKMELSELDEDDYAYTAKSRNMLSQSSKTSTNICTLIKTPGVWDPFVKSYVEMLEFYGDQDGARELLTNYAYDEKFPSNPNAHVYLYEFLKREKAPRAKLISVLKILHEIVPSHSLMLEFHTLLRKSETEEHRKLGLAVLFEVLDFSGCTKNITAWKYLAKYLKQTLMESHREWVEEEWKSRRNWWPAFHFSFFWAKSDWKADAELACEKAFVAGILLGKGCRYFRYILKQDHETLKKKIKRMKKSVKKYTIVNPGVHT
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum.
Sequence:
MAGKDLKSLIERLNLSSSKDEHSQVAAAYLELVANGCDDVCGALEKCVTALIKQDRYEQAMEVFAEYADVCKEGRFALLKLYTFYKLGQSAAFETEWAQVAEKVEASLAQDTVTAELRPLLHVRAQFDYKMGRYSDMFRTYKYLAAHNEEEADDGMELACNERVPLAFLPAEAVAEVSGKLVEDSYDMLLNESMVCSSKGQLEQAESLLKRALELARAEEVEDDVHTIQLQLAYVTQLLGRKKESRKLLTDLQKQVSAVSPLVSIIKTNLKSLDDLSRYSENSNLPLVLRELDAERLASSSSKTYSHDQWLRLQANLLFMRLFSNTIIRSKSTILSRTLAQYSKLVDNVCLESYTVQAKTLFDHVLSLIAKKDENAVGVLVLAVQLQLKAKNIGRAILLCEKYWENMAAESHKELVSSLLVHLYKQTRRKRSLLRHLAEITESFDPVNVRQSYDYWKFIGFQLLENQLGSARDVFAALAEVRPADSLVAKVLNPADQHELSEDMITDLVRDIDVEALIANGVDPLEASCRIPKASAGKVSKKRRTGKPKLPKAFDPEKQPDPERWLPLRDRSSYRPKKRHGKQTQGGVVDKRAESNLDITKQKKKPKQKKAGHR
The following text describes a protein:
Function:
Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Membrane raft. Cytoplasm, cytosol. Note=Palmitoylation is required for association with membranes.
Sequence:
MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE
The following text describes a protein:
Function:
May enhance MrpA stability, assembly, or function. May play chaperone or assembly roles for MrpA and perhaps for other mrp proteins; Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
Miscellaneous:
MISCELLANEOUS: Mrp-dependent antiport apparently occurs by a secondary, proton motive force-dependent mechanism, but the similarity of several Mrp proteins to membrane-embedded subunits of energy-coupled NADH dehydrogenase complexes raises the possibility that there is a capacity for electron transport that could provide a primary energy coupling option for Mrp functions.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MIETAKVVVAVFILLGALICLIASFGVLRLPDVFTRAHAASKGSTLGVNMILLGVFFYLWFVTGELSAKILLGILFIFITSPIGGHLICRAAYNSGVKLDERSVQDDYNGIRNFVIKRKEDSYL
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for maturation of extramitochondrial Fe/S proteins.
Sequence:
MATSSRFSSIVQLTDLDDFINPSQECIKPAKTANVKQVTSAGSAKIQIGDDGTYTQINKEGQPEKLEKAQITLNDCLACSGCITSAESVLIGQQNHTEFLKLCKEIQLSSESRMYDKIVVGLSSQPILSFANKFQVSPIEARAKLSALFRQLGAAKVFDVESFADMCLVECGHDFVQRFREKSTNATSVPVLASACPGWICYAEKTHGSWILPHISEVKSPQQIAATFIKDLLPNELQTDASRLAVVMIMPCFDKKLEASRSDFLREDQQTKDVDFVITPVEIEQILEELDVEFTDLDSSHVDHLSKAEIPTWNIPSGSGSGGYAEHVLRFAAKELYDVTLEHITFQPVKNSDIREAFLEMDGQQVLSVAICNGFRNIQNLVQKMKRKKRTYDYVEVMACPSGCLNGGAQLRLESNETKILLSNLEILHTKIEKHDIDETKADDLCHAWLGKSSIEERLKRLRTNYHAVQKSTNALTVKW
The following text describes a protein:
Function:
May act as a component of the cytoskeleton or as a chaperone for the reorganization of intermediate filament proteins during terminal differentiation in the lens. Does not seem to have enzymatic activity.
Sequence:
MLCIVYFILTCNFAPHGDLNWHLLVMANEINAVDLYETDFCEVDGSIISRIRRKMGVKVTGKYIPPLEWEKNNTSSSTRYLSWSPLDKDCTDTDNNKDAHIEKVSNRSAEPLLKDSREATDYPNYREEETFKTEEKHIMDKQQVESLQANTSQICLAKIKDAKGTSKYNFGKINDKLILFGPAIPKETLKEIKSISMERPSITNKCNIKYRPVATEIKLAKYYDTRTEKAGLTFETFRPTVQKSSQSLSIKNPEKKSLCESDYSSSESTEPVKRSLNENQSQIQEKSSTAAGKHLDHTSPDIYGHRSIGSKDLHCGKIGIPEPLYINSHIEVIKQQIAQEDIHFIRFEAPDLHGFPRSKTIPERYFHEKAVSGIHMPRSYLESNMNPKEPEIDHKRATYFNCDIVLKPELSTFRVLPWAEKTGNVICDAYTIMGDLLLTSPRYLAKHLLTQLQESGFSLHASFTYEFSIFGVAETVDSKQVVFPAATLVTDNDQSIIQELFDRMYYIGVDIESFCSSSTPGQMEVSFQPEYGLATADNAFTFRNGLKEVAKNYGYIASFYNDVSGIFNSGVFSHSLWDSSGTKNLFNDGNRVQKLTDIGKNWLSGLLLHSAALSCLVSPGESCRMHFAKGAKDLQQSIEVTYGFNDTSCSYNVKCHCSNGTYIENKLCSASANPYLVLREKQISRVFHLDHNM
The following text describes a protein:
Function:
Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K64-type polysaccharides of Klebsiella pneumoniae capsule.
Subcellular Localization:
Virion. Note=Tail appendage.
Sequence:
MSLSNLSSSNSNGAFLDYGEFRSGVYIQTSNQILYFTDENGNKVGYQWKGLLPHTTTTNDPSTDGGISDTAWCSIVGSGFIEKLSKEGIDLSWKAHLPTVEVSYNLPHKSLKIWEEGTNSTDNDYWLYPGDGTVWNGIGVLGDIPDAPFKQIVPQNNVIEWSAIATEGQNQFTVPYEFTNISVFINGLLQNKSTGGYVVNGSTVTLNGSLKAGDDIHVVISNIPIKNINYITDVELSQPDAAQKIGLLHGGNIQNLQNFLSFDMFNIDKTGSTDVTSQINNIFSLANQLNIPIKQHDGTYLVSGSTIFTINTDCDLSGVTILPSSNFTGYFLYTQNEQPTTYNSSSSLVTLINSATINANDSILYGLINDTTLDGNAIFMKGNDPLYVARGTTKNWWCNTRISNRGKMDDYLKYGVSGINEVISLPISKKVTTIKLPNWDFINQPANNGVIRFNNISRYRIHGGSVFNRPLNDINKDPVIISINYAYDIILQDFYDEYPSWPLVGGSIAYAYTINFNYINRVTFKDINSQGYGWGIVGGQLATNITYLRCNINRVDMHDPFMGYLKILDCDLGYYGVSATGMGDMYIERTTFNIDDLAFNGWREVDGIINTRPDFGGWFDGGVYIKDITIIGDASKFREINNRGVSLFSAYSYNATLSYIPNGSPVEPWGFKEIIVNGLRCTKPITGKRFSSLVYAASVQNVDYFPRHVKFNNCDFNSSDVECIDLHGWKITPDNSSKTSISNTMNFKSTNFIEFTDCSFVGLEILRPYSSYDYMNLELKLNNCKYIGSNISPISFYTDQVGNYEFTNCDINFISDTTKSTSSLSNRQSSFVINGGQINSVSVPFSILYNSGYSTPVLVNNTIFKGSFSQSSVTSINLNVAEFAQLSNCRFYSNVNNSYISPALWLGSTSNSATSITVMRGNKINTVITNTTTVSGISIKTDIIPFGVASGHINGSFYVDATGTTGTYQLYLNSLNLKSQIGKIVSNGTISGIYLQ
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MGFLWKTAKLGIKVGLVAGAVKLSIDNDIWSTNNVKGSELYQKLKKYILPGTVVFPQQLPTVEECQLKAGGTWNNAVDSVFTTIENVPSSVNTVANRLINNK
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Sequence:
MELACFNGFPETPSLSGSLVQQRHNLLDSVKSAGPPGPVFRVEFELFDDESPKTCANFRNLCAGRTTSRKGETYWFQGVVPSYRGTYFHKIIPQFCAQGGDLTMRVDNGANHLSSFGRGWFADEYKRRRMNEVGLLAMANNGPNSNGSQFFITTSDSNEKALNGRHVCFGRVVQGLKEFMHEVAPFGDSAGYPSRFIVVTDCGEGPLPATLGSTLPDKTPAADISEEGARECGRVSVKSPSGG
The following text describes a protein:
Function:
Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis. Has a role in chromosome segregation by recruiting condensin and ark1 kinase to appropriate sites as the cell progresses through mitosis. Ark1 activity depends upon bir1 function and phosphorylation. Ark1 with bir1 function is required for full-scale association with kinetochores and formation of a complex with mad3.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere. Note=Interacts with the outer centromeric regions of the chromosomes during interphase. After chromatid separation moves to the middle of the spindle.
Sequence:
MKPITSSSKRRWNRFRREMCNYSKRLDTFQKKKWPRAKPTPETLATVGFYYNPISESNSEERLDNVTCYMCTKSFYDWEDDDDPLKEHITHSPSCPWAYILSSKNNPNQNPQAAALTKCREQTFVDKVWPYTNRPDYHCEPSVMAASGFVYNPTADAKDAAHCLYCDINLHDWEPDDDPYTEHKRRRADCVFFTWKDPNSLSPTKLSFLSTSNIDPEDLTEDNSILPVSPTRDSTKSHKTLNFSPSRKNNLNARPLTMSLYTNTSEEKDSQPTRAPQSPTKPVLLTAPRRKNKSPKKSKPAVFKPVKPIFSDEDEDDDDLTASQPFSKGICNDSMQVAKKNFTEEIPLKEDEKDNELEHLVSPATSVHTTVSDITGHQSVTDESDEQNNCMSTPPKIEIESKIEEEISVVSKSKEISSSVSSVGKEQNHTEKQVAIETPEQQKVEKEDEHLNLQGSFIEESTKQPISSKPSTSSPDMTDAATGGRVSSSSFRDKILQTNFSPRSTIDSFSNISKKRNSEEANDENDETNLKIPIPEKKRKFQEVLQSKNILVSSTEDSHEPVKVTEDSQTAIHVSKFEDLENKSMESEQSLQLLSESENDDKPLIDLIPLLAIKRKDNLVSGVLEKGKSTSTSKTKFDTSIVDFIEKPKTEISEVLPEEKRKAICDESQTVRVSIDRGVTKTRDVSSPVSDEKSENVNHEEANSGHTVMNVHSSLDPQPIVQPNELESGSYLKDLPDRNVGNSEKVTFQEDDINSPKLQSKNNQTVEAVNTETSDKLQEKEANHELENIEKIEEKLTEVDKVSLSDAFPDQEIKNSRTSVQNGTRSVSKNTPEKETKVDKIDNVSKKDVETSPGSCETSSAFAKTYAEKEVTSINLPSVRKPLDESYYDHSISPFDPLCQSSFLAPQTPVKSKHALPLVEANAPPWEPIDFSSLLESPVPNPVEPNKLSEKELDMTVEQWIKFMYAKCAKEFEEACEEKIEWLLEEGKRAEEYIQNL
The following text describes a protein:
Function:
May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
Sequence:
MAFFKTFQQNLPSVSSLVDTISNAVEDLTAAVGEVGYTLTDSVAEQVTNMINGFRPEEESSAVAEVVADASEQANAVSPEFSKDTNCQKTQSSLDHRANRSGCYNTLVSQKQDQGMNEERVSTHTDDRQQSPPKPQDSSNAGSDSSLKGHLSDGGISVIKQNARAGSASQELERTDRCKKIGLGIPDNGKNLKEVRSQEMKENHLKKAEKHTKSKGSKGNEWSGNECSPKDILASNRHTIQKPTVKEDIHPALSANSRDKLHGKIKEQINPTAYYKVKGDIKIKKNEAISAHKGTARSKDEKYSKLIPGKDNSYMDKDEHGSSSESEDEALGKYHEALSRTHNSRLPLADSRQKNYAWETRQKYSPLSAEYDGYSSEASIDEGNCIQRMRRTPPLDELQPPPYQDDSGSPHLSCTPSEIGDSKCEFSHCSNSPRCSYNKCPSEGSTGHEVESFPNKGYEEDVPSDSTAVLSPEDMSAQGSSSQLPKPFDPEPEAKYGTLDVTFDYDSQEQKLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLPVILEPSYNHSGCDSQMSVSEMSCSESTSSCQSLEHGSVPEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNGLFCCLKHLIGGQVYIIRDTYVKLTLLNSMGQEMSKCKTSIRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNKRSMKRKEMIGWISLGLNSSGEEELNHWTEMKESKGQQVCRWHALLES