wanglab/gogpt-training-data huggingface dataset:
Protein: Flocculin (E9P9G2)
Organism: Saccharomyces cerevisiae (Baker's yeast)
Interaction partners:
Sequence:
MQRPFPFAYLVLSLLFYSALGFPTALVPRGSSEGTSCNSIVNGCPNLDFNWHMNQQNIMQYTLDVTSVSWVQDNTYQITIHVKGEENIDLKYLSSLKIIGVTGPKDTVQLYGYDENTDWIDNPLVSRCDENTYLIDNPTDFTATFEVYATQDVNSCQVWMPNFQIQFEYLQGSAAEYACSWEWGTTSFYLSTGCDNYDNQGYSQTDFPGFYWNIDCDNNCAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPAPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPAPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPAPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVPTPCSSTTESSSAPAPTPSSSTTESSSAPATSSTTESSSAPVPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPAPTPSSSTTESSSAPAPAPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPAPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVPTPCSSTTESSSAPAPTPSSSTTESSSAPATSSTTESSSAPVPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVPTPCSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSVAPVPTPSSSSNITSSAPSSTPFSSSTESSSVPVPTPSSSTTESSSAPAPTPSSSTTESSSAPVSSSTTESSVAPVPTPSSSSNITSSAPSSTPFSSSTESSSVPVPTPSSSTTESSSAPVSSSTTESSVAPVPTPSSSSNITSSAPSSSKYPGSQTETSVSSTTETTIVPTTTTTSVTTPSTTTITTTVCSTGTNSAGETTSGCSPKTITTTVPCSTSPSETASESTTTSPTTPVTTVVSTTVVTTEYSTSTKPGGEITTTFVTKNIPTTYLTTIAPTPSVTTVTNFTPTTITTTVCSTGTNSAGETTSGCSPKTVTTTVPCSTGTGEYTTEATTPVTTAVTTTVVTTESSTGTNSAGETTTGYTTKSVPTTYVTTLAPSAPVTPATSAVPTTITTTECSAATNAAGETTSVCSAKTIVSSASAGENTTPVTTAIPTTVVTTESSVGTNSAGETTTGYTTKSIPTTYITTLIPGSNGAKNYETVATATNPISIKTTSQLATTASASSMAPVVTSPSLTGPLQSASGSAVATYSVPSISSTYQGAANIKVLGNFMWLLLALPVVF
Protein: Polyadenylate-binding protein RBP45B (Poly(A)-binding protein RBP45B) (RNA-binding protein 45B) (AtRBP45B) (Q9SAB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein binding the poly(A) tail of mRNA and probably involved in some steps of pre-mRNA maturation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Sm protein F
- Splicing factor YJU2
- Vacuolar protein sorting-associated protein 2 homolog 2
- THO complex subunit 4B
- At1g75800/T4O12_2
- Pathogenesis-related thaumatin superfamily protein
- Pathogenesis-related thaumatin superfamily protein
- Pathogenesis-related thaumatin superfamily protein
- Pathogenesis-related thaumatin superfamily protein
Sequence:
MMQQPPPGGILPHHAPPPSAQQQYGYQQPYGIAGAAPPPPQMWNPQAAAPPSVQPTTADEIRTLWIGDLQYWMDENFLYGCFAHTGEMVSAKVIRNKQTGQVEGYGFIEFASHAAAERVLQTFNNAPIPSFPDQLFRLNWASLSSGDKRDDSPDYTIFVGDLAADVTDYILLETFRASYPSVKGAKVVIDRVTGRTKGYGFVRFSDESEQIRAMTEMNGVPCSTRPMRIGPAASKKGVTGQRDSYQSSAAGVTTDNDPNNTTVFVGGLDASVTDDHLKNVFSQYGEIVHVKIPAGKRCGFVQFSEKSCAEEALRMLNGVQLGGTTVRLSWGRSPSNKQSGDPSQFYYGGYGQGQEQYGYTMPQDPNAYYGGYSGGGYSGGYQQTPQAGQQPPQQPPQQQQVGFSY
Protein: Histidine biosynthesis bifunctional protein hisIE, chloroplastic (Protein HISTIDINE BIOSYNTHESIS 2) [Includes: Phosphoribosyl-AMP cyclohydrolase (PRA-CH) (EC 3.5.4.19); Phosphoribosyl-ATP pyrophosphatase (PRA-PH) (EC 3.6.1.31)] (O82768)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Imidazole glycerol phosphate synthase hisHF, chloroplastic
- ATP phosphoribosyltransferase 1, chloroplastic
- 1-
- ATP phosphoribosyltransferase 2, chloroplastic
- Histidinol dehydrogenase, chloroplastic
- Imidazoleglycerol-phosphate dehydratase 1, chloroplastic
- Imidazoleglycerol-phosphate dehydratase 2, chloroplastic
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Helicase protein with RING/U-box domain-containing protein
- Histidinol-phosphate aminotransferase 2, chloroplastic
Sequence:
MAVSYNALAQSLARSSCFIPKPYSFRDTKLRSRSNVVFACNDNKNIALQAKVDNLLDRIKWDDKGLAVAIAQNVDTGAVLMQGFVNREALSTTISSRKATFFSRSRSTLWTKGETSNNFINILDVYVDCDRDSIIYLGTPDGPTCHTGEETCYYTSVFDQLNNDEASGNKLALTTLYSLESIISKRKEESTVPQEGKPSWTRRLLTDDALLCSKIREEADELCRTLEDNEEVSRTPSEMADVLYHAMVLLSKRGVKMEDVLEVLRKRFSQSGIEEKQNRTK
Protein: D-aminoacyl-tRNA deacylase (DTD) (EC 3.1.1.96) (D-tyrosyl RNA deacylase) (D-tyrosyl-tRNA(Tyr) deacylase) (Gly-tRNA(Ala) deacylase) (Gly-tRNA(Gly) deacylase) (P0A6M4)
Organism: Escherichia coli (strain K12)
Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid. Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS. Acts via tRNA-based rather than protein-based catalysis. Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs. Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-tRNA(Gly) from hydrolysis, while increasing Dtd levels or inactivating EF-Tu decreases protection. Hydrolyzes mischarged glycyl-tRNA(Ala) (but not seryl-tRNA(Ala)) even in the presence of EF-Tu, edits about 4-fold better than the editing domain of AlaRS. Has greater activity on glycyl-tRNA(Ala) than glycyl-tRNA(Gly) due in part to its recognition of the conserved tRNA(Ala) G3.U70 wobble base pair. Binds D-amino acids but not L-amino acids. Overexpression of E.coli or P.falciparum Dtd is toxic in E.coli, toxicity can be rescued by supplementation with Gly. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. Hydrolyzes D-tyrosyl-tRNA(Tyr). Hydrolyzes D-phenylalanyl-tRNA(Phe). Hydrolyzes D-aspartyl-tRNA(Asp). Hydrolyzes D-tryptophanyl-tRNA(Trp). Hydrolyzes glycyl-tRNA(Gly). Hydrolyzes glycyl-tRNA(Ala).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518, ECO:0000305|PubMed:4292198}.
Interaction partners:
- Probable acyltransferase FabY
- Alpha-D-glucose 1-phosphate phosphatase YihX
- UPF0761 membrane protein YihY
Sequence:
MIALIQRVTRASVTVEGEVTGEIGAGLLVLLGVEKDDDEQKANRLCERVLGYRIFSDAEGKMNLNVQQAGGSVLVVSQFTLAADTERGMRPSFSKGASPDRAEALYDYFVERCRQQEMNTQTGRFAADMQVSLVNDGPVTFWLQV
Protein: Long-chain fatty acid-CoA ligase (A0A1D8PU56)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Fatty acid synthase subunit alpha reductase; 3-oxoacyl-[acyl-carrier-protein] synthase]
- Palmitoyl-protein thioesterase 1
- Very long-chain fatty acid transport protein
- Serine aminopeptidase S33 domain-containing protein
- Acylglycerol lipase
- Acetyl-CoA carboxylase
- Faa2-3p
- Faa2p
- Faa2-1p
Sequence:
MAPLTIAVGEAKPGETAPRRKAAQKDGAVMRPTDSKATTMPEFIDECFKRNGNKDAMAWRDLKDVIVETKQITKVIDGKPTKVNKDWTYYEMGPYNYIKYPELLKLVQNYSKGLLELGLLPDQQSKLMVFAGTSHKWMQTFLAASFQGIPIVTAYDTLGESGLTHSLVQTESDAIFTDNQLLSQLIRPLQKASSVKYIIHGEEIDPKDGRQNGKLYQDAKSAKEKILEIRPDIKFISYDEVIQSGANAKDKQSLHYPKPEDPICIMYTSGSTGDPKGVVITNSNIIAAIGGISCNAGRDLIRPTDRLIAFLPLAHIFELAFECITFWWGVPLGYANVKTLTEASCRNCQPDLIEFKPTVMVGVAAVWESVRKGVLSKLKQASPIQQKIFWAAFKAKTTFKHFGIPGADMFDVVFKKVKSATGGQLRYVLNGGSPISVDAQVFISTLIAPMLLGYGLTETCANAAILEHTHFQIGTLGTLVGSITAKLVDVADAGYYAKNNQGEIWLKGGPVVSEYYKNEKETKEAFTDDGWFKTGDIGEWTSDGGLKIIDRKKNLVKTLNGEYIALEKLESVYRSNHLVQNLCVYADQSKVKPIAIVLPIENNLRQMLKEEKVIDNAETEEFAHLVHDKKVTKAVLKHLLTTGKHQGLKGIELLQNVVLSDDEWTPQNGFVTSAQKLQRKKILESCKKEVQEAYKE
Protein: C-C chemokine receptor 4 (Q91ZH4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MNATDVTDTTQDEAAYNSYYFDESLPKPCTKEGIKAFGEVFLPPLYSLVFLLGLFGNSVVVLVLFKYKRLKSMTDVYLLNLAISDLLFVLSLPFWGYYAADQWVFGLGLCKIISWMYLVGFYSGIFFIMLMSIDRYLAIVHAVFSLRARTLTYGVITSLITWSVAVFASLPGLLFSTCDTENNHTYCKTQYSVNSTTWKVLSSLEINVLGLVIPLGIMLFCYSMIIRTLRHCKNEKKNRAVRMIFAVVVLFLGFWTPYNVVLFLETLVELEVLQDCTLERYLDYAIQATETLAFIHCCLNPVIYFFLGEKFRKYIAQLFRTCRGPPVLCQHCDFLQISSADTSSSSYTQSTVDHDFRDAL
Protein: Splicing factor YJU2 (Complexed with cdc5 protein 16) (Pre-mRNA-splicing factor cwf16) (Q9P7C5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03226}.
Interaction partners:
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor cwf25
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor cwf14
- Pre-mRNA-splicing factor cwf3
- Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16
- Pre-mRNA-splicing factor prp5
- Pre-mRNA-splicing factor cwf12
- Pre-mRNA-splicing factor cwf2
Sequence:
MSERKVLNKYIPPDYDPSIRPPKKKKKFQGPNGGKLTVRLMTPFSMRCHTCGEYIYKGKKFNARKEKTGEKYFSIDILRFYIRCTRCAAEITFITDPKHADYAAESGASRNYEPWHEKRLQEYEENELAERNDIPEEDEMEKLEQKTLDTKRQMQISDALDELREKSARRSRVNIDDAIALLKEDAYGSIEEEESKKRKFEEEEIDREAKSLFSSQDGEIIRRLNAETTVEKELPKPIDLVSEKLATSNIPNFQPPKYAKRKMEKKKVLV
Protein: Isocitrate dehydrogenase [NADP], mitochondrial (IDH) (EC 1.1.1.42) (ICD-M) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) (P56574)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.
Subcellular location: Mitochondrion {ECO:0000269|Ref.2}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- Cytoplasmic aconitate hydratase
- 2-oxoglutarate dehydrogenase complex component E1
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Citrate synthase, mitochondrial
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
Sequence:
MAGYLRAVSSLCRASGSTRTWAPAALNVPSWPEQPRRHYAEKRIKVEKPVVEMDGDEMTRIIWQFIKEKLILPHVDVQLKYFDLGLPNRDQTNDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVVDRAGMFKLVFTPKDGSGAKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYSIQKKWPLYLSTKNTIMKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQTLEKVCVQTVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALGKQ
Protein: Schwannomin-interacting protein 1 homolog (A8DYY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (hpo), in complex with its regulatory protein Salvador (sav), phosphorylates and activates Warts (wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (yki) oncoprotein. Schip1 promotes kinase activity of Tao and enhances phosphorylation of hpo by Tao.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:26954546}. Apical cell membrane {ECO:0000269|PubMed:26954546}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase Tao
Sequence:
MDIYITKGITNPNYPGFQKFAHTLSDDYIEYSDMECNESDLTDSDREDDPTFPSKMAKESGSETFKNGQDSILSNCDNGNTYISEEESVNRSENIPDIVNENYSATSENSKRALQKPDLIYNLSQNYTTNPEFPSWSCTINSKYEGQLQGQSPIDIVGDFGGEVEREFELLLTGYKNKKEADELKGSNLDKICDAELSNGTEALKQTSSTRLSGNSTRKNKKKNTPYGHQIVKTKHPKPSHDERQLPPDTFDYKTYSQRKYIICDADQYSSVPEKNKNDSPNLNQAEIPNMSSLEIGGSGSQQNLDEDNNKVASRKYSNQSRWSQYLEDPIKYSKDPCSTMVLEQFDAYKIANDMDVETLQNHYKKVKQIEKKRRFNRDEIRKRLAIGDKDSLNNDIKKEEFLTGSDNESYSSDSETCPKLSSGVLRKQSEFCETKRNKEFENDKIFQKNQINQDKSMNHMNGNPIGTTDYPSDENLFFFANQSKLQIEVRIALAQSKEIAQMKVKARKHGVTPIVDVIRSMLCDVGIKMNSNHRWISRQLLTGIQVPTLQLLVNNLQEYIENLNVTLLESLKERDDLNSDQDDILHDLEKINNFFVFQQQSGQQVNKIVRHGHLD
Protein: TATA-box binding protein associated factor 15 (F6QCI0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XPMTGSSGGDRGGFKNFGGHRDYGPRPDADSESDNSDNNTIFVQGLGEGVSTDQVGEFFKQIGIIKTNKKTGKPMINLYTDKDTGKPKGEATVSFDDPPSAKAAIDWFDGKEFHGNIIKVSFATRRPEFMRGGGSGGGRRGRGGYRGRGGFQGRGGDPKNGDWVCPNPSCGNMNFARRNSCNQCNEPRPEDSRPSGGDFRGRGYGGERGYRGRGGRGGDRGGSYGGDRGGYGGDRGGYGGDRGGYGGDRGGYGGDRGGYGGDRSRGAYGGDRGGSGSGSGGYGGDRSGGYGGDRSGGYGGDRGGYGGKMGGRNDYRNDQRNRPY
Protein: Basic helix-loop-helix-like (Os06g0526100 protein) (Q653A4)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MGDALCDQLLLVDSDGGEFIPHHADADADDLFTILETWEGCANVVAGGAPATTTTLGSPIAAAACISGVVGGQNHQQLPEPAAAKTVPATNNKRREEEVADRDGDGDDDDGSPQKRRKCCSPESSTTDVAAATTPKTAHIAVERNRRKQMNENLAVLRSLMPCFYVKRGDQASIIGGVVDYIKELQQVLHSLEAKKQRKVYTDQVLSPRPPATVAASCCSPRPPQLSPRLPPQLLKSTPPLSPRLAVPISPRTPPTPGSPYRLLRLPPPPPPASGSNYASPAMTPTHHETAAPSLDAIAAELSAYASRQALGGGLLLPDVKVEFAGANLVLKTVSQRSPGQAVKIIAALEGRSLEILHAKISTVDDTAVNSFTVKIGIECELSAEELVQVIQQTFT
Protein: Splicing factor 3B subunit 6 (Pre-mRNA branch site p14-like protein) (Q9VRV7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (Probable). SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA (By similarity). Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing (By similarity). Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18981222}.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 4
- LD45152p
- Splicing factor 3A subunit 2
- U1 small nuclear ribonucleoprotein A
- Probable small nuclear ribonucleoprotein G
- Microfibrillar-associated protein 1
Sequence:
MNKRNHIRLPPEVNRLLYVRNLPYKITSDEMYDIFGKFGAIRQIRVGNTPETRGTAFVVYEDIFDAKNACDHLSGFNVCNRYLVVLYYQSNKAFKRVDMDKKQEELNNIKAKYNLKTPEAP
Protein: Kelch domain-containing protein 3 (Testis intracellular mediator protein) (Q8VEM9)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC3) complex specifically recognizes proteins with a glycine (Gly) at the C-terminus, leading to their ubiquitination and degradation: recognizes the C-terminal -Arg-(Xaa)n-Arg-Gly, -Arg-(Xaa)n-Lys-Gly, and -Arg-(Xaa)n-Gln-Gly degrons. The CRL2(KLHDC3) complex mediates ubiquitination and degradation of truncated SELENOV and SEPHS2 selenoproteins produced by failed UGA/Sec decoding, which end with a glycine (By similarity). May be involved in meiotic recombination process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12606021}. Note=Also found in meiotic chromatin. {ECO:0000269|PubMed:12606021}.
Interaction partners:
- Cullin-2
- Elongin-B
- Amyloid protein-binding protein 2
- Kelch domain-containing protein 2
- Ribosomal RNA processing protein 36 homolog
- Protein fem-1 homolog C
- E3 ubiquitin-protein ligase RBX1
- Kelch domain-containing protein 10
- Protein zer-1 homolog
- Protein fem-1 homolog B
Sequence:
MLRWTVHLEGGPRRVNHAAVAVGHRVYSFGGYCSGEDYETLRQIDVHIFNAVSLRWTKLPPVRPAVRGQAPVVPYMRYGHSTVLIDDTVFLWGGRNDTEGACNVLYAFDVNTHKWSTPRVSGTVPGARDGHSACVLGKIMYIFGGYEQLADCFSNDIHKLDTSTMTWTLVCTKGNPARWRDFHSATMLGNHMYVFGGRADRFGPFHSNNEIYCNRIRVFDTRTEAWLDCPHTPVLPEGRRSHSAFGYNGELYIFGGYNARLNRHFHDLWKFNPGSFTWKKIEPKGKGPCPRRRQCCCIVGDKIVLFGGTSPSPEEGLGDEFDLIDHSDLHILDFSPSLKTLCKLAVIQYSLDQSCLPHDIRWELNAMTTNSNISRPIVSSHG
Protein: Formate dehydrogenase (FDH) (EC 1.17.1.9) (NAD-dependent formate dehydrogenase) (D6CJK0)
Organism: Bacillus sp. F1(2010)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210}.
Interaction partners:
Sequence:
MAKIVCVLYDDPVTGYPKTYARDDLPKIECYPDGQTLPTPRAIDFQPGALLGSVSGELGLRKYLESNGHELVVTSSKDGDNSVLDRELADAEIVISQPFWPAYMTAERIKRAKKLKMIVTAGIGSDHTDLQAAMEHGITVAEVTYCNSNSVAEHVMMTTLALVRNYLPSYQWVLKGGWNIADCVERSYDLEGMHVGTVAAGRIGLRVLRLMKPFGTHLHYLDRHRLPESVEKELNLTHHTSLESLAKVCDVVTLNCPLHPETEHMINADSLKHFKRGAYLINTARGKLCDRDAVAAALESGQLAGYGGDVWFPQPAPADHPWRSMPHHGMTPHISGTSLSAQTRYAAGTREILECYFENRPIRNEYLIVQNGKLAGVGAHSYSAGNATGGSEEAARFKKSA
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 7.1.1.2) (Q17880)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein {ECO:0000256|RuleBase:RU364066}; Matrix side {ECO:0000256|RuleBase:RU364066}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase iron-sulfur protein 4
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- Acyl carrier protein
- Cytochrome c domain-containing protein
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 1
- Complex I-49kD
Sequence:
MASAAVSLGARLIGQNVPKVAVRGVVTSAQNANAQVKQEKTSFGNLKDSDRIFTNLYGRHDYRLKGAMARGDWHKTKEIILKGSDWILGELKTSGLRGRGGAGFPSGMKWGFMNKPFDGRPKYLVVNADEGEPGTCKDREIMRHDPHKLIEGCLIGGVAMGARAAYIYIRGEFYNEACILQEAINEAYKAGYLGKDCLGTGYNFDVFVHRGAGAYICGEETALIESLEGKQGKPRLKPPFPADIGLFGCPTTVTNVETVAVAPTICRRGGDWFASFGRERNRGTKLFCISGQVNNPCTVEEEMSVPLKDLIERHCGGVIGGWDNLLAIIPGGSSVPLMPKNVCDTVLMDFDALVAAQSGLGTAAVIVMNKQTDIVKCIARLSLFYKHESCGQCTPCREGCNWLNKMMWRFVDGKAKPSEIDMMWELSKQIEGHTICALGDAAAWPVQGLIRHFRPELERRMAEFHKQVLAEQGAKQISQ
Protein: Serine protease EspP (EC 3.4.21.-) [Cleaved into: Secreted autotransporter protein EspP (Extracellular serine protease plasmid-encoded EspP); Autotransporter protein EspP translocator] (O32591)
Organism: Escherichia coli
Function: Serine protease with cytotoxic effect. Disrupts actin cytoskeleton resulting cell detachment in vitro.
Subcellular location: [Serine protease EspP]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted autotransporter protein EspP]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Autotransporter protein EspP translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MNKIYSLKYSHITGGLIAVSELSGRVSSRATGKKKHKRILALCFLGLLQSSYSFASQMDISNFYIRDYMDFAQNKGIFQAGATNIEIVKKDGSTLKLPEVPFPDFSPVANKGSTTSIGGAYSITATHNTKNHHSVATQNWGNSTYKQTDWNTSHPDFAVSRLDKFVVETRGATEGADISLSKQQALERYGVNYKGEKKLIAFRAGSGVVSVKKNGRITPFNEVSYKPEMLNGSFVHIDDWSGWLILTNNQFDEFNNIASQGDSGSALFVYDNQKKKWVVAGTVWGIYNYANGKNHAAYSKWNQTTIDNLKNKYSYNVDMSGAQVATIENGKLTGTGSDTTDIKNKDLIFTGGGDILLKSSFDNGAGGLVFNDKKTYRVNGDDFTFKGAGVDTRNGSTVEWNIRYDNKDNLHKIGDGTLDVRKTQNTNLKTGEGLVILGAEKTFNNIYITSGDGTVRLNAENALSGGEYNGIFFAKNGGTLDLNGYNQSFNKIAATDSGAVITNTSTKKSILSLNNTADYIYHGNINGNLDVLQHHETKKENRRLILDGGVDTTNDISLRNTQLSMQGHATEHAIYRDGAFSCSLPAPMRFLCGSDYVAGMQNTEADAVKQNGNAYKTNNAVSDLSQPDWETGTFRFGTLHLENSDFSVGRNANVIGDIQASKSNITIGDTTAYIDLHAGKNITGDGFGFRQNIVRGNSQGETLFTGGITAEDSTIVIKDKAKALFSNYVYLLNTKATIENGADVTTQSGMFSTSDISISGNLSMTGNPDKDNKFEPSIYLNDASYLLTDDSARLVAKNKASVVGDIHSTKSASIMFGHDESDLSQLSDRTSKGLALGLLGGFDVSYRGSVNAPSASATMNNTWWQLTGDSALKTLKSTNSMVYFTDSANNKKFHTLTVDELATSNSAYAMRTNLSESDKLEVKKHLSGENNILLVDFLQKPTPEKQLNIELVSAPKDTNENVFKASKQTIGFSDVTPVITTRETDDKITWSLTGYNTVANKEATRNAAALFSVDYKAFLNEVNNLNKRMGDLRDINGEAGAWARIMSGTGSASGGFSDNYTHVQVGVDKKHELDGLDLFTGFTVTHTDSSASADVFSGKTKSVGAGLYASAMVDSGAYIDLIGKYVHHDNEYTATFAGLGTRDYSTHSWYAGAEAGYRYHVTEDAWIEPQAELVYGSVSGKQFAWKDQGMHLSMKDKDYNPLIGRTGVDVGKSFSGKDWKVTARAGLGYQFDLLANGETVLRDASGEKRIKGEKDSRMLMSVGLNAEIRDNVRFGLEFEKSAFGKYNVDNAVNANFRYSF
Protein: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (PP2A subunit A isoform PR65-beta) (PP2A subunit A isoform R1-beta) (P30154)
Organism: Homo sapiens (Human)
Function: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
- Striatin-interacting protein 1
- Striatin-3
- Striatin-4
Sequence:
MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA
Protein: Crossover junction endodeoxyribonuclease RuvC (EC 3.1.21.10) (Holliday junction nuclease RuvC) (Holliday junction resolvase RuvC) (Q9A3G6)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00034}.
Interaction partners:
- Holliday junction branch migration complex subunit RuvA
- Holliday junction branch migration complex subunit RuvB
- Uncharacterized protein
- Vitamin B12-dependent ribonucleotide reductase
- FtsW/RodA/SpoVE family cell cycle protein
Sequence:
MMNANRLPTRILGLDPGLRRTGWGVLAVEGSRMTHIAHGVITPDEKAEFADRLLHLFEGITAVIEQHRPDEAAVEEVFLNTNAQSTLKLGHARAAALIAPARAGLLVAEYSTRLVKKAVVGTGAADKAQIGFMIARLLPTAGKTTADCADALAVAITHANLRVANRRVA
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q583L5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Variant surface glycoprotein
Sequence:
MHHFQLQLPYVEILLMVATQPIATNKDSTTVKAACHEVAFNDKLAAAFKQKIDGLAAKKSQLLKEAEALDAAACLATDHKTKKATRMLASIGSSRAAATEANADAVKQLKASIETLKRRNAQLMAAIAFNTKGDLTISHDASAQKSDLIGGAGAKSCSVTITQPPKNEHGCQSSLVNDPAINDDVNNVQNLDSYQAIHDKAFQLTDIAADIGNKGDYGSATPATHNKKIACVDTGDRSNKLGSVAKGIILTNFARKADWNTPTKNTIKSKGDGTDCEDDQDSDKKAFVTAKAAGYAICNGRRQTVTEPETLSQLTMDALKEQKDVQEAAMLITAGPTAELPDTDKQKEAVVALVGEGKTTVHDKFLKDMEANKLDFKIGDKHVNKGIVSISGTEDYARAIGFCLGDQYRKEKAQKKVESVTAAAPENNKECKGETDEGKCNEKVGCEFKDGKCEAKVTETTGTNGKITNTTESNSFVINKAPILLEFLAL