wanglab/gogpt-training-data huggingface dataset:
Protein: Putative antiholin (O48472)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Function: Probably functions as a holin together with holin-like protein 26. Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis.
Subcellular location: Host cell inner membrane {ECO:0000269|PubMed:27825035}; Multi-pass membrane protein {ECO:0000255}. Note=Classified as a class II holin. {ECO:0000250|UniProtKB:P27360}.
Interaction partners:
Sequence:
MKMDTGTKVRTILFLIAWVNQLLSFDNLEPIPVDETTAQQVYDAVSVLFTIVVTVWTSFKNNYLTLKGRKQREALKKNGLTK
Protein: Inosine-uridine preferring nucleoside hydrolase (Q9A6Z8)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- Adenine deaminase
- Xanthine dehydrogenase, C-terminal subunit
- Hypoxanthine-guanine phosphoribosyltransferase
- Guanine deaminase
- NAD-dependent protein deacylase
- AMP nucleosidase
- 5'-nucleotidase SurE
- Ribokinase
- Transcriptional regulator, LacI family
- Transcriptional regulator, LacI family
Sequence:
MRLIIDTDTAGDDVFSLMLALTRTGVELEAITIAHGNVGFEQHAENALVTLDRCGRAGEVPVYLGAQFPLMRAPLDAAYVFGRDGMSDSGFARTSQRPAEGHAVDELVRRIMAAPGEITLIAQAPLTNIALAYQREPRIAKALKHLWVMGGTDNGVGNVTPAAEYNFYADPEAAKIVVNAGFNLSIATWTLTLKDGLWTTEKLDALDALGTEKARFFTDVNRASLAFARETEGLDGSLHPDALTCAIALDEGLILEAETCVVDVETVGELTRGYLSVSHSILPDIEIADPALKRRPPNARVIKAIDREGFFAAMRTALL
Protein: Coiled-coil domain-containing protein 125 (Protein kenae) (Q86Z20)
Organism: Homo sapiens (Human)
Function: May be involved in the regulation of cell migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19787194}.
Interaction partners:
Sequence:
MSKVARSSSESDVQLWETEEDDMTEGDLGYGLGRKPGGIYEIEFSHRSRKRSDGKNFSPPPFPRKGEERNEASFQYSKHKSQQDTFPQVSRISNYRRQSSTVDSNSELSNEELRQCLNETLEEVEMLKTELEASQRQLRGKEEALKILQSMAILGKATSHTQAVLQKTMEQNRSLEKEINALQWEIEFDHNRFKNIEESWIQKYDRLNCENAVLKENLKVKTEEIKMLKSDNAVLNQRYLEALAMLDIKQQKMAQENMCCDKSGFAEASGLELAVLGACLCHGPGGNPCSCARMAASTRKLLLQLKQELEILQKSKEEAYVMADAFRIAFEQQLMRKNDQALQLTQMDKMHKKATKWMNWKHLKEDGFPSPRSKKTFGQRLLGMLPSENSSKRMEDQDSPQEVLKMLIDLLNDKEEALAHQRKVSYMLARALEDKDTASNENKEKNPIKENFPFNNPWRKTSEFSVLGDPIHSSVCILNSVGCICSIQHSQIDPNYRTLKRSHSLPSSIIF
Protein: Translation initiation factor eIF2B subunit gamma (Putative pyrophosphorylase ppp-1) (eIF2B GDP-GTP exchange factor subunit gamma) (P80361)
Organism: Caenorhabditis elegans
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56288}.
Interaction partners:
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit alpha
- protein-synthesizing GTPase
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2 subunit 1
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Probable phosphomannomutase
- dTDP-D-glucose 4,6-dehydratase
Sequence:
MHEMQGILLCSGGGTRMPVLTRHVQKCLLPVVGVPMFLYPLSSLLRTGITDIKIFVREVLQLTLEKEVKKSKLLEKYPAHIEYICVNQEDFGTADLLKNHHSKITKDALIVSCDFISDASLIPLVDFFRATNSTLVALIADTCVNAPAPGSKSKKPKATDVMAIVESTGQLAFLCGDDDFDAPLVMEKSLKIFPSIKLTSKYNDCHVYAIRHKVLLNLSKSKHISSFKADFVPLLIDKQFEPDSDIKCFAYRLPHENGFVTAHANTLGSYFEVNKAIQKSFTRLMEYRGNGKNFNYKTDKIAAHESRIEESAEIDKDSVIKRSFISDNCRIGEKTKLKESIIAKGVVIGNGASISNSIICDGVEIGENADVTNCIVAKDQKVPAKGKVQNEVVEDGEDEEWTDD
Protein: Cytosolic IMP-GMP specific 5'-nucleotidase (Q5ZZB6)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Interaction partners:
- Segregation and condensation protein A
Sequence:
MDTHKVFVNRIINMRKIKLIGLDMDHTLIRYNSKNFESLVYDLVKERLAESFHYPEEIKKFKFNFDDAIRGLVIDSKNGNILKLSRYGAIRLSYHGTKQISFSDQKKIYRSIYVDLGDPNYMAIDTSFSIAFCILYGQLVDLKDTNPDKMPSYQAIAQDVQYCVDKVHSDGTLKNIIIKNLKKYVIREKEVVEGLKHFIRYGKKIFILTNSEYSYSKLLLDYALSPFLDKGEHWQGLFEFVITLANKPRFFYDNLRFLSVNPENGTMTNVHGPIVPGVYQGGNAKKFTEDLGVGGDEILYIGDHIYGDILRLKKDCNWRTALVVEELGEEIASQIRALPIEKKIGEAMAIKKELEQKYVDLCTRSIDESSQQYDQEIHDLQLQISTVDLQISRLLQEQNSFYNPKWERVFRAGAEESYFAYQVDRFACIYMEKLSDLLEHSPMTYFRANRRLLAHDIDI
Protein: LD07388p (Q8IH19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
THCGAHRYFLIADSSADSRVQILTLLFNLLSHPPPPSVGRCCSCCCCAGNLLFVGGARGSSQIAKSSIVNRHRRNVCAELMKCPRRFFINENKKRGDYPPNSISKICSCAFG
Protein: Probable inactive DNA (cytosine-5)-methyltransferase DRM3 (Protein DOMAINS REARRANGED METHYLTRANSFERASE 3) (Q8H1E8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytically inactive DNA methyltransferase that acts as regulatory factor for DRM2-mediated DNA methylation. Required for maintenance of non-CpG DNA methylation. Required for normal establishment and maintenance of RNA-directed DNA methylation (RdDM) and accumulation of specific repeat-associated small interfering RNAs (siRNAs). Required for nucleolus organizer region (NOR) nuclear organization during interphase. Acts downstream of the production of siRNAs. May promote RNA polymerase V (Pol V) transcriptional elongation or assist in the stabilization of Pol V transcripts.
Subcellular location: Nucleus {ECO:0000269|PubMed:25316414}. Note=Colocalizes with AGO4 in perinucleolar region. {ECO:0000269|PubMed:25316414}.
Interaction partners:
- DNA
- DNA-directed RNA polymerase V subunit 1
- DNA
- DNA
- Dormancy-associated protein homolog 1
- Helicase-like transcription factor CHR27
- Helicase-like transcription factor CHR28
- tRNA
- DNA-directed RNA polymerase IV subunit 1
- Putative DNA
Sequence:
MADMRRRNGSGGSSNHERNEQILFPKPETLDFDLPCDTSFPQQIGDNAASSSGSNVKSLLIEMGFCPTLVQKAIDENGQDDFELLLEILTKSTETEPPGPSFHGLMEPKPEPDIEYETDRIRIALLTMKFPENLVDFALDRLGKDTPIDEMVDFIVAAQLAEKYAEESEDSLDGAEINEEDEDVTPVTARGPEVPNEQLFETMDKTLRLLEMGFSNDEISMAIEKIGTKGQISVLAESIVTGEFPAECHDDLEDIEKKVSAAAPAVNRTCLSKSWRFVGVGAQKEDGGGGSSSGTANIKPDPGIESFPFPATDNVGETSRGKRPKDEDENAYPEEYTGYDDRGKRLRPEDMGDSSSFMETPWMQDEWKDNTYEFPSVMQPRLSQSLGPKVARRPYFFYGQLGELSPSWWSKISGFLFGIHPEHVDTRLCSALRRTEGYLHNLPTVNRFNTLPNPRLTIQDAMPHMRSWWPQWDIRKHFNSGTCSNMKDATLLCERIGRRIAECKGKPTQQDQTLILRHCHTSNLIWIAPNILSPLEPEHLECIMGYPMNHTNIGGGRLAERLKLFDYCFQTDTLGYHLSVLKSMFPQGLTVLSLFSGIGGAEIALDRLGIHLKGVVSVESCGLSRNILKRWWQTSGQTGELVQIEEIKSLTAKRLETLMQRFGGFDFVICQNPSTPLDLSKEISNSEACEFDYTLFNEFARVTKRVRDMM
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (F4I0X0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAEETMENEERVKLFVGQVPKHMTEIQLLTLFREFSIVNEVNIIKEKTTRAPRGCCFLTCPTREDADKVINSFHNKKTLPGASSPLQVKYADGELERLDVLDCSCNPEHKLFVGMLPKNVSETEVQSLFSEYGTIKDLQILRGSLQTSKGCLFLKYESKEQAVAAMEALNGRHIMEGANVPLIVKWADTEKERQARRLLKVQSHVSRLDPQNPSMFGALPMSYVPPYNGYGYHVPGTYGYMLPPIQTQHAFHNVISPNQGNGRALQGTALTESVPPRLAPRRNFPTALGNYGYHGLQYPMAFPRGMIPPRLPLTTVSPGISNNGTSIPSSLQTEGPAGANLFIYNIPREFEDQELAATFQPFGKVLSAKVFVDKATGISKCFGFISYDSQAAAQNAINTMNGCQLSGKKLKVQLKRDNGQQQQQQQSKNPLFNGLLNS
Protein: Microtubule-associated protein (A0A0B4LIS6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU000686}.
Interaction partners:
Sequence:
MADVLEKSSLLDAVPPLGDPHPPLPHQQLQQEAAAAAAANAAPPAPPQQQQPPPHQLQQQQPQQQQLQQKPANARANQDQKEGDNDSGVDESTQEKDRNGPNSPSSPVKTPTSTSSKPDKSGTSRPPSATPSNKSAPKSRSASKNRLLLKTPEPEPVKKVPMNKVQVGHAPSPNLKAVRSKIGSLDNATYKPGGGHVKIESKKIDIKAAPRIEAKNDKYMPKGGEKKIVTTKLQWNAKSKIGSLENAAHKPGGGDKKIETLKMDFKDKAKPKVGSTANVKHQPGGGDIKIQTQKLEIKAQSKVGSLDNVKHKPGGGEKKIFDDKDYLKNVEHSVALTTPPTQYWKAPRIQRATTLTSSMSLPAECLVLSVSMPSLNSEPKRPKSAGPKKKPGQAVHSKPFRLY
Protein: Wtf element wtf15 (A0A482AT42)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: May act in meiotic drive.
Subcellular location: Spore membrane {ECO:0000255, ECO:0000269|PubMed:32032353}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSNNYTSLSSSLDEEMGLKAGHEIDLEGSPPSEHNSEEKSTLPSNSDILTSANPVSQASETPDHSIESNTGSTQSPTSHSLLLKFSFCIVYYFYFAIVVLGCVLPFEHTHTFLIAFLVIFGIISVILFSGSIYYYETWTKTVKHFLKKVISPFKKEYIVCAFLKTFVFYGLLKTIEHFLVLLSGDKWGWKCSTLSSILTPVSCISFCLNESVQLRSCSTHLFINTVAWIKSLGGGKNAFENNYNQLNETSPEDLV
Protein: Fibrinogen C-terminal domain-containing protein (Q8CEZ7)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
GDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGKDAPFKDSEDRVPEGQTPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLAPTHLDNGVDKTSRGKRLPKMTQLIGLTPNATHLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGNRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFFTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQERKKGIFWKTWGRYYPLQATTLLIQPMEATAAS
Protein: Enhancer of polycomb homolog 1 (A0A8I6GEL3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHIEHHLQRAISAQQVYGEKRDNMVIPVPEAESNIAYYESIYPGEFKMPKQLIHIQPFSLDAEQPDYDLDSEDEVFVNKLKKKMDICPVQFEEMIDRLEKGSGQQPVSLQEAKLLLKEDDELIREVYEYWIKKRKTCRGPSLIPSVKQEKRDGSSTNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRRDLSRAVTILEMIKRREKSKRELLHLTLEIMEKRYNLGDYSGEIMSEVMAQRQPVKPTYAIPIIPITNSSQFKHQDVTDAKEFKVNKQDKADLIRPKRKYEKKPKVLPSSAAAPQQPSPAALPGFSAKDLNQYDFPSSDEEPLSQVLSGSSEAEEENDPDGPFAFRRKAGCQYYAPHLDQTGNWPWTSPKDGGLGDVRYRYCLTTLTVPQRCLGFARRRVGRGGRVLLDRAHSDYDSMFHHLDLDMLSSPQPSPVNQFANTSETNTSDRPSSKDLSQILVDIKSCRWRHFRPRTPSLPDSDSGELSSRKLHRSISRAGPAQPGAHTCSASTQSRSSSGSTHCAFTAEQYQQHQQQLALMQQQQLAQTQQQQANSSSSTAAPQGFVSKTLDSASAQFAASALMTSEQLMGFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSTLLQPSNITQTSGSHSALSHQVTAANSATTQVLFGNNIRLTVPSSVPTVNSIAPINARHIPRTLSAVPPSALKLAAAANCQVSKVPSSSSVDSVPRENHESEKPALNNIADNTVAMEVT
Protein: Cadherin 11, osteoblast (Cadherin 11, type 2, OB-cadherin (osteoblast)) (Cadherin-11 isoform X1) (Cadherin-11 precursor) (Cdh11 protein) (B3DGG4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
Interaction partners:
- Catenin alpha-2
- Catenin beta-1
- Catenin, beta 2.
- Pleckstrin homology domain-containing, family B
- Cadherin-related family member 5 isoform X2
- Junction plakoglobin a.
- Junction plakoglobin b.
- Catenin
- Catenin alpha-1
Sequence:
MWEGLRLQVFFLCLGAALWSAAAAATHRGSGPRERGHRRHLSLHRHRERGKEGQVLHRSKRGWVWNQFFVIEEYTGPDPVLVGRLHSDVDSGDGNIKYILSGEGAGTIFVIDDKTGNIHATKTLDREEQAQYTLTAQAVARDTNKPLEPPSEFIVKVQDINDNPPEFLHGPYYARVAEMSNVGTSVIKVTATDADDPTYGNSARLVYSILQGQPYFSVEPQTGIIRTALPNMDREARQEYDVVIQAKDMGGHMGGLSGTTQVKITLTDVNDNPPKFAQGVYAMAVSEDKVPGEEVGRLKARDPDLAENGLVDYRILEGDGMNYFEITKDSETQEAVIKLKKPVDFETKRSYTLKVEATNTHVDPRFIAWGPYKDTTIVKISVEDADEPPTFMAPSYNFEVEENAPAGTLVGRVHAKDTDMMNNPIRYMIPHYTDLEEFFTINPEDGIIKTTRPLDREAQAWHNISVSATEIGGHHQDAKVRVNIKVKDVNDNAPEFATQNEVLVCENVNPGKLIETVSATDKDEMAHRQHFHFSLAPEVANNHSFSLKDNRDSTASIFVIRKGFSRMTQDIYHLPIEINDNGVPPMSSTNTLIIRVCSCDSKDTILSCNVEPFILTAGLSTGALIAILACIVILLAIVVLFVALRRQKKEPLIVFEEEDIRENIITYDDEGGGEEDTEAFDIATLQNPDGANGFLPRKDMKPELQYGMRPGLRPIGNSVDVDDFIKTRISDADNDPTAPPYDSIQIYGYEGRGSIAGSLSSLESVTTDSDLDYDYLQSWGPRFKKLADLYGTKDSVDDNS
Protein: Max dimerization protein 1 (Max dimerizer 1) (Protein MAD) (Q05195)
Organism: Homo sapiens (Human)
Function: Component of a transcriptional repressor complex together with MAX. In complex with MAX binds to the core DNA sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing with MYC for MAX binding. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding.
Subcellular location: Nucleus {ECO:0000305|PubMed:8425218}.
Interaction partners:
- Protein max
- Paired amphipathic helix protein Sin3a
- Myc proto-oncogene protein
- Sin3 histone deacetylase corepressor complex component SDS3
- AT-rich interactive domain-containing protein 4A
- RAC-alpha serine/threonine-protein kinase
- Max-binding protein MNT
Sequence:
MAAAVRMNIQMLLEAADYLERREREAEHGYASMLPYNNKDRDALKRRNKSKKNNSSSRSTHNEMEKNRRAHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKLGIERIRMDSIGSTVSSERSDSDREEIDVDVESTDYLTGDLDWSSSSVSDSDERGSMQSLGSDEGYSSTSIKRIKLQDSHKACLGL
Protein: Neuromedin-B [Cleaved into: Neuromedin-B-32; Neuromedin-B-30; Neuromedin-B] (P01297)
Organism: Sus scrofa (Pig)
Function: Stimulates smooth muscle contraction. Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem (By similarity). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (By similarity). Contributes to induction of acute itch, possibly through activation of the NMBR receptor on dorsal root ganglion neurons (By similarity). Increases expression of NMBR and steroidogenic mediators STAR, CYP11A1 and HSD3B1 in Leydig cells, induces secretion of testosterone by Leydig cells and also promotes Leydig cell proliferation. Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6 (By similarity). Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to positive regulation of the expression of the CSF1 receptor CSF1R (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9CR53}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9CR53}. Note=In neurons of the retrotrapezoid nucleus//parafacial respiratory group, expressed on neuron projections which project into the pre-Botzinger complex. {ECO:0000250|UniProtKB:Q9CR53}.
Interaction partners:
- Gastrin releasing peptide receptor
- Neuromedin-B receptor
- Bombesin receptor subtype 3
- Gastrin-releasing peptide
- Neuropeptide FF-amide peptide precursor.
- Elongator complex protein 3
Sequence:
MTLRARGARLLGGLLFFTLLAAGAAPLSWDLPEPRSRAGKIRVHPRGNLWATGHFMGKKSLEPPNPSLLGTTHHISLRDQRLQLSHDLLRILLQKKALGLSLSGPASHTPYRRLLVQTLEK
Protein: Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41) (Q80ZM8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UJA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UJA2}.
Interaction partners:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
- Tafazzin family protein
- Phosphatidate cytidylyltransferase 2
- Lysocardiolipin acyltransferase 1
- Phosphatidate cytidylyltransferase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
- Lysophosphatidylcholine acyltransferase 2
- Lysophosphatidylcholine acyltransferase 1
- Lysophospholipid acyltransferase LPCAT4
Sequence:
MLAWRVARGAWGPLRVALRPPGARLGRGGSRRALLPPAACCLGCLAERWRLRPAAFALRLPGAGPRTHCSGAGKAAPEPAAGGGGAAAQAPSARWVPASAASSYENPWTIPNLLSMTRIGLAPVLGYLILEEDFNVALGVFALAGLTDLLDGFIARNWANQKSALGSALDPLADKVLISILYISLTYADLIPVPLTYMIISRDVMLIAAVFYVRYRTLPTPRTLAKYFNPCYATARLKPTFISKVNTAVQLILVAASLAAPVFNYADSIYLQILWCCTAFTTAASAYSYYHYGRKTVQVIKGK
Protein: Hydrazine synthase subunit alpha (HZS-alpha) (EC 1.7.2.7) (Q1Q0T2)
Organism: Kuenenia stuttgartiensis
Function: Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine. The alpha subunit catalyzes the second half-reaction, i.e. the condensation of hydroxylamine formed in the active site of the gamma subunit with ammonia, yielding hydrazine. Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans.
Subcellular location: Anammoxosome {ECO:0000305|PubMed:21964329}.
Interaction partners:
Sequence:
MGKRKLGVIASAFVAGALVCGSTLVNAEPVMTGGPVQGKALWTDYSGMSKEVQGPVSQILFTQSPRTAKGDPYQNYPHYIPEGSRIVLFDLNTKELKVLTNDFATAFDPCTYWDGKKFAFAGVHKKGGGCQIWEMNIDGSGLRQMTDLKGTCRSPIYYAAGSIEEGEGRIIWRDRYFEGDWKEHGMVEKTGMIIFSGSPEGVMDEFHNPYAYNLYRLDTQGGKIIQRITGHVLSGIEFPHLNTTIDQITYNLSSNFDPWLTPDGNILFSSVQANGSRAGGEGRVMICVDNWDGAYPRPIYGNCDGEIGGTSGRSQAKITFGDRKIVYVESPYMNWGVGQLAAVSWDAPFNKTYEKLTGKDGGLYRSPYPLPDDRMLVSYAERGDFGIYWFNFSKCAAGDKVYDDPNWNDHQPAPVYVKYKPRWINTFTAGKNFGVTVVTYQPFDQVKVEGYPHSWGTWICFDTTLSDQPVGPYPHQKAKNVSHGDIKAVRIIQGYQCVEPDSTRFRVGAGAHLLGGERSSSNSGTAFQQRGIIGYQYVESDGSTVTSQLSDVPYYMQILDDKGMSVQTALTWAYLRPYHGRICSGCHYGSYRGRAFKNIHAKALYNWWYDDRSHYDSPFAFRYLKFDNDGNYKGVKHGEDVVVPSDIYYGGPSGTTSQPVEGLTLDKQRTVDFRRDIQPILDAKCAMCHDSNNPPNLGGGLELVSVDGIAAYSRAYNSLLEPQRGKDPNIGGKYVNPSAAINSLLVWRLYEAELSANAPREKIFPIEGRLLHNKFLTQDERYAIVEWIDLGAQWDNIPGPDFYPGYLVK
Protein: Villin-like protein quail (Q23989)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the formation of cytoplasmic actin filament bundles in nurse cells, possibly by regulating both the polymerization and organization of actin filaments. Mutations in quail result in female sterility due to the disruption of cytoplasmic transport from the nurse cells into the oocyte late in oogenesis.
Interaction partners:
- Gelsolin
- Conserved oligomeric Golgi complex subunit 8
- Caspase-8
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 4
Sequence:
MELSLSPKETEIRPNTIPDLKVDATFRKVAKHAITFAIWKIDEDRLEAVQRSHYGTFYDSCAYIIYAASLSGHYANHETITREQKPNVSLERYIHYWLGKNVSEQNRSNVVHKIQELDSYLGNISSIYRETQNLESARFLSYFKKGYDVRSGALISAPQRPRLFQLYARKWLRSIEVATIDWSHFNSDYVMVLQTDNLTYVWIGRSSSGIERRSALDWVQKHCSGSPITIVDDGYEQAMSQEHKELWNTMLPLKKRMVCQASQLVSEYADYNSNKFRIYKCNQRGRLHLDQLDVGMPAKDDLSDAHGVYLLDNYGQSIWLWVGGQAPQADALSAMGNGRAFVKKKKYPDNTLVVRVLEGHEPVEFKRLFANWLNVWQENTRGHKPVSTKFGKLDAHSLCERPKMAADTQLVDDGRGERVIYRVFGDQVQEVPISKTVVFTTNASFVVKYSVQCATVVPADLASVGIKTIIYQWNGSEASVESISRADKFAKASFDGLKEPGMFVQLYEFDEPPHFLQIFEGKLIIRRGQRTEMPYNGNSNALLDTFLLKVYGDASYNAKAVEETHLSSISSKDCYVIKTNHVWVWCGQSSTGDAREMAKAVGALMGENSLVLEGKESKEFWQSVAMYFNQTLVINGNGNSCSSSTSSSSGAGSMCNGSSNGGNISPTLSNNCYLNTSVPSKPRPPVQLFLVWWQQSSLRYEEILGFDQQDLSSDCTYILDTGSLTYVWLGSQAPNQERYTAIAQSYVQNAPFGRRSATALAVVRQFQEPNVFKGFFESWQNDYGKNFHSYEKMRKDLGNKVTSNCCFASEGSALILNNRQKDFDGHKKYPLTVLIQEMDMLPPDINPLKREVHLTHDDFVSVFNMSFYEFDELPKWKKMELKKQFKLF
Protein: Regenerating islet-derived protein 3-gamma (REG-3-gamma) (Pancreatitis-associated protein 3) (Regenerating islet-derived protein III-gamma) (Reg III-gamma) [Cleaved into: Regenerating islet-derived protein 3-gamma 16.5 kDa form; Regenerating islet-derived protein 3-gamma 15 kDa form] (O09049)
Organism: Mus musculus (Mouse)
Function: Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota.
Subcellular location: Secreted {ECO:0000269|PubMed:28811323, ECO:0000269|PubMed:36240758}. Cytoplasm {ECO:0000250|UniProtKB:P42854}.
Interaction partners:
- Interleukin-22
- Angiogenin-4
- Regenerating islet-derived protein 3-beta
- Mucin-2
Sequence:
MLPRITITIMSWMLLSCLMLLSQVQGEVAKKDAPSSRSSCPKGSRAYGSYCYALFSVSKNWYDADMACQKRPSGHLVSVLSGAEASFLSSMIKSSGNSGQYVWIGLHDPTLGYEPNRGGWEWSNADVMNYINWETNPSSSSGNHCGTLSRASGFLKWRENYCNLELPYVCKFKA
Protein: Spectrin beta chain, brain (F4K9W2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein kinase superfamily protein
- At5g07400
- AT1G56000 protein
- Zinc finger, C3HC4 type
- Formin-like protein 20
- Protein cereblon
- Protein EARLY STARVATION 1, chloroplastic
- AP-1 complex subunit gamma-2
- Pirin-like protein 2
- Ankyrin repeat-containing protein ITN1
Sequence:
MLGSGNNLSRGTIGLSSDTPNLSQVLTLEPIRLGNQNYTRSGELRRVLGVPSRASSEDNSFGMSHPRPSPPVATEELKHFKESVLDTSREAGDLVKKLSENIFKLDKYAETINSKKRRRNDIPPGERMDAATFDKVRNQVPRTQDIMAQRSEERKKMLGLNKRARTTVADVRGDARISALARQHVIEKGSDSPPSVSGESVRIEEKIRRLPVGGEGWETRMKRKRSVATLGNRIMNPEQRVMQPKPTADSKLRSCDSQNFRSKSSPGVSGINRLDTSFEPDSPCMGALSRNELETVSIARDRSVLAEQRLAKGNNKRNLLDDSPTNSSTAILKGKVSRAPRTAAIMGVESSAKVDSPSGVLQGSSAHAMAQWVGQRPHKNSRTRRTNVVSPVIKHSESKISGQGFATSDFSPRASPGTTGPLSVVDSSPLKMKRELRNASSPYGLSESEDSGAGDNKTRERAFASGDLFTTPKSGSLLLPTRKNKIQTSHKGGGAWKQGKSESVSSLTTPGFHPIMVKSENLPVEKPFHNIKIASDKNRSKYGRPPAKKVKDRKPATRLASNANTPSDITGESDDDREDIFAAANSARKAANLACSGKFWKKMDHIFAAVNVDDMQNMKDQLNFAQELDKSLSDAILDGYNILGLKLPKAVHRPGVGNVDYSGPTSSCVSGLSFERLDMRKLNESTPLYKRVLSALIEEDDGEEVVQFNGGKNLSLHYASDDSHCGSCTYIDTEFRERDRMEFEVESSGDFQTPKSGLFDRFSSERSVVSNPFRNGGMSISVHSNEQWIGDDDLSHSDAALGNETYSNSLGQLQAREVNIPNFPVSDTQYQLMSLDERLLLELQSIGVFPEAMPDLAEETMSTDVMELKEGIYQEILNKKKKLEKLIITIQKGKDVEKRKIEHLAMDQLVETAHKKRMACRGSKAAKVNKVTRQVALGFIRRTVARCRKFEETGFSCFSDPALQDILFSSPSNDAKSSENGGSGTASNTLNEPSNHQAEAKGSGAVSSTKRREALIDDVIGCASSKVTTSKGSAVLSGGGAQGKRSEREDGFRNKNKPKPKENNNNNNGNQSRSTTTSTHPTGPASRGASNRGVTSGDGAVDDEAPIDFSKLAFRDLDEIDEQADLGNWFEGLQDIDTAGLDEVPMDDLSFMFG
Protein: Multicopy suppressor of chk1 protein 1 (Q9UT79)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in regulating chromatin structure via global deacetylation of histone H3. This function is associated with the activity of a histone deacetylase.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:15082762}. Note=Associates with chromatin.
Interaction partners:
- Histone H2A.Z
- SWR1-complex protein 4
- SWR1 complex subunit swc3
- Helicase swr1
- SWR complex protein 2
- Actin-like protein arp6
- RuvB-like helicase 1
- Actin-related protein 4
- Actin
- RuvB-like helicase 2
Sequence:
MRKNSSHENQSSENIIEFPYVDFEELNVHSNIFSELEHAKPSTQQQQQQQNISNETTSTGPRICISRDEFKAVNLLTKEEINVRVTPKKEEFSRGLDFISDLYDQTARKSGAVRVIPPDNWKCPLTINTTTFKFLTRKNNPSSMSLVSNYPLDAISSQQKFHGNDKTLEKNSAKATINKSNSTAETSSTATVEPYDSNDLYRIFDRPDAVVLSYIFVLGKAVDLLQIKQWLQLSKQKNLLEFEFWSQAAQHYKLDVNSLRNAYNLYAETGVTTRTGNDGGSPINRPAKRVKRQNHIPKCKLCAQEGSSLVTCCICQSNYHYACVEAPFAPFSDIHYWTCNSCIPSSLKILWKEVDYHCISSFLQSSNELASSLKKQLPSFLAQTPLTLPSNTKTPPASARQSSRRTRSTSGKGFETKISINLDSDIKLLNTLSPLETFFWCCSFPSTASTSSPFSYYPESLPTPLLGRAVNTTAFPTSRQNAYYNDPWNLYFIHFSKLSPLRFTPPGILTSTISLGQPLTCQGWQRDSMSLFGMHYHHYGAQRIWYVIPEVDGPKYEKLLNDLSPSFIQEKPETLIKSKILLPISMLISNGIQVLTFVQNSNEFVITSPNTYYTVLDTGFSLSESVPFATKEWIQDMHAENSFNMYKNLHISAPFSLDHILLANATLDKTVHSAYWLMTCLKDRVDRELTLRNEFRKRHPLLTWIPTPLESSVMACAFCKTFAYLASIEEKNGTKTACLSHKDECFPNTDSDLTVLVRYDDNALLAAYSKVVERAHKADTWLENYKEALGSDNSRPSLKVLKTLLNEAETICCPLQEVSLVRNLVKTAQQWLDKFAIIFKKKSMVKKEKRKPKRGSATHSHLESPSEEVEDLNSSNINEADLLINLVEEAEQFTFDFPEMAVAFEKAESLKIFREKANAMKERSLSYEECLAIVEEGESLQLKTPELLYFKQYMEKTEWIDSFNQISQKTDSTMEELVELIERGEKIGLTSDNENMATALLLKEKSENWMKQVEGLLSQETLSTSKLFQLKSEANSICINRGLLEQLNEVLQKSENFHTQLVSLISRARDPDYYSRPTIEEAKTVLAESENLTNKPEEYTVAQKLLTQTYEWVRRGKRLFGKANAPLEIFNQHLEFVEQRNTNAMVDEGSDAPFHVGNEYYVIAGSDPSDFHYCFCRQPEAGMMIECELCHEWYHAKCMKMSKKKLRADEKFICPICDYRVEVPRHSHRPPLIELQKMVDDIPTLPFQPIEIELLKRVVKQAEEFKNKMQSEVCDPTQLSEKDVPLLQFYLRKLEGSEILFTEELNVFRQKLHEFMPVAPQPPPFIGESRSNRKPRPTKRQREIMEQVESGKLTSAEGAAAIAATQTRNQNNFISKPFNVHTLSTTLSPWAMKSLAQAAISPNPMPSAHDLLPTSNPAELFTNISPEIKELSVDSTSTLGGLNSSHLVSDQNASVICLCRQPFAISDGTVQCHNCLEWFHYECVGLSSDIVSTLSNYACPDCCSKEGKLYPWNTRPRSTPSVWLSQAYSPSVLQGTTENVAFLNKAFSASANLFDVLPVSNTPSHFSKMDYVLEDRKPDLFTETYLSM