PharMolix/UniProtQA huggingface dataset:
Protein: MA7D1_MOUSE
Sequence: MESGPRVEPGPGAPAAVLARIPQEPRPSPEGDPSPPPPPTPMSALVPDTPPDTPPALKTATNPKQLPLEPGNPTGQISPQPAPPQEECPSSEAKSRGPTPTATGPREAKPSRRSSQPSPTTVPASDSPPAKQDVKKAGERHKLAKERREERAKYLAAKKAVWLEKEEKAKALREKQLQERRRRLEEQRLKAEQRRAALEERQRQKLEKNKERYEAAIQRSVKKTWAEIRQQRWSWAGALHHSSPGRKTSGSRCSVSAVNLPKHVDSIINKRLSKSSATLWNSPSRNRSLQLSAWESSIVDRLMTPTLSFLARSRSAVTLPRNGRDQGRGSGPGRRPTRARAGASLAPGPHPDRTHPSAAVPVCPRSASASPLTPCSAPRSAHRCTPSGERPERRKPGAGGSPALARRRLEATPVQKKEKKDKERENEKEKSALARERNLKKRQSLPASIRPRLSTGSELSPKSKARPSSPSTTWHRPASPCPSPGPGHALPPKPPSPRGTTASPKGRVRRKEEAKESPSPSGPEDKNHRKSRAAEEKEPAAPASPAPSPVPSPTPAQPQKEQSSTQIPAETAVPAVPAAPTAPPTAAPSVTPSKPMAGTTDREEATRLLAEKRRQAREQREREEQERKLQAERDKRMREEQLAREAEARAEREAEARRREEQEAREKAQAEQEEQERLQKQKEEAEARSREEAERQRQEREKHFQKEEQERQERRKRLEEIMKRTRKSEAAETKKQDAKETAANNSGPDPVKAVETRPSGLQKDSMQKEELAPQEPQWSLPSKEMPGSLVNGLQPLPAHQENGFSPKGTAGDKSLGRTAEGLLPFAEAEAFLKKAVVQPPQVTEVL
What are the official names of this protein?
MAP7 domain-containing protein 1.
What is the protein family that this protein belongs to?
Belongs to the MAP7 family.
What are the subcellular locations of this protein?
Cytoplasm, cytoskeleton, spindle.
Protein: GCH4_BURP0
Sequence: MNLMNPEFAMPDVQSTVDTRQMPIQRVGVRAVRHPLTVRTAEGETQATVGTWNLDVHLPADQKGTHMSRFVALLEERGGPLTADAFRTMLATMLEKLEARAGRIEVSFPYFVNKTAPVSGVRSLLDYEVTLTGDVRDGLTRVFAKVLVPVTSLCPCSKKISQYGAHNQRSHVTIDAELAADVPVEDLIRIAEEEASCELWGLLKRPDEKFVTERAYENPKFVEDLVRDVARRLDADERIVAYVLEAENFESIHNHSAYALIERDKRRGA
What is the function of this protein?
Converts GTP to 7,8-dihydroneopterin triphosphate.
What are the official names of this protein?
GTP cyclohydrolase FolE2.
What is the protein family that this protein belongs to?
Belongs to the GTP cyclohydrolase IV family.
Protein: LPXD_DESOH
Sequence: MKRSLEQIARLVSGRVVGDAAKKVSGAAPFEQAGPEEITLAGSAGFLKRIDQTGAGALVVPTDFTDSRRNLVAVENPAAAFARIRQMFDTGCRQPVGIDPRAVIGGGFACGEDVSIGPGVVIGDHVTLGDRVLLYPGVFLGNHVRIGNDGIIHANTSILRECVLGNRVIIHAGSVIGSDGFGFAPDGEMYVKIPHSGMVQIDDDVEIGAGNAIDRATFGRTWIRQGVKTDNLVHIAHNVTVGENTIIVAQVGIAGSTTVGRHVILAGQAGISGHLDIGDNAVVGPQAGIVKSIKPGETVSGTPGMPHKLWLRAQSIVAGLPGMRKKIAELEKRLAVLEKG
What is the function of this protein?
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor.  Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
What are the official names of this protein?
UDP-3-O-acylglucosamine N-acyltransferase.
What is the protein family that this protein belongs to?
Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
Protein: SRDE_NEUCR
Sequence: MAPQSTKFALITGCGAGGIGEALILEYLRRGIHPIATLLPFESSEHLDKAGITWFKLDVTNEESVVQLKKDVSELTKGRLDFLVNNAGICYTMTAIDTDVKSVQRMFDVNLFGPMRMVHHFHDMLIASSGIIVNIGSIGGVVPFVYGSSYNASKAALAHWGNSLRVELAPLGVRVLVIISGEVGTNILKNDHGRTLPEGSYYSPMAEEFKNHVHRTPDAATDRFVYAKNVVGESLKKSPTTWFWTGSYSGVIRFLHTFFPKTVFDRWFSSLFNLAKLKEAHDAAMKKKVA
What is the function of this protein?
Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sordarial, a salicylic aldehyde structurally related to the phytotoxin pyriculol (PubMed:19277664, PubMed:28485098, PubMed:30908040).  The most interesting aspect of this pathway is formation of an aromatic product from the highly reducing polyketide synthase srdA (PubMed:30908040).  SrdA synthesizes a reduced polyketide chain from one molecule of acetyl-CoA and five molecules of malonyl-CoA (PubMed:30908040).  The polyketide chain is then reductively released as an aldehyde (PubMed:30908040).  The oxidoreductases srdC, srdD and srdE then oxidize one of the hydroxy groups to facilitate the intramolecular aldol condensation, followed by dehydration to yield a salicylic aldehyde (PubMed:30908040).  This aldehyde can undergo facile reduction by endogenous reductases to yield the alcohol 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene (PubMed:30908040).  The flavin-dependent srdI counteract against the propensity of the aldehydes to be reduced under physiological conditions and is responsible for reoxidizing 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene back to the salicylic aldehyde (PubMed:30908040).  This salicylic aldehyde is then selectively epoxidized by the cupin-domain-containing oxidoreductase srdB to yield the epoxide, which can be hydrolyzed stereoselectively by the hydrolase srdG to give the final product sordarial (PubMed:30908040).
What are the official names of this protein?
Short-chain dehydrogenase srdE, Sordarial biosynthesis cluster protein srdE.
What is the protein family that this protein belongs to?
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
What are the subcellular locations of this protein?
Membrane; Single-pass membrane protein.
Protein: ARLY_CHLCH
Sequence: MSSKNKELLWQSRFSLPFDRDALRFSSSVHVDKALYREDIQGSIAHVTMLAEQQIVSHEEAQAIIAGLQEIELELRDGNIVPHWEDEDIHTVIENRLKEKIGAVAGKLHSGRSRNDQVATDTRLYLRRNIGSLQAALSELLTVLLQKAEHYCDTIIFGYTHLQRAQPISAGHYYMAYFTMFLRDRDRLQDLLKRVNISPLGAAAFAGSTLPLNPARSAELLGFEGIFSNSIDAVSDRDILIEFLSDCAMVMMHLSRFAEDVILWSSYEFGYLEISDAFATGSSLMPQKKNADIAELVRGKAGRVYGNLMAMLTIMKGLPLSYNRDMQEDKQPLFDSTETAINSVTIFSKMLENTRLKEERLAKLTSEDLSLATEIAEYLVQKHIPFRDAHRITGKIVSWSIESGVALPHIPLEQFKSFAAEFDEGIYACLKADASVRAKKTHGSCSFESVKQQINAAKERI
What are the official names of this protein?
Argininosuccinate lyase, ASAL, Arginosuccinase.
What is the protein family that this protein belongs to?
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: CYOE1_SHEB9
Sequence: MAKPLSITSSLPTFSVTWRAYFEMTKPKVVALMLLTVLVGMCLAVPHAVPVQPLLAGMLGIAMMAGSAAALNHLIDRRIDGLMARTYNRPLPKGRISATRALIFAASLGSLGFIVLYSLVNPLTAWLTFASLIGYALVYTAYLKRATSQNIVIGGLAGAMPPLLGWTAVTNEFHGHALLLVIIIFTWTPPHFWALAIHRRAEYAKVDIPMLPVTHGVEFTKTCILLYTVLLAIACLLPVLVGMCGPVYFVCSSLLSTGFIYKAWQLKYRDHDGLAMQVFRFSIYHLMLLFMALLLDHYLWN
What is the function of this protein?
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
What are the official names of this protein?
Protoheme IX farnesyltransferase 1, Heme B farnesyltransferase 1, Heme O synthase 1.
What is the protein family that this protein belongs to?
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: MTNN_COLP3
Sequence: MKAGIIGAMEPEVAILKEKLTDAKSTEHAGYTFHQGQLDGSDVVIVQSGIGKVAAALATAILIDRFQVDYVVNTGSAGGFDASLKVGDIVVSSEVRYHDVDLTAFGYEIGQLPANPAAFMPHDDLVAAAKKGIEQLSQTAGENIKAVTGLITTGDTFMTKEEDVAKARANFPTMAAVEMEGAAIAQACLQLKTPFVVIRSLSDIAGKESPHTFEEYLETAAVNSSQLVLNMLGQLKGKVLSAA
What is the function of this protein?
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively.  Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
What are the official names of this protein?
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, MTA/SAH nucleosidase, MTAN, 5'-deoxyadenosine nucleosidase, DOA nucleosidase, dAdo nucleosidase, 5'-methylthioadenosine nucleosidase, MTA nucleosidase, S-adenosylhomocysteine nucleosidase, AdoHcy nucleosidase, SAH nucleosidase, SRH nucleosidase.
What is the protein family that this protein belongs to?
Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.
Protein: NUOB_AERHH
Sequence: MKYTLTRIDPDAPVERYPQEQRQTVEDPLAQEASRGIMIGRLEEVLQDTVNWGRKNSLWPYNFGISCCYVEMCTAFTSPHDVARFGAEVIRASPRQADFMVIAGTPFIKMAPVIQRLYEQLLEPKWVISMGACANSGGMYDIYSVVQGVDKFLPVDVYIPGCPPRPEAFLQALMLLQDSIGKERRPLSWVVGDQGIYRPQMPAEKDRKRGERINVTNLRTPDEI
What is the function of this protein?
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.  The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone.  Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
What are the official names of this protein?
NADH-quinone oxidoreductase subunit B, NADH dehydrogenase I subunit B, NDH-1 subunit B.
What is the protein family that this protein belongs to?
Belongs to the complex I 20 kDa subunit family.
What are the subcellular locations of this protein?
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Protein: HIS6_BUCAP
Sequence: MLAKRIIACLDVNNGVVVKGIQFKNHEIVGDIISLSKRYTKEGIDELVFYDITASTNNKLVDRSWIKKVAEIINIPFCVAGGIKSVEDAQNILSFGADKISINSSALIDPDLITKIANRFGVQCTVVGIDSWFDSDKKKYMVQQYTGDANRTYQTDWETIDWVEKVQKKGAGEIVLNMMNQDGLQNGYDLSQLNEIRKKCKVPLIASGGAGCADHFYQAFDHANVDGVLAASVFHKKIVNIKDLKYFLIQKGLEIRIC
What is the function of this protein?
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate.  The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity).
What are the official names of this protein?
Imidazole glycerol phosphate synthase subunit HisF, IGP synthase cyclase subunit, IGP synthase subunit HisF, ImGP synthase subunit HisF, IGPS subunit HisF.
What is the protein family that this protein belongs to?
Belongs to the HisA/HisF family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: Y2058_ACTP7
Sequence: MDNVVLMPREKLLASGAESLTDQELLAIFLRTGIKGMPVMQLSQEVLNGFGSLRELLSADLATFCRMKGLGQTQFIQLQASKEMTKRYLAQQMQVRENINEPYLAVMCFQAELESEEREVFMVMFLDNQNRLIKKEKMFYGTINQATVYPREIIKEALKCNAAAIIVAHNHPSGNCTPSESDRALTKKLEMACDLVGIRFVDHIVVGKGDYFSFEEEKFR
What are the official names of this protein?
UPF0758 protein APP7_2058.
What is the protein family that this protein belongs to?
Belongs to the UPF0758 family.
Protein: AES_ECOL5
Sequence: MKPENKLPVLDLISAEMKTVVNTLQPDLPPWPATGTIAEQRQYYTLERRFWNVGAPEMATRAYRVPTKYGQVKTRIFYPQPDRPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGIDYTLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKVAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYSGMLHAFLHYSRMMKTADDALRDGARFFSDRLQQD
What is the function of this protein?
Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons).  Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate.  Negatively regulates MalT activity by antagonizing maltotriose binding.  Inhibits MelA galactosidase activity.
What are the official names of this protein?
Acetyl esterase.
What is the protein family that this protein belongs to?
Belongs to the 'GDXG' lipolytic enzyme family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: PNPH_ARCFU
Sequence: MIGIIGGTHILEIKVLKDVEETRIETPYGTAEIDVGRVDGIDVAIIQRHGKRKDKPPHRINHAANFYALKSLGVKYVIGMGSVGALREEYSLPSLIIPHDYIDFFSGVTIYNDSLVHVTPGFDEYLREVLVEVARKISSFPVIDKGVYFQTRGPRLETKAEIAMIKSFADCVGMTAGSEATIARELGLSYAIVCTMDNYAHGIKNQSIDYREIVEKAKENARECLKIVEEAVKKVWEEKIQRT
What is the function of this protein?
Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides.  Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules.  Involved in purine salvage.
What are the official names of this protein?
Probable 6-oxopurine nucleoside phosphorylase, Purine nucleoside phosphorylase, PNP.
What is the protein family that this protein belongs to?
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Protein: STTA_ASPTN
Sequence: MDTISDVMKHCVPINYDDYDPLPADHFSTYPVFCSKATAEAIEASAEFTRKWKRACEVDGLHQDKLNFQACTTHLGHYNQWAYPDCLPERVSLNAVLSDCAFFWDGMSPVTGRSTNVMITSPVDVSDSISAEKMNELTQDFGIAMLSELQSGRRIEPRFEINKMAVQVIRDFIAVDPFTGIGHLKEWKGHLDAQEKSTHNNMSWEKYVEHRVNESGGNWGISVGCWTNDIRISDEEKESVKYLTQLACAGGILGNDYYSFPKEFDEHHRSGTLDRLQNGVALLMREYGYTEEEAKEIIKKEVIIREKKWMDGFDAWSRQAGPETGEIRRYLVMTMALMSGSMFWMSHAGRYHRTDLATTAEDRATLIGKSRGALRVLAGYPPPKNLEGIVREPLASAVQDDNGHVQHKDAVADSSVRNGVHHAFKKRNSRNGKQNGTEGSKSTFTNGNYVQPAKLQQHGTSINSMAIYTAPFQEAAGDICDAPYSYIDSLPSKKNRNKLLDLLNDWLQVPPSSLKRIKNIVHMLHNSSLMLDDIEDASALRRGQPATHTFYGISQTINSANYVYVHAVHEVTRLYNPDADELRNLHRGQSLDLYWRHHARCPSMEEYIVMVDNKTGGLFRLMLRLMTAESSISRPLDTALCRLLTLTGRYYQIRDDYLNLASADYESKKGFCEDFDEGKFSLPLIHLLSHTRYPDRITSALFNRKPGTNLPYEMKRYILAEMEEVQTLAYSQDVLKYLHEELMHALDETENRLGANDGIRMMLLGMGPKLLLC
What is the function of this protein?
Sesterterpenoid synthase; part of the gene cluster that mediates the biosynthesis of aspterpenacids (PubMed:28604695, PubMed:34085529).  Performs both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and then converting GFPP into preaspterpenacid I (PubMed:34085529).  C22-oxidative modification of preaspterpenacid I by the cytochrome P450 monooxygenase sttB then leads to preaspterpenacid II.  It has still to be determined how preaspterpenacid II is further modified to produce aspterpenacids (PubMed:34085529).
What are the official names of this protein?
Preaspterpenacid I synthase sttA.
What is the protein family that this protein belongs to?
In the C-terminal section; belongs to the FPP/GGPP synthase family.
Protein: NCAP_I36A0
Sequence: MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDTTYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVLSFIKGTKVVPRGKLSTRGVQIASNENMETMESSTLELRSKYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDRTTVMAAFTGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDN
What is the function of this protein?
Encapsidates the negative strand viral RNA, protecting it from nucleases.  The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication.  The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex.  NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway.  Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins.  It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export.  M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals.  Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein.  Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
What are the official names of this protein?
Nucleoprotein, Nucleocapsid protein, Protein N.
What is the protein family that this protein belongs to?
Belongs to the influenza viruses nucleoprotein family.
What are the subcellular locations of this protein?
Virion. Host nucleus.
Protein: CACP_HUMAN
Sequence: MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSPGVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSCRVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSSLQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVYRSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIEYTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKDFPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVKAMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNAARLAHYLEKALLDMRALLQSHPRAKL
What is the function of this protein?
Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio.  Also plays a crucial role in the transport of fatty acids for beta-oxidation (PubMed:15099582, PubMed:29395073).  Responsible for the synthesis of short- and branched-chain acylcarnitines (PubMed:23485643).  Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates (PubMed:23485643).  Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates (PubMed:23485643).
What are the official names of this protein?
Carnitine O-acetyltransferase, Carnitine acetylase, Carnitine acetyltransferase, CAT, CrAT.
What is the protein family that this protein belongs to?
Belongs to the carnitine/choline acetyltransferase family.
What are the subcellular locations of this protein?
Endoplasmic reticulum. Peroxisome. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome.
Protein: ATP9_DEBHA
Sequence: MQLALAAKYIGASMATLGLGGAAIGIALVFVALINGTSRNPSLRATLFPQAILGFALAEACGLFCLMMSFLLLYAV
What is the function of this protein?
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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.  F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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.  Part of the complex F(0) domain.  A homomeric c-ring of probably 10 subunits is part of the complex rotary element (By similarity).
What are the official names of this protein?
ATP synthase subunit 9, mitochondrial, Lipid-binding protein.
What is the protein family that this protein belongs to?
Belongs to the ATPase C chain family.
What are the subcellular locations of this protein?
Mitochondrion membrane; Multi-pass membrane protein.
Protein: Y053_RICFE
Sequence: MKKLLLTASIICLASAGLAEENPTPVISNSDTEIKLEGFYLFESGYIKQDHLILFDKNVTDNRKKLGFYTEAAFAATISKTINDVIAGAKIVLQPTTRVKTSASYNGSHIFIETSYGKVELGSPVDASAKLRVTGSQVTAGTGGWYRYALLDGQYMRYNGLKPDFDTSASFYLESYSNSFDQINEKTEKARRLNFFTPKMKGFQAGISYTPDTANTGGNKDINNLTLESSGRNGVSVSRTGIKTVSLGNGETMTINQNIRDAFSAGLTYEHEISEDADLKLSVTGEYGKPARRLVHAKMEGTKVIEVLNTYKLSNLKAYNLGAVFTYGNFSCGASYGSLGKSLTAKEYYKVGRDTYYYNGAVAYGQGPIKTSLEYLKTSRYKNTVDAVSLATEYKIMPGLLPYAEISHFQAKGKPVYYPEAPSKTTRGTVGLIGTKLKF
What are the official names of this protein?
Uncharacterized protein RF_0053.
Protein: DAPB_BRASO
Sequence: MSRMRLIVAGAGGRMGRALVRAIADSDGAELAGALEAPGSELIGKDSGLLAGLPANNIKLSADLWAMSAEADGILDFTVPAATIANVAIAAERGIVHVVGTTGLSASDDAVIKSVTKRAIVVQSGNMSLGVNLLSALVKQVAKSLDANFDIEILEMHHKHKVDAPSGTALMLGRAAAEGRGITLDGHSARGRDGITGARRSGDIGFASLRGGTAAGDHSVIFAGPSERLVLSHQAEDRMIFAHGALKAALWAHGKPPGYYTMDDVLGLKDLF
What is the function of this protein?
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
What are the official names of this protein?
4-hydroxy-tetrahydrodipicolinate reductase, HTPA reductase.
What is the protein family that this protein belongs to?
Belongs to the DapB family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: SUMO1_PIG
Sequence: MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
What is the function of this protein?
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer.  Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4.  This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction.  Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2.  Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1.  Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.  May also regulate a network of genes involved in palate development.  Covalently attached to ZFHX3.
What are the official names of this protein?
Small ubiquitin-related modifier 1, SUMO-1.
What is the protein family that this protein belongs to?
Belongs to the ubiquitin family. SUMO subfamily.
What are the subcellular locations of this protein?
Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Cell membrane. Nucleus. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity).
Protein: GYRB_ECOLI
Sequence: MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI
What is the function of this protein?
DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state (PubMed:186775, PubMed:3031051, PubMed:1323022, PubMed:8248233, PubMed:7811004, PubMed:8621650, PubMed:9657678, PubMed:12051842, PubMed:12051843, PubMed:18642932, PubMed:19060136, PubMed:19965760, PubMed:22457353, PubMed:23294697, PubMed:20356737, PubMed:20675723, PubMed:23352267, PubMed:24386374, PubMed:25202966, PubMed:25849408).  This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E. coli (PubMed:9334322).  Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes (PubMed:22457352).  Relaxes negatively supercoiled DNA in an ATP-independent manner (PubMed:337300).  E. coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at comparable concentrations E. coli gyrase introduces more supercoils faster than M. tuberculosis gyrase, while M. tuberculosis gyrase has higher decatenation than supercoiling activity compared to E. coli (PubMed:22457352).  E. coli makes 15% more negative supercoils in pBR322 plasmid DNA than S. typhimurium; the S. typhimurium GyrB subunit is toxic in E. coli, while the E. coli copy can be expressed in S. typhimurium even though the 2 subunits have 777/804 residues identical (PubMed:17400739).  The enzymatic differences between E. coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box (PubMed:8962066, PubMed:16332690).
What are the official names of this protein?
DNA gyrase subunit B, Type IIA topoisomerase subunit GyrB.
What is the protein family that this protein belongs to?
Belongs to the type II topoisomerase family.
What are the subcellular locations of this protein?
Cytoplasm.