lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transport of uracil.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MESVDNNSFFSRIRNSNAYRKVKDFVILDHRPGMTMAERMLTNKDLYPVPPSKRLWGPWNFISFWLADAVNINTWMISATAIELGLNWWEAWICVWVGYLICGILVATTGRPGAVYHISFPVLSRSSFGTWGSLWPILNRSVLACVWYGVQAWIGGECVVLMIRSIWPSFSHIPNTMAKSGTETYQWVGFFIFWLLSNIAIWFPVHQIRHLFTFKAIVAPPAAIAFLIWALVKAHGAGPVIHEPTKLGQYEHAWVVINGIVTCIDGFATLIVNNPDFARFATTPGAVHWPQIITVPLAFGVTSLIGVLVSSASKAIYGTTLWDPTQLLASFLDHSNAHGVRAGVFFIAFGLCIAQLGVNIAANSVSAGNDLSALLPTVINVRRGGYIASIIALCMCPWNLLSSNNNFTTYLSSYSVFLSSFAGVIIADYYFVRKGLIRVAPLYSSSSSSPYYFWKGINFRAFASYICGMLINIVGMAGSTGQKVPKVANTMFNLNYFLGITVACLSHIIICKIFPVTECGEKMLSEVPEEADDYLLTLASEDSIDKDSTSEIYIDGLPTEKEVEKDDVLSITSKKLSGCFP
The following text describes a protein:
Function:
Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis.
Miscellaneous:
MISCELLANEOUS: Two distinct classes of crossovers have been demonstrated in budding yeast. Class I is MSH4/MSH5 dependent and exhibits crossover interference. Class II is MUS81/MMS4 dependent and exhibits no interference.
Sequence:
MSHEWLISASETMRSIGNGEGLRDKGAVVANNDGEFNEGDTNREEDSSTIFSFDFDEEIVMCIDFSGGKLGCSILDYHTKTLKAFDQDYVVNKTTISSHDLIDDADMSSNDISLLLGLLIMEANPTVCLVPARLEDWIFDYIKTKCDEINCRLELQPIKRFKKWDLLQSLQLRGHDNQTILNDILSNSKFTTTVTLGTVGCILANHEQLGEYNDSTASSNMVTGRLVQNAFEDVIHGIRYIDIRDRMVLDENTISALHIFPTAHKLGHDKMMRNGFFSVFELFNQVSSDYARRILKSWLINPLTNKKRIETRYSIIRTLLDKQNAIIFSDLSQSIKRCPDAFGFINQLRSGKSTLGTWSKVASFLEKGIAIFQLVSSLKLGSDEANILHDIKNKVDISALKECLRKVETVIDFDTSRDTKTLTINTGVDNRLDECRNIYNHLEGILLDVARETQIFLLNTMPQEDCKTTKSLEKLVNAVYIPQLGYLVTISVLMEPLLDGIPNLQWEEIFRSSENIYFKNGRVLELDETYGDIYGAISDFEIEILFSLQEQILRRKTQLTAYNILLSELEILLSFAQVSAERNYAEPQLVEDECILEIINGRHALYETFLDNYIPNSTMIDGGLFSELSWCEQNKGRIIVVTGANASGKSVYLTQNGLIVYLAQIGCFVPAERARIGIADKILTRIRTQETVYKTQSSFLLDSQQMAKSLSLATEKSLILIDEYGKGTDILDGPSLFGSIMLNMSKSEKCPRIIACTHFHELFNENVLTENIKGIKHYCTDILISQKYNLLETAHVGEDHESEGITFLFKVKEGISKQSFGIYCAKVCGLSRDIVERAEELSRMINRGDDVVQQCGNLTEKEMREFQKNQEIVKKFLSWDLDLETTTTSENLRLKLKNFLR
The following text describes a protein:
Function:
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
Sequence:
MLNKVFIIGRLTGDPVITYLPSGTPVVEFTLAYNRRYKNQNGEFQEESHFFDVKAYGKMAEDWATRFSKGYLVLVEGRLSQEKWEKEGKKFSKVRIIAENVRLINRPKGAELQAEEEEEVPPIEEEIEKLGKEEEKPFTDEEDEIPF
The following text describes a protein:
Function:
Probable ATP-dependent zinc metallopeptidase.
Sequence:
MGSFAARSPPISPSPSPSPIFPTARSLLFLRPFPPPSPTYRRGRRRFPRTTVFRASSSSAGDGSASFTWENFYESLRRGSARFTSSFGEHLKKETGIDLESANATAAVLVERTRDVTKKGLAAVDQFRSEWLSEFLEWNKWENWKDLRKWEPRRIGALILYIIVVSISSRKFYVALTSQINRQSKRELTEAYMEALIPEPSPANVRRFKKGVWRKTMPKGLKIMKFIEGPSGQLIQDNSYVGEDAWDEDPELPQDTISKIIDSDKKLSLEDKKSLKVNLSISDAVGTSVDGQESSTTWQERLSKWKEILQKEKLTEQIDSLNAKYVVDFDMQEVEKSLRKEVVERKSDTDASRALWISKRWWHYRPKLPYTYFLNKLDSSEVAAVVFSEDLKKIYVTMKEGFPLEYIVDIPLDPYLFEIVSSSGVEVDLLQKRQIHYFLKVVFALLPGLLILYLIRESVMLLYITNKRFLYKKYNQLYDMAYAENFILPVESSGETKSMYKEVVLGGDVWDLLDEIMIYMNNPMDYYEKQVAFVRGVLISGPPGTGKTLFARTISKESGLPFIFASGAEFTDSEKSGAARINEIFSIARRNAPSFVFVDEIDAIAGRHARKDSRRRATFDALMTQLDGEKEKTGVNRFSLRQAVIFICATNRPDELDAEFVRPGRIDRRLYIGLPDAKQRVRIFDVHSAGKKLAEDVDFGKLVFRTVGYSGADIRNLVNEAAIMSVRKDHSLITHQDIIDVLDKQLLEGMGVLLTEEEQQKCEARVSIETRRLLAVHEAGHILLAHLFPRFDWHAFSQLLPGGKETAISIFYPREDMVDQIQEYTTFGYMKMQMVVAHGGRCAERICFGDDITDGGRDDLKKLTKIAREMVISPRNSRLGLTTLVKRVRRMDRPDNPDGELIKFKWDDPNVIPADMTPEVSELFTRELTRYIEETEELAMKGLLQNRHILDAIAIELLEKSRITGLEADERVKQMSPVMLEDLAQPFQVNLDEDGPLPVNKHLQYQPLDIYPAPLHRC
The following text describes a protein:
Function:
Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Probably involved in the repression of many genes located in euchromatin, such as E2F1, MYC and CDC25A. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1. Mediates the recruitment of NIPBL to sites of DNA damage at double-strand breaks (DSBs) (By similarity).
Subcellular Localization:
Nucleus. Note=May be associated with microtubules and mitotic poles during mitosis (Potential). Associates with euchromatin and is largely excluded from constitutive heterochromatin.
Sequence:
MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCPELIEDFLNSQKAGKEKDGTKRKSLSDSESDDSKSKKKRDAADKPRGFARGLDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLTWHSCPEDEAQ
The following text describes a protein:
Function:
Putative odorant or sperm cell receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MHGDNKTFSSDFTLTGLFTNNKASGFLFSVICAIFFMAMIANGVMIFLIHIDPHLHTPMYFLLSHLSFIDMMFISTIVPKMLVDYLVGKGTISFFACTAQYFLYLGFVGAEFFLLGLMAYDRYVAICTPLRYPVVMSHRVCWVILTTSWFGGALDSFLLTPITMSLPFCASHKINHFFCEAPTMLRLACGDKAVYETVMYICCVMMLLIPFSVVIASYARLLIIVHQMKSAEGKKKAFATCSSHMMVVMLFYGAALYTYMLPQSYHTPVKDKVFSAFYTILTPLLNPLIYSLRNRDVSGALKRALARCQ
The following text describes a protein:
Function:
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription.
Subcellular Localization:
Nucleus.
Sequence:
MVKSVENGTSLPPFLVKCYEMVNDESTNELISWTESNDSFVIWDESKFASQLLPKYFKHSNFSSFVRQLNIYGFKKIDTDQWQFANESFVKGQKHLLKNITRRKQPQIPVHQNNPPQQKDTIAPQQSKQEEERRLALWKEVENLKTDKNALTQQLMKLSQHQQNSQSKMLLVRKQLQGMEKNQQQMLSFIVMAMQSPEFMVQFFQPKENNNNSNRKLSEVTDDCEPSDKMIVPYQPLKDDAPEASNLEDFMELDFSLDEMSDFFKDIDFPNDGSVGPSGNDEGRLVLPDISENDVMLEELLSSNPSTEIEEFAELDDDEIDNAFDKVEVITKKMGSLASEIR
The following text describes a protein:
Function:
In vitro catalyzes the phosphorolysis of D-kojibiose into beta-D-glucose 1-phosphate and D-glucose. No other disaccharides tested substitute for D-kojibiose. In the reverse direction disaccharides can be formed from beta-D-glucose 1-phosphate plus D-glucose, L-sorbose, D-sorbitol, L-iditol or 1,5-anhydro-D-glucitol, but with low efficiency. The beta-D-glucose 1-phosphate product is the substrate for YcjU (AC P77366), the next apparent enzyme in the putative biochemical pathway encoded in this locus (yjcM to ycjW).
Miscellaneous:
MISCELLANEOUS: Kojibiose does not support bacterial growth of K12 / BW25113 nor of BL-21(DE3), perhaps because it is not transported into E.coli.
Sequence:
MTRPVTLSEPHFSQHTLNKYASLMAQGNGYLGLRASHEEDYTRQTRGMYLAGLYHRAGKGEINELVNLPDVVGMEIAINGEVFSLSHEAWQRELDFASGELRRNVVWRTSNGSGYTIASRRFVSADQLPLIALEITITPLDADASVLISTGIDATQTNHGRQHLDETQVRVFGQHLMQGSYTTQDGRSDVAISCCCKVSGDVQQCYTAKERRLLQHTSAQLHAGETMTLQKLVWIDWRDDRQAALDEWGSASLRQLEMCAQQSYDQLLAASTENWRQWWQKRRITVNGGEAHDQQALDYALYHLRIMTPAHDERSSIAAKGLTGEGYKGHVFWDTEVFLLPFHLFSDPTVARSLLRYRWHNLPGAQEKARRNGWQGALFPWESARSGEEETPEFAAINIRTGLRQKVASAQAEHHLVADIAWAVIQYWQTTGDESFIAHEGMALLLETAKFWISRAVRVNDRLEIHDVIGPDEYTEHVNNNAYTSYMARYNVQQALNIARQFGCSDDAFIHRAEMFLKELWMPEIQPDGVLPQDDSFMAKPAINLAKYKAAAGKQTILLDYSRAEVNEMQILKQADVVMLNYMLPEQFSAASCLANLQFYEPRTIHDSSLSKAIHGIVAARCGLLTQSYQFWREGTEIDLGADPHSCDDGIHAAATGAIWLGAIQGFAGVSVRDGELHLNPALPEQWQQLSFPLFWQGCELQVTLDAQRIAIRTSAPVSLRLNGQLITVAEESVFCLGDFILPFNGTATKHQEDE
The following text describes a protein:
Function:
One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins.
Sequence:
MDPGELKLLKEFVTVCKANPEILHTPPLEFYKEYLESLDAKIPGPKETPSTSSGAASSEPSAQAPPAPEPEPEPEPEEPMDPESEESDLELDNEGVIEPDTDEPQPMGDTSKEVTDEMQDEANSKRSEAMAAVSEGNIEEAIKIFTEAIEINPHSALLHAKRASCFVRLNKPNAAIRDCDKGIDLNPDSAQVYKWRGKAHRLLGHWEEAFRDLQMACKLDYDESAYEMLKEVEPRAKKIVEHKRKYERKHQERELNEKKERIRKAKLAAEKARKEEEERRKREAEEGFPGGFPGGFPGGFPGGMPGGFPGGFPGGMGGGGMPGGFPGGMPGGMGGGMPGGMPGGMGGGMPGGMGGMPGGMPGGMGGMPGGMGGMPGGMPGGMPDISGIMSDPEILSAFQDPQVQEAFADISSNPANIAKYQNNKKITDLIAKMQSKVPRGAGGAGGPPGGPPSPPPPASGGGAPPQGEPSAPGASTQDID
The following text describes a protein:
Function:
Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
Sequence:
MTQTPARRTVLLCTGAGAAALCVGCGGGGDSSGASPGQELVRTGDVPVAGGKILTDEKIVVTQPRQGEFKAFSAVCTHQGCIVSDVRDGTIDCACHGSRFAVADGSVVRGPATEPLPGKRITVEGNSVRLA
The following text describes a protein:
Function:
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPRSLGNCQLNYSKERMWEPGYLKAKCAELRLESEFRLYRIRLWKSYLLTFFMLHIFVTSVHCALLLATIERRSIIYFDVALSIGCALVLILVLSVNFCDEFIAKHTWYMYASSIFASLTLVFADLTESIYHTYAHSWILGTFYDTYIIYMIYMFLPIHFISGAVLLALLVSGLYILYFVIFIAQGFAQFASALFSVGGMSVDIVHYLCLNLVGIFYRVMNDTVVRSSFLDRHQYIKEKIWLRNARLQEKQLLDSILPPQISLPLQKDIQGRIVMAKQGIHSWTAMERTMAIQIHPDVSILYADVVNYTHLTTTLTVEMLVKVLHDLYGRFDLAAYRYKVQRIKFLGDCYYCVAGLSDPDPDHANNCVILGLSMINHIMEVRDIHGLDINMRIGVHSGNLFAGVIGEAKLQFDIWGLDVTIANVLESTGVPGCVHISGATLNNLDVNRFDIEDGPEEARDHPLLKKYRIRSYIIRQDLHMDDEDSDEFLGDLHSISLCNMGAQPRISDSANQSLRALFHEELREEFRKMPVSAFSPKRLLGICRFNTGKEVPAHQNLNICLTFTDPILERAYLKQTDYMYKYSIILSASVGCSLVYIELMDTQMICSSCFVLPASVATIQCILALIAWYKKYCWTRYGRNNVPHHYNGFSCFIFRIHDKILNSLPIRICIYLFLMISSFFVMCLIVMSCQREEFEMAYIEERLFHYEQEAHICFHPWVTTNMLSLMICLTFTFAHIPIMVKTAVAILETLAYLLLIFFQFDFVFHHSVTTNPYFKSEYAHALLICITFLIMFVKERQIEFTNKVNFNWRVDLRKEENAASLTNHSIIIILNNILPSHIVDVYLNSLAKHELYFENYRMVSVMFAMLINFEMDLRSLRVLNEIIAEFDTLLLFYKEYYTVEKIKIVGCTYMAACGLDLNFAGSTSTNRKESIPPTEFNEEQSRRILFQQSNEDLDEVVFVMTSYALDMMRTLAKSNEAYQSIAGDRNITDGTIAIGISSGEVMAGIVGASQPHYDIWGNPVNMASRMESTGLPGHIHVTEETSEILQQFGITCSYRGMTFVKGRGKIPTYLVGIDENLNFIPQKATRFPSHQERSTVISLQSTYTHAENNNSIASTSRHTLQSL
The following text describes a protein:
Function:
Catalyzes the attachment of L-vancosamine to a monoglucosylated heptapeptide intermediate during the final stage of glycopeptide antibiotic vancomycin biosynthesis.
Miscellaneous:
MISCELLANEOUS: In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA (AC P96558), GtfB (AC P96559) and GtfC (AC P96560) are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD and GtfE (AC G4V4R9) are involved in biosynthesis of vancomycin.
Sequence:
MRVLLSVCGTRGDVEIGVALADRLKALGVQTRMCAPPAAEERLAEVGVPHVPVGLPQHMMLQEGMPPPPPEEEQRLAAMTVEMQFDAVPGAAEGCAAVVAVGDLAAATGVRSVAEKLGLPFFYSVPSPVYLASPHLPPAYDEPTTPGVTDIRVLWEERAARFADRYGPTLNRRRAEIGLPPVEDVFGYGHGERPCWPADPVLAPLQPDVDAVQTGAWLLSDERPLPPELEAFLAAGSPPVHIGFGSSSGRGIADAAKVAVEAIRAQGRRVILSRGWTELVLPDDRDDCFAIDEVNFQALFRRVAAVIHHGSAGTEHVATRAGVPQLVIPRNTDQPYFAGRVAALGIGVAHDGPTPTFESLSAALTTVLAPETRARAEAVAGMVLTDGAAAAADLVLAAVGREKPAVPA
The following text describes a protein:
Function:
ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MAVSKKSRKSEPSAAFTAADGLVLDQSEIMRAMLAAQKGKQKEESEGNDESDEEDDDVSNEGEDEGESSGSEAESSVAAQRNLKRRRSLSFELDAEGEEDKENEESEPRPQPSSGAGMLSRTALATKDMTPKPRSKPQPNGLASASKPSADVTFESLGLSHPLITALASINIKKPTEIQAACVEPILSGRDCIGGAKTGSGKTMAFALPIVERIARDPFGVWAVVLTPTRELAYQLSEQFLVIGKPLGLTTATIVGGMDMMKQAQELEARPHIIVATPGRLCDLLRSGGVGPGKLSRVRTLVLDEADRMLTPSFAPELAYLFSQIPAKRQTCLFTATVSEAIMELANKEPPAGKQRPFVYRVASDTLTVSNLKQKYLFIPSQIRDPYLLYILQNPLEDIDVALRVDPKKAKAREREAALGKKGKKPRQAKEEEDAPSVPSTVIFTQRCATAHLLHLLLNSLDIPSVPLHSHLTQPQRLLSLARFRAHEVPVLVTTDVGSRGLDIPEVAMVINWDCPRRSDDYVHRVGRTARAGRGGVAVTIITERDTELVKIIEDEVNVRLEELKLDEDKVLEGLNKVSLARRMATMEMHDSGFGERQATNKAKQIKRMKRDAAAAGKA
The following text describes a protein:
Function:
Mitochondrial outer membrane protein which regulates mitochondrial fission/fusion dynamics. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L.
Subcellular Localization:
Mitochondrion outer membrane; Single-pass membrane protein.
Sequence:
MAGSGERKGKKDDNGIGTAIDFVLSNARLVLGVGGAAMLGIATLAVKRMYDRAISAPTSPTRLSHSGKRSWEEPNWMGSPRLLNKDMKTGLSRSLQTLPTDSSAFDTDTFCPPRPKPLARRGQVDLKKSRLRMSLQEKLLTYYRNRAAIPAGEQARAKQAAVDICAELRSFLRAKLPDMPLRDMYLSGSLYDDLQVVTADHIQLIVPLVLEQNLWSCVPGEDTIMNVPGFFLVRRENPEYFPRGSSYWDRCVVGGYLSPKTVADTFEKVVAGSINWPAIGSLLDYVIRPAPLPEALTLEVQYERDKRLVIDFLPSVTLGDTVLVARPHRLAQYDNLWRLSLRPAETARLRALDQADSGCRSLCLKILKAICKSIPALGHLTASQLTNVILHLAQEEADWSPDMLADRFLQALRGLISYLEAGVLPSALNPKVLRENENRKPRTLRETFHPGCSSESSWSLKIHVPACCPGRLV
The following text describes a protein:
Function:
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular Localization:
Mitochondrion.
Sequence:
MVSFITNRLASGFTTLNKTGLISSLNNSTNGRLSILRHYSAYQKNLRNIGISAHIDSGKTTLTERILYYTGRIKEIHEVRGKDGVGAKMDSMDLEREKGITIQSAATYCKWGENHINIIDTPGHVDFTIEVERALRVLDGAVLVMCGVSGVQSQTITVDRQMRRYNVPRLVFINKLDRLGANPWNVIEQLKKKLNLNAVALQIPIGKEANLEDIPSGLAEFAREKKIELVETIANVDDQLGEWIIENDFPTNMPDEALLNEAIRRTTIARTVVPVCMGSAFKNTGVQPLLDSVIKFLPSPTDRKIVALDTSVKDKETEVELYTDPKKPFVGLAFKLEEGRFGQLTYIRVYQGTLKRGDMIKNVNLNKTIKVPRLVRMHANEMEEVQEVGAGEICAMFGVDCYSGNTFANQNLSYTMTSMHVPEPVMSLSIAPKTKDGQANFSKALSKFQKEDPTFRVESDQDSGQIIISGMGELHLEIYVERMKREYNVETVVGKPLVAYRETIQNRGDYSFTHKKQTGGQGQYAKMIGYAEPQENMENEFVNDVVGTAIPPNFVEAIRKGFNDSITKGPLIGHPVVGVKFVVNDGATHSVDSSELAFRIATAGAFREAFDEGTPSILEPIMKVEVAIPLEFQGPVISGINRRKGAITNTTSQGESVTFECEVPLNNMFGYSTELRSMTQGKGEFSMEYLKHNQVSRELFNTLTEEFKKKREEGNK
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MAQELSEKELLKMEVEQLKKEVKNPRALISKTGKEIKDYVEAEAGNDPLLKGIPEDKNPFKEKGGCMIS
The following text describes a protein:
Function:
Subunit f, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MASIVPLKEKKLMEVKLRELPSWILMRDFTPSGIAGAFRRGYDRYYNKYINVRKGSISGINMVLAAYVVFSYCISYKELKHERRRKYH
The following text describes a protein:
Function:
Part of the pafABC operon, however PafB does not seem to be involved in pupylation or substrate degradation. Appears to play at least a small role in resistance to reactive nitrogen intermediates (RNI) in vitro.
Sequence:
MATSKVERLVNLVIALLSTRGYITAEKIRSSVAGYSDSPSVEAFSRMFERDKNELRDLGIPLEVGRVSALEPTEGYRINRDAYALSPVELTPDEAAAVAVATQLWESPELITATQGALLKLRAAGVDVDPLDTGAPVAIASAAAVSGLRGSEDVLGILLSAIDSGQVVQFSHRSSRAEPYTVRTVEPWGVVTEKGRWYLVGHDRDRDATRVFRLSRIGAQVTPIGPAGATTVPAGVDLRSIVAQKVTEVPTGEQATVWVAEGRATALRRAGRSAGPRQLGGRDGEVIELEIRSSDRLAREITGYGADAIVLQPGSLRDDVLARLRAQAGALA
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MLTKFESKSARVKGLAFHPVRPWICASLHNGVIQLWDYRVGTVIDRFEEHDGPVRGVDFHLHEPLIVTGGDDYKIKVWDYKLRRCLFTLLGHLDYIRTVQFHPNATQFPWILSASDDQTLRLWDFHKRSCLSVLTGHNHYVMCAAFHPSEDLIVSASLDQTVRVWDTTGLRKKQLGGSGSAAHATAMNVQAELFGTNDVVVKYVLEGHDRGVNWAAFHPTLPLLASAADDRQVKLWRMSETKAWEVDTLRGHANNVSCCLFHPKQELVVSNSEDRSIRVWDVSKRVGVQTFRREGDRFWILAAHRSQNLLAAGHDSGMIVFKLERERPASANGPGDKLYYVRGRELFCHDYGRATGGSSGVDVPIASLRRVAQTDGIGSGPRFLSYNMHNPKEGNVLVCSEVDGGCYELITFSLTNAGGSVTDGKRGSCLGPGVFLGSNRFAVLDRHKREIVVKNMNNETTKRVAAPVPNVDCLYDGGASGRIILRADDRAVLFEVQSRRVLGELTAPKIKNVVWSPDGSKVALLCKYGVVIADRQLQQLCSISDTVRIKSGAWDVSPTGGTNSNLFIYTTLHHVKYCLPTGDTGTIRTLDNPIYATRVVKNQLFCLDREARSRVIIIDTTEARFKLALANKKAIMHMVRHSRLCGRAIVAYLQSKGFPEVALHFVRDPQTRFRLALACGNIEAAMESAFSLEQQKGIDGKSGDVWGELGSEALRQGNHQVVEMSYQRKKDFDRLSFLYMLTGDSEKLRKMLKISNMRNDIMGRYHNALLLGDASERVAVLEASGNLSLAYISAKLHGLDDVAERIKVAIETQEGSVPVGTKKGGRLLQPPTPIVRAGNWPTLEIKKTTLEDLSAADEGENFEEEAPAAQADTGASSAWDDGLDDAGLGAAAANDDFDMGDDDMGWGDDLDDLGDLGEADKPAHVDEMAGLDDIGDNVGFQMPPAGRPPAGCWAANSSHAADHMAAGGASSAMLLLHRQIAASDFTNLKSSMLSCYLGSTVSMPGIPGSGSVIVPLLRNDASGHPGNESLPRTSSTIKSLVAGVRSGYRSFQGGKFNDAKAAFEDVLSQIPITITENRNEANEMKEMLEICREYITAIRIKSAMADAGADPVRSTELSAYFTHCNLQPVHLLLALRSAMGTAFKHKNFIVAASFARRLLELPDMKSERNADLRMKATKVLQKSEQMARNEHTLNYNENAAFAIDCQDFVPIYSGEECVKCSYCGSSYKGSAMKGKICVTDGFCTVGVETIGLVTGK
The following text describes a protein:
Function:
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular Localization:
Mitochondrion.
Sequence:
MALLRPCLSNVLNRYKIITNRHVTCLNLLRKRHHYSGQAITAISDLLQDLGPQFYADGDKIRFLHQPTDFYQELLSKIKTAKKRITLASLYIGNGSLEQRMVDELQQVSRSSIQLNKPLDINILLDYTRGSRGKQNSRKMLLPLINESHSSVNVALFHTPHLRGPLKAIVPERFNETIGLSHLKVYLFDNDVIISGANLSDSYFVNRQDRYIVIEDNPEFANFFQDLITVVSKYSLQLQPDDTTKMLEDINVHPYENNDSSQEFINAMRSDIHQLLHKYKDSIKNNNLSKSNTVIFPLIQMGPFEVRFDEEATQRLFGSLRKDSTLLLASGYFNLIEKYLATILTKSKGDYKILTAAPEANGFYGASGIAGYIPDSYTYIAKQFYQRIVSENQDQRIKLLEYERQGWTFHVKGLWYYYQQEQLPSMTLIGSSNFGYRSTYRDLEAQIAVVTSESNLQELMKAEQESIFSYGKAVNQDVFRSDRRQVAFWAQMVTKYILWKFL
The following text describes a protein:
Function:
This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
Sequence:
MGRFGYAFQNYDATRHVRSSVREKDMSHKHAREVAVAIKGLSIEKARDYLQAVVNKDRAVAFRRYKNQVGHKADPGMMSGRYPQKTAREFIKVLDNLESNAEYKGMDLDRLKIVNATVHKGVIVKRFIPRAMGRATPKNNVLTHVELVAQEI
The following text describes a protein:
Function:
Essential for RNA editing. RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Subcellular Localization:
Mitochondrion.
Sequence:
MQLQRLGAPLLKRLVGGCIRQSTAPIMPCVVVSGSGVFLTPVRTYMPLPNDQSDFSPYIEIDLPSESRIQSLHKSGLAAQEWVACEKVHGTNFGIYLINQGDHEVVRFAKRSGIMDPNENFFGYHILIDEFTAQIRILNDLLKQKYGLSRVGRLVLNGELFGAKYKHPLVPKSEKWCTLPNGKKFPIAGVQIQREPFPQYSPELHFFAFDIKYSVSGAEEDFVLLGYDEFVEFSSKVPNLLYARALVRGTLDECLAFDVENFMTPLPALLGLGNYPLEGNLAEGVVIRHVRRGDPAVEKHNVSTIIKLRCSSFMELKHPGKQKELKETFIDTVRSGALRRVRGNVTVISDSMLPQVEAAANDLLLNNVSDGRLSNVLSKIGREPLLSGEVSQVDVVLMLAKDALKDFLKEVDSLVLNTTLAFRKLLITNVYFESKRLVEQKWKELMQEEAAAQSEAIPPLSPAAPTKGE
The following text describes a protein:
Function:
Involved in heavy metal homeostasis. Probably exports nickel and cobalt ions out of the cell (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTLTACEVTAAEAPFDRVSKTIPHPLSWGAALWSVVSVRWATVALLLFLAGLVAQLNGAPEAMWWTLYLACYLAGGWGSAWAGAQALRNKALDVDLLMIAAAVGAVAIGQIFDGALLIVIFATSGALDDIATRHTAESVKGLLDLAPDQAVVVQGDGSERVVAASELVVGDRVVVRPGDRIPADGAVLSGASDVDQRSITGESMPVAKARGDEVFAGTVNGSGVLHLVVTRDPSQTVVARIVELVADASATKAKTQLFIEKIEQRYSLGMVAATLALIVIPLMFGADLRPVLLRAMTFMIVASPCAVVLATMPPLLSAIANAGRHGVLVKSAVVVERLADTSIVALDKTGTLTRGIPRLASVAPLDPNVVDARRLLQLAAAAEQSSEHPLGRAIVAEARRRGIAIPPAKDFRAVPGCGVHALVGNDFVEIASPQSYRGAPLAELAPLLSAGATAAIVLLDGVAIGVLGLTDQLRPDAVESVAAMAALTAAPPVLLTGDNGRAAWRVARNAGITDVRAALLPEQKVEVVRNLQAGGHQVLLVGDGVNDAPAMAAARAAVAMGAGADLTLQTADGVTIRDELHTIPTIIGLARQARRVVTVNLAIAATFIAVLVLWDLFGQLPLPLGVVGHEGSTVLVALNGMRLLTNRSWRAAASAAR
The following text describes a protein:
Function:
Transcription factor that activates both viral and cellular genes by binding to the symmetrical DNA sequence 5'-CAGCTG-3'.
Subcellular Localization:
Nucleus.
Sequence:
MEYFMVPTQKVPSLQHFRKTEKEVIGGLCSLANIPLTPETQRDQERRIRREIANSNERRRMQSINAGFQSLKTLIPHTDGEKLSKAAILQQTAEYIFSLEQEKTRLLQQNTQLKRFIQELSGSSPKRRRAEDKDEGIGSPDIWEDEKAEDLRREMIELRQQLDKERSVRMMLEEQVRSLEAHMYPEKLKVIAQQVQLQQQQEQVRLLHQEKLEREQQQLRTQLLPPPAPTHHPTVIVPAPPPPPSHHINVVTMGPSSVINSVSTSRQNLDTIVQAIQHIEGTQEKQELEEEQRRAVIVKPVRSCPEAPTSDTASDSEASDSDAMDQSREEPSGDGELP
The following text describes a protein:
Function:
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Subcellular Localization:
Cytoplasm.
Sequence:
MSFIITVIGAGHAGLEAAFIVSKFNIKVNLLVLDINHLGSCPCNPSIGGPAKGIVTREIDVLGGMQAIAADNNALQYKLLNSSKGPAVQAIRAQIDKIGYKNWFQSQVKLNKNINLIQSEAINLIVRNEKIKGVILKDGSELLSDAVIITTGTYLRSKTYCGNTVKNQGPDQSKNSEKLSTNLINRGFKTIRLKTGTPPRILKTSLDYNQMELEINNNQNLAFSTTNKNFLPLEKQIPCYLVHTNQKIHDLILKNLKKSAMFNGSISAQGPLYCPSIEDKVFKFSQKPRHQIFVEPESLSLDTIYLAGLSTSFTPEIQKEIIQLLPGFQNAEIKKFGYAIEYDAFLSNQLKPTLETKLIENLYFAGQINGTSGYEEAAGQGLMAGINAALKLLKKPPFILQRNEAYIGVMINDLVTKTISDPYRLLTSRAEYRLWLRNDNVQERLIKKSFELGLTDKKTYELFLKKEKKKQELISFLKNTQVGKVKALKFTNKNTAQSLYDFNKRSEINLDKLIKDLPEKYQLDSETLKQIEIEIKYEGYIKKNEKYFKGLDKLSKIKIPHTFDYHKVKNLASEAIFKLSNFKPSNLAIASQIAGVNFNDIIAIKHFLKTYE
The following text describes a protein:
Function:
GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle.
Subcellular Localization:
Nucleus.
Sequence:
MFNHPGFKLLIVGDEGTGKTTFVKRLLREDFEEIYEPTTGVKVYPLLFFTNRGMIRFDCSDTPGQGLRDGYYIRGQCAIIMFDVTAGSTYMNVPGWHRDLCRVCENIPIVLCGNKVDVQNRQLEARQFTYGWSNNSPHFEISARSMYNLEEPFLYLARELVGDPNLHFVEPPALAPPEVHMGFQALPNQPMFNHPGFKLLMVGDPGTGKTTFLKRLIPGEFENRYEPTTGVEFYPLDFLTNKGTIRFNCWDTPGQGLRDKYYIRGQCAIIMFDVTAGSTYMNVPGWHRDLCRVCENIPIVLCGNKVDGENRQVEARQFTFGCRNNLQHYEISARNMYNLEEPFLYLARELVGDPNLHFVELPALAPPAVHMDFAPQQQHEAELAEAAIRPLPDGARKPVFRLGDSNGHSRRQVVSACILAILEFYIGDGRCSHFFGFAKLHNCFRLIYQIDLNFGKHVLIVNSIHIFLDNCSTWMLSRVLNRRVGLKMVRSKLIHLICIDPFLCNTILIICTRPDLYCCNASI