wanglab/gogpt-training-data huggingface dataset:
Protein: Chromosome partition protein MukB (Structural maintenance of chromosome-related protein) (P22523)
Organism: Escherichia coli (strain K12)
Function: Plays a central role in chromosome condensation, segregation and cell cycle progression. Functions as a homodimer, which is essential for chromosome partition. Involved in negative DNA supercoiling in vivo, and by this means organizes and compacts chromosomes. May achieve or facilitate chromosome segregation by condensation of DNA from both sides of a centrally located replisome during cell division. Stimulates both DNA relaxation and to a lesser extent decatenation activity of topoisomerase IV.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:11886550, ECO:0000269|PubMed:22380631}. Note=Restricted to the nucleoid region, far from the cell poles.
Interaction partners:
- Chromosome partition protein MukF
- DNA topoisomerase 4 subunit A
- Chromosome partition protein MukE
- Macrodomain Ter protein
- Negative modulator of initiation of replication
- Acyl carrier protein
- tRNA 5-carboxymethoxyuridine methyltransferase
- Methylmalonyl-CoA decarboxylase
- Methylmalonyl-CoA mutase
- Cell division protein FtsZ
Sequence:
MIERGKFRSLTLINWNGFFARTFDLDELVTTLSGGNGAGKSTTMAAFVTALIPDLTLLHFRNTTEAGATSGSRDKGLHGKLKAGVCYSMLDTINSRHQRVVVGVRLQQVAGRDRKVDIKPFAIQGLPMSVQPTQLVTETLNERQARVLPLNELKDKLEAMEGVQFKQFNSITDYHSLMFDLGIIARRLRSASDRSKFYRLIEASLYGGISSAITRSLRDYLLPENSGVRKAFQDMEAALRENRMTLEAIRVTQSDRDLFKHLISEATNYVAADYMRHANERRVHLDKALEFRRELHTSRQQLAAEQYKHVDMARELAEHNGAEGDLEADYQAASDHLNLVQTALRQQEKIERYEADLDELQIRLEEQNEVVAEAIERQQENEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYNQAIAALNRAKELCHLPDLTADCAAEWLETFQAKELEATEKMLSLEQKMSMAQTAHSQFEQAYQLVVAINGPLARNEAWDVARELLREGVDQRHLAEQVQPLRMRLSELEQRLREQQEAERLLADFCKRQGKNFDIDELEALHQELEARIASLSDSVSNAREERMALRQEQEQLQSRIQSLMQRAPVWLAAQNSLNQLSEQCGEEFTSSQDVTEYLQQLLEREREAIVERDEVGARKNAVDEEIERLSQPGGSEDQRLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPSRHAIVVPDLSQVTEHLEGLTDCPEDLYLIEGDPQSFDDSVFSVDELEKAVVVKIADRQWRYSRFPEVPLFGRAARESRIESLHAEREVLSERFATLSFDVQKTQRLHQAFSRFIGSHLAVAFESDPEAEIRQLNSRRVELERALSNHENDNQQQRIQFEQAKEGVTALNRILPRLNLLADDSLADRVDEIRERLDEAQEAARFVQQFGNQLAKLEPIVSVLQSDPEQFEQLKEDYAYSQQMQRDARQQAFALTEVVQRRAHFSYSDSAEMLSGNSDLNEKLRERLEQAEAERTRAREALRGHAAQLSQYNQVLASLKSSYDTKKELLNDLQRELQDIGVRADSGAEERARIRRDELHAQLSNNRSRRNQLEKALTFCEAEMDNLTRKLRKLERDYFEMREQVVTAKAGWCAVMRMVKDNGVERRLHRRELAYLSADDLRSMSDKALGALRLAVADNEHLRDVLRMSEDPKRPERKIQFFVAVYQHLRERIRQDIIRTDDPVEAIEQMEIELSRLTEELTSREQKLAISSRSVANIIRKTIQREQNRIRMLNQGLQNVSFGQVNSVRLNVNVRETHAMLLDVLSEQHEQHQDLFNSNRLTFSEALAKLYQRLNPQIDMGQRTPQTIGEELLDYRNYLEMEVEVNRGSDGWLRAESGALSTGEAIGTGMSILVMVVQSWEDESRRLRGKDISPCRLLFLDEAARLDARSIATLFELCERLQMQLIIAAPENISPEKGTTYKLVRKVFQNTEHVHVVGLRGFAPQLPETLPGTDEAPSQAS
Protein: Probable cytosol aminopeptidase (EC 3.4.11.1) (Leucine aminopeptidase) (LAP) (EC 3.4.11.10) (Leucyl aminopeptidase) (P9WHT3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aminopeptidase N
- Glutathione hydrolase proenzyme
- Probable gamma-glutamyltranspeptidase GgtB
- Glutamate--cysteine ligase EgtA
- Putative glutamate--cysteine ligase 2
- Probable zinc metalloprotease Zmp1
- Uncharacterized protein Rv2212
- Aminomethyltransferase
- O-acetylserine sulfhydrylase
- L-cysteine desulfhydrase Cds1
Sequence:
MTTEPGYLSPSVAVATSMPKRGVGAAVLIVPVVSTGEEDRPGAVVASAEPFLRADTVAEIEAGLRALDATGASDQVHRLAVPSLPVGSVLTVGLGKPRREWPADTIRCAAGVAARALNSSEAVITTLAELPGDGICSATVEGLILGSYRFSAFRSDKTAPKDAGLRKITVLCCAKDAKKRALHGAAVATAVATARDLVNTPPSHLFPAEFAKRAKTLSESVGLDVEVIDEKALKKAGYGGVIGVGQGSSRPPRLVRLIHRGSRLAKNPQKAKKVALVGKGITFDTGGISIKPAASMHHMTSDMGGAAAVIATVTLAARLRLPIDVIATVPMAENMPSATAQRPGDVLTQYGGTTVEVLNTDAEGRLILADAIVRACEDKPDYLIETSTLTGAQTVALGTRIPGVMGSDEFRDRVAAISQRVGENGWPMPLPDDLKDDLKSTVADLANVSGQRFAGMLVAGVFLREFVAESVDWAHIDVAGPAYNTGSAWGYTPKGATGVPTRTMFAVLEDIAKNG
Protein: Phospholipid scramblase (Q21319)
Organism: Caenorhabditis elegans
Interaction partners:
- Cell death abnormality protein 8
Sequence:
MNIQPGQLPLKAISLTSAVKSPEEVEQDSKKDEPRAEGAGFGRRNNAGTKLPAARSTPMKIPNQVAAMPVQMTGFVQLASNNILSAIAHTNSLMVVQCIEPLEIFTGFETPNRYVVHDMYCRPLLYCMERSNVFARQYHGNNRNFGMQIMDTHGAQVMTCFRGRPCCSCDDFLSTQFLDQQIGMMKRECCNPNFELIGSGCNQPLLIQSPVCAGCGGTQKFPVMTYNGALVGEIVRLYPGFMQEMFTDADTYIVHFPMDMPPILKLLLVTSVFLIDFTYFEDRNQDRHHHGGMHGGMHSSF
Protein: 2-methylcitrate dehydratase (2-MC dehydratase) (EC 4.2.1.79) ((2S,3S)-2-methylcitrate dehydratase) (Aconitate hydratase) (ACN) (Aconitase) (EC 4.2.1.3) (P77243)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate. It is also able to catalyze the dehydration of citrate and the hydration of cis-aconitate at a lower rate. Due to its broad substrate specificity, it seems to be responsible for the residual aconitase activity of the acnAB-null mutant.
Interaction partners:
- 2-methylcitrate synthase
- 2-methylisocitrate lyase
- Propionate--CoA ligase
- Aconitate hydratase B
- Propionate catabolism operon regulatory protein
Sequence:
MSAQINNIRPEFDREIVDIVDYVMNYEISSKVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQFQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAVASGKAPLTMKQVLTAMIKAHEIQGCIALENSFNRVGLDHVLLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAKTGEMGYPSALTAPVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAGKTAADIEKVTIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEKRAIANAITLEFTDGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRARLEQMPVNEYLDLYVI
Protein: DgcB, Dimethylglycine catabolism (Q9HTG5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- DgcA, Dimethylglycine catabolism
- Glycine betaine monooxygenase reductase subunit
- Glycine betaine monooxygenase oxygenase subunit
- 4-vinyl reductase 4VR domain-containing protein
- Electron transfer flavoprotein alpha/beta-subunit N-terminal domain-containing protein
- Probable electron transfer flavoprotein alpha subunit
- Membrane dipeptidase
- Sarcosine oxidase alpha subunit
- Sarcosine oxidase gamma subunit
- Glutathione-independent formaldehyde dehydrogenase
Sequence:
MLDTLLPVLLFAALALAVLGAAKRFLMWRRGRPAKVDWIGGLLQMPRRYLVDLHHVVERDRYMSRTHVATAGGFVLAALLAILVHGFGLHGRILGFALLAATALMFVGALFVARRRLDPPSRLSKGPWMRLPKSLLAFAASFFLATLPVAGILPEGFGGWFLAGLLAIGVAWGVSELFLGMTWGGPMKHAFAGALHLAWHRRAERFGGGRSTGLKALDLADPQAPLGVEKPSDFTWNQLLGFDACVQCGKCEAMCPAFAAGQPLNPKKLIQDMVIGLAGGNDAKFAGSPYPGKPLGEHGGGPHQPIVALDGKALVDADTLWSCTTCRACVEECPMMIEHVDAIVDMRRHLTLEKGATPNKGAEVLDNLIATDNPGGFAPGGRLNWAADLNLPLMSEKKSADVLFWVGDGAFDMRNQRTLRAFVKILKAAAVDFAVLGLEERDSGDVARRLGDEATFQNLARRNIATLAKYRFTRIVSCDPHSFHVLKNEYGALGGDYQVLHHSTFIDELLRAGTLQPGRSKAGSVTYHDPCYLGRYNGEYEAPRNVLRALGIEVKEMQRSGFRSRCCGGGGGAPITDIPGKQRIPDMRMADIRETGAELVAVGCPQCTAMLEGVVAPRPEIKDIAELVAEALIEQAEAPAKKPLRREAVAEVH
Protein: Autophagy-related protein 14 (O42862)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific vps34 PI3-kinase complex I. This complex is essential to recruit the atg8-phosphatidylinositol conjugate and the atg12-atg5 conjugate to the preautophagosomal structure. Atg14 mediates the specific binding of the vps34 PI3-kinase complex I to the preautophagosomal structure (PAS) (By similarity).
Subcellular location: Cytoplasm. Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein atg6
- Vacuolar protein sorting-associated protein 38
- Serine/threonine-protein kinase vps15
- Phosphatidylinositol 3-kinase pik3
- PtdIns3K complex I subunit atg38
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Vacuolar segregation protein 7
- Protein VAC14 homolog
Sequence:
MLHVNKCQLCETRRPSICESCLKKQLYDFYHKRDEFSRDIESELEKVAKLKSESFSLKGKITQKEELTYRLQNLAASLNEKKSLSCDLHSRKQLIEDDLSNRKKSINIASQKLAGLSHSTSDYFSKEYLTAYRRSELLQNKLHEYQKKLITRVLDMYQLHWQRDLVLNTQGCTQKSAQMGSEFNPDSIDSSLAYRLSKLSMGNSKSDLSHSDNETGHFYSNFFSQVMELNASVTISGIPVCIRSKEKMFLNPDCALTLSFICIFLAQYTSIPLPCPLQLPSPDQKPMTSFSSEQMLYIMYNIVWISWNCGIFSFPRGITQSQLFELMQYTGFWLVQLRTKPLTSQKPDWHYKMGMDFDLFHRLYLARLPIPINYSSLRSRSSSKPYQLIS
Protein: AAA-type ATPase family protein (Q8RXI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Kinesin-like protein KIN-10B
- Carbon-sulfur lyase
- At5g67310
- Metallothionein-like protein 2B
- Probable E3 ubiquitin-protein ligase ARI14
Sequence:
MAQKIAIGVISALAASASLAPSKFAAADGPFTFSGFSTSPSASIPQQQGSTPPASESGKEPSVAGEESDAPPRIRNNNPRTTSAGFDPEALERGAKALKGINNSAHAKKVFESIKTREETRQAEFTAKAQEFKAMQSQAEAERQRVIYEEQKKLAQHQAQTKSQMARYEDELARKRMQAENEAQRTRNQELVKMQEESAIRREVARRATEEEIQAQRRQTEREKAEIERETIRVKAMAEAEGRARESKLSEDVNRRMLVDRANAEREKWVSAINTTFDHIGGGLRTILTDQNKLIVAVGGLTALAAGIYTTREGAKVIWSYVDRILGQPSLIRESSRGKYPWSGSASRVLSTLRGGGKESTSKTGKGFGDVILRPALEKRIEQLANATANTKAHQAPFRNILFYGPPGTGKTMAARELARRSGLDYALMTGGDVAPLGAQAVTKIHQLFDWSKKSKRGLLLFIDEADAFLCERNKTYMSEAQRSALNALLFRTGDQSKDIVLALATNRPGDLDSAVADRIDETLEFPLPGEEERFKLLNLYLEKYISKTNLKKPGLLQSLFKKEQQTIEIKGVTEDLLKEAAAKTKGFSGREIAKLMASVQAAVYGSANCLLDANLFREVIDYKVAEHQQRKKLAGTDAGNKKK
Protein: Inhibitor of growth protein 1 (Q9QXV3)
Organism: Mus musculus (Mouse)
Function: Isoform 1 inhibits p53-dependent transcriptional activation and may function as an oncoprotein. Isoform 2 acts as a negative growth regulator by cooperating with p53 in transcriptional activation of p53-responsive genes and may act as a tumor suppressor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone deacetylase 1
- Histone deacetylase complex subunit SAP30
- Histone-binding protein RBBP4
- AT-rich interactive domain-containing protein 4B
- Paired amphipathic helix protein Sin3b
- Histone-binding protein RBBP7
- Histone deacetylase 2
- AT-rich interactive domain-containing protein 4A
Sequence:
MLSPANGEQIHLVNYVEDYLDSIESLPFDLQRNVSLMREIDAKYQEILKELDDYYEKFKRETDGTQKRRVLHCIQRALIRSQELGDEKIQIVSQMVELVENRSRQVDSHVELFEAHQDISDGTGGSGKAGQDKSKSEAITQADKPNNKRSRRQRNNENRENASNNHDHDDITSGTPKEKKAKTSKKKKRSKAKAEREASPADLPIDPNEPTYCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPKGKWYCPKCRGESEKTMDKALEKSKKERAYNR
Protein: V-type sodium ATPase catalytic subunit A (EC 7.2.2.1) (Na(+)-translocating ATPase subunit A) (V-type sodium pump catalytic subunit A) (Q08636)
Organism: Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R)
Function: Involved in ATP-driven sodium extrusion.
Interaction partners:
Sequence:
MQIGKIIKVSGPLVMAENMSEASIQDMCLVGDLGVIGEIIEMRQDVASIQVYEETSGIGPGEPVRSTGEALSVELGPGIISQMFDGIQRPLDTFMEVTQSNFLGRGVQLPALDHEKQWWFEATIEEGTEVSAGDIIGYVDETKIIQHKIMVPNGIKGTVQKIESGSFTIDDPICVIETEQGLKELTMMQKWPVRRGRPIKQKLNPDVPMITGQRVIDTFFPVTKGGAAAVPGPFGAGKTVVQHQIAKWSDVDLVVYVGCGERGNEMTDVVNEFPELIDPNTGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVAIMADSTSRWAEALREMSGRLEEMPGDEGYPAYLGSRLAEYYERSGRVIALGSDQREGSITAISAVSPSGGDISEPVTQNTLRVVKVFWGLDSSLAQKRHFPSINWIQSYSLYSTEVGRYMDQILQQDWSDMVTEGMRILQEEEQLNEIVRLVGIDSLSDNDRLTLEVAKSIREDYLQQNAFDDVDTFTSREKQFNMLKVILTFGKEARKALSLGAYFNEIMEGTVAVRERISRSKYIPEEELAKISSINEEIKETIQLIVSEGGMTDD
Protein: procollagen-lysine 5-dioxygenase (EC 1.14.11.4) (A3KNH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004367}; Lumenal side {ECO:0000256|ARBA:ARBA00004367}. Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}.
Interaction partners:
- Collagen beta
- Procollagen galactosyltransferase 1
- procollagen galactosyltransferase
- Cerebral endothelial cell adhesion molecule
- Si:ch211-13f8.2.
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- procollagen-lysine 5-dioxygenase
- Calmodulin-lysine N-methyltransferase.
Sequence:
MTPVPVILTVILAVIQLSRTEPRKPNELLVITAATEVTDGYLRFMRTIRQFNYTIQVLGLGEQWRGGDVARTVGGGQKVRWLKTELEKHKDKQNTVIMFVDSYDVILASGPVELLRKFSRFSHRVVFSAEGFCWPDQRLASKYPAVHHGKRYLNSGGFIGFAPEIHAIVQQWKYKDDDDDQLFYTRIYLDKEKRRKFNMTLDHRSQIFQNLNGAIEEVVLKFEKSRVRVRNVAYDTLPVVIHGNGPTKLQLNYLGNYVPTAWTYENGCGICEEDLLDLSHLSDEEMPLVHVAVFIEQPMPFLEEFLERLATLNYPHTRIRLFLHNNVVYHEQHVERFWTRHRSLFTGARIVGPEENLKHDQARTMAVEACKKDVSCDYFFSLDADVALTNPDVLRILIEENKSVIAPMLSRHGKLWSNFWGALSPEGFYSRAEDYIDIVQSKRVGLWNVPYITQVYLIRGETLRSRLAAVSLYQQEGMDPDMSFCKSVREQGIFMFVSNRDEFGRLVSSANYNISRLHPDMWQIFDNPVDWREKYIHENYSRIFEDDESVVEQPCPDVYWFPAFSERMCDDLVETMEEFGQWSGGGHKDERLSGGYENVPTVDIHMNQIQFEKEWLKFLKEYIVPVTEKLYPGYYPKAQAVMNFVVRYRPDEQPSLRPHHDSSTFTINIALNSKGVDYEGGGCRFLRYNCKVESPRKGWSFMHPGRLTHYHEGLPTTRGTRYIMVSFVDP
Protein: Galectin (G5EGB1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAHESAFPVPYRSKLVEPFEPGQTLIVKGKTGEDSIRFTVNLHTNTADFSGNDVPLHVSVRFDEGKLVFNTFSKGEWGKEERKSNPYKKGDDIDIRIRAHDSKFQIFVDQKEVKEYEHRVPLSSITHFTIDGDVLVNYIHWGGKYYPVPYESGLAGEGLAPGKTLTVFGIPEKKAKRFHINLLKKNGDIALHLNARFDEKHVVRNSLINSAWGNEEREGKMPFEKAVGFDLEIHNEPYAFAVTVNGERFASYAHRLSPDEVNGLQIGGDVEITGIQLA
Protein: Ethylene-responsive transcription factor 5 (AtERF5) (Ethylene-responsive element-binding factor 5) (EREBP-5) (O80341)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Scarecrow-like protein 13
- Mitogen-activated protein kinase 3
- Probable WRKY transcription factor 33
- Ethylene-responsive transcription factor 6
- Zinc finger protein ZAT10
- 1-aminocyclopropane-1-carboxylate synthase 6
- Autophagy-related protein 18h
- Mitogen-activated protein kinase 6
- Ethylene-responsive transcription factor 8
- Probable WRKY transcription factor 40
Sequence:
MATPNEVSALWFIEKHLLDEASPVATDPWMKHESSSATESSSDSSSIIFGSSSSSFAPIDFSESVCKPEIIDLDTPRSMEFLSIPFEFDSEVSVSDFDFKPSNQNQNQFEPELKSQIRKPPLKISLPAKTEWIQFAAENTKPEVTKPVSEEEKKHYRGVRQRPWGKFAAEIRDPNKRGSRVWLGTFDTAIEAARAYDEAAFRLRGSKAILNFPLEVGKWKPRADEGEKKRKRDDDEKVTVVEKVLKTEQSVDVNGGETFPFVTSNLTELCDWDLTGFLNFPLLSPLSPHPPFGYSQLTVV
Protein: OSJNBa0086O06.20 protein (Q7XLY9)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALDTLCSAGGDVLIYDTFNASAAAAAAVVPPASFLFGNNNAGGAAGTETRVQVAAGAVPEVDQLLKQAQQPGRRKRRRRARSCKSREDAESQRMTHIAVERNRRRQMNEYLAVLRSLMPESYVHRGDQASIVGGAIDFVKELEQLLQSLEAQKRTLLMQPPPPPQQQREPKCDAADSTSAADQETPAAAAAAAAADGPPFARFFTYPQYVWCHNPAQDGGGGGGAAAENRAGVADIEVSLVETHASIRVMAARRPGQLLKMVAGLQALRLTVLHLNVTALGSLALYSISVKRFHGGKAIASLGPLGVFFLCALYLWYSTTVVEEGCGMATVDDIAAAVHHVLCIIDAEAASQMLLAGEASG
Protein: Zinc uptake regulation protein (Zinc uptake regulator) (P0AC51)
Organism: Escherichia coli (strain K12)
Function: Acts as a negative controlling element, employing Zn(2+) as a cofactor to bind the operator of the repressed genes (znuACB).
Interaction partners:
- Zinc import ATP-binding protein ZnuC
Sequence:
MEKTTTQELLAQAEKICAQRNVRLTPQRLEVLRLMSLQDGAISAYDLLDLLREAEPQAKPPTVYRALDFLLEQGFVHKVESTNSYVLCHLFDQPTHTSAMFICDRCGAVKEECAEGVEDIMHTLAAKMGFALRHNVIEAHGLCAACVEVEACRHPEQCQHDHSVQVKKKPR
Protein: Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1 homolog) (Q9WVA1)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit Tim21
Sequence:
MESSSSSSGSALAAVDPQLQHFIEVETQKQRFQQLVHQMTELCWEKCMDKPGPKLDSRAEACFVNCVERFIDTSQFILNRLEQTQKSKPVFSESLSD
Protein: V-type proton ATPase subunit D (V-type proton ATPase subunit d) (Vacuolar proton pump subunit D) (A0A8I6AHT1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029434}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029434}.
Interaction partners:
Sequence:
LSGDNTYVCFVFCRAQTIMKARLKGAQTGRNLLKKKSDALTLRFRQILKKIIETKMLMGEVMREAAFSLAEAKFTAGDFSTTVIQNVNKAQVKIRAKKDNVAGVTLPVFEHYHEGTDSYELTGLARGGEQLAKLKRNYAKAVELLVELASLQTSFVTLDEAIKITNRRVNAIEHGDYRALKTFEFLCTERKSPSCRLKKIQEKKKIIKEKSEKDLERRRAAGEVMEPANLLAEEKDEDLLFE
Protein: Subtilisin-like protease SBT1.6 (EC 3.4.21.-) (Subtilase subfamily 1 member 6) (AtSBT1.6) (Subtilisin-like serine protease 2) (At-SLP2) (O49607)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Eukaryotic aspartyl protease family protein
- Serine carboxypeptidase-like 50
- Tetratricopeptide repeat
- Lon protease homolog 1, mitochondrial
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- E3 ubiquitin-protein ligase SPL1
- Prolyl carboxypeptidase like protein
- Serine carboxypeptidase-like 26
- Serine carboxypeptidase-like 34
- Serine carboxypeptidase-like 42
Sequence:
MASSTIVLLLFLSFPFISFAASQAAKTFIFRIDGGSMPSIFPTHYHWYSTEFAEESRIVHVYHTVFHGFSAVVTPDEADNLRNHPAVLAVFEDRRRELHTTRSPQFLGLQNQKGLWSESDYGSDVIIGVFDTGIWPERRSFSDLNLGPIPKRWRGVCESGARFSPRNCNRKIIGARFFAKGQQAAVIGGINKTVEFLSPRDADGHGTHTSSTAAGRHAFKASMSGYASGVAKGVAPKARIAAYKVCWKDSGCLDSDILAAFDAAVRDGVDVISISIGGGDGITSPYYLDPIAIGSYGAASKGIFVSSSAGNEGPNGMSVTNLAPWVTTVGASTIDRNFPADAILGDGHRLRGVSLYAGVPLNGRMFPVVYPGKSGMSSASLCMENTLDPKQVRGKIVICDRGSSPRVAKGLVVKKAGGVGMILANGASNGEGLVGDAHLIPACAVGSNEGDRIKAYASSHPNPIASIDFRGTIVGIKPAPVIASFSGRGPNGLSPEILKPDLIAPGVNILAAWTDAVGPTGLPSDPRKTEFNILSGTSMACPHVSGAAALLKSAHPDWSPAVIRSAMMTTTNLVDNSNRSLIDESTGKSATPYDYGSGHLNLGRAMNPGLVYDITNDDYITFLCSIGYGPKTIQVITRTPVRCPTTRKPSPGNLNYPSITAVFPTNRRGLVSKTVIRTATNVGQAEAVYRARIESPRGVTVTVKPPRLVFTSAVKRRSYAVTVTVNTRNVVLGETGAVFGSVTWFDGGKHVVRSPIVVTQMDTL
Protein: Galactofuranosyltransferase GlfT2 (GalTr 2) (EC 2.4.1.288) (Arabinogalactan galactosyltransferase 2) (Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase) (Polymerizing galactofuranosyltransferase GlfT2) (O53585)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the galactan polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacteria cell wall. Thus, successively transfers approximately 28 galactofuranosyl (Galf) residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and 1->6 links, forming a galactan domain with approximately 30 galactofuranosyl residues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11304545}.
Interaction partners:
- Galactofuranosyltransferase GlfT1
- UDP-galactopyranose mutase
- Decaprenyl-phosphate phosphoribosyltransferase
- Probable O-antigen/lipopolysaccharide transport integral membrane protein ABC transporter RfbD
- Decaprenylphosphoryl-5-phosphoribose phosphatase
- Probable O-antigen/lipopolysaccharide transport ATP-binding protein ABC transporter RfbE
- Galactan 5-O-arabinofuranosyltransferase
- Terminal beta-
- dTDP-4-dehydrorhamnose reductase
- Decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Sequence:
MSELAASLLSRVILPRPGEPLDVRKLYLEESTTNARRAHAPTRTSLQIGAESEVSFATYFNAFPASYWRRWTTCKSVVLRVQVTGAGRVDVYRTKATGARIFVEGHDFTGTEDQPAAVETEVVLQPFEDGGWVWFDITTDTAVTLHSGGWYATSPAPGTANIAVGIPTFNRPADCVNALRELTADPLVDQVIGAVIVPDQGERKVRDHPDFPAAAARLGSRLSIHDQPNLGGSGGYSRVMYEALKNTDCQQILFMDDDIRLEPDSILRVLAMHRFAKAPMLVGGQMLNLQEPSHLHIMGEVVDRSIFMWTAAPHAEYDHDFAEYPLNDNNSRSKLLHRRIDVDYNGWWTCMIPRQVAEELGQPLPLFIKWDDADYGLRAAEHGYPTVTLPGAAIWHMAWSDKDDAIDWQAYFHLRNRLVVAAMHWDGPKAQVIGLVRSHLKATLKHLACLEYSTVAIQNKAIDDFLAGPEHIFSILESALPQVHRIRKSYPDAVVLPAASELPPPLHKNKAMKPPVNPLVIGYRLARGIMHNLTAANPQHHRRPEFNVPTQDARWFLLCTVDGATVTTADGCGVVYRQRDRAKMFALLWQSLRRQRQLLKRFEEMRRIYRDALPTLSSKQKWETALLPAANQEPEHG
Protein: SpoVT-AbrB domain-containing protein (Q8DW96)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Interaction partners:
- PpGpp-regulated growth inhibitor
- Possible DNA-damage-inducible protein
- Glutaredoxin-like protein NrdH
- Membrane protein
Sequence:
MQLVINKWGNSSAIRLPKQLVQELQLQTNDVLDYKVSGNKIILEKVNNIPELTVEDLFKDYQGEPVNVTPALFESVGNEQW
Protein: BCL2 associated transcription factor 1 (E9PK91)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGRSNSRSHSSRSKSRSQSSSRSRSRSHSRKKRYSSRSRSRTYSRSRSRDRMYSRDYRRDYRNNRGMRRPYGYRGRGRGYYQGGGGRYHRGGYRPVWNRRHSRSPRRGRSRSRSPKRRSVSSQRSRSRSRRSYRSSRSPRSSSSRSSSPYSKSPVSKRRGSQEKQTKKAEGEPQEESPLKSKSQEEPKDTFEHDPSESIDEFNKSSATSGDIWPGLSAYDNSPRSPHSPSPIATPPSQSSSCSDAPMLSTVHSAKNTPSQHSHSIQHSPERSGSGSVGNGSSRYSPSQNSPIHHIPSRRSPAKTIAPQNAPRDESRGRSSFYPDGGDQETAKTGKFLKRFTDEESRVFLLDRGNTRDKEASKEKGSEKGRAEGEWEDQEALDYFSDKESGKQKFNDSEGDDTEETEDYRQFRKSVLADQGKSFATASHRNTEEEGLKYKSKVSLKGNRESDGFREEKNYKLKETGYVVERPSTTKDKHKEEDKNSERITVKKETQSPEQVKSEKLKDLFDYSPPLHKNLDAREKSTFREESPLRIKMIASDSHRPEVKLKMAPVPLDDSNRPASLTKDRLLASTLVHSVKKEQEFRSIFDHIKLPQASKSTSESFIQHIVSLVHHVKEQYFKSAAMTLNERFTSYQKATEEHSTRQKSPEIHRRIDISPSTLRKHTRLAGEERVFKEENQKGDKKLRCDSADLRHDIDRRRKERSKERGDSKGSRESSGSRKQEKTPKDYKEYKSYKDDSKHKREQDHSRSSSSSASPSSPSSREEKESKKEREEEFKTHHEMKEYSGFAGVSRPRGTFHDDRDDGVDYWAKRGRGRGTFQRGRGRFNFKKSGSSPKWTHDKYQGDGIVEDEEETMENNEEKKDRRKEEKE
Protein: Polysialic acid O-acetyltransferase (EC 2.3.1.136) (Capsule O-acetyl transferase) (A1ADJ6)
Organism: Escherichia coli O1:K1 / APEC
Function: Catalyzes the O-acetylation of capsular polymeric sialic acid. Shows high substrate specificity toward polymers of sialic acid that contains a large number of residues.
Interaction partners:
Sequence:
MLRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSRLKTQDSFSVDDNGSGNVFVCGDLVNSKENKVQFNGNNNKLIIEDDVECRWLTVIFRGDNNYVRIHKNSKIKGDIVATKGSKVIIGRRTTIGAGFEVVTDKCNVTIGHDCMIARDVILRASDGHPIFDIHSKKRINWAKDIIISSYVWVGRNVSIMKGVSVGSGSVIGYGSIVTKDVPSMCAAAGNPAKIIKRNIIWARTDKAELISDDKRCSSYHAKLTQ
Protein: Paired box 5 (E7ERW5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQAPPTIIALPPEEPPHLQPPLPMTVTDPWSQAGTKH