wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase II large subunit (Pol II) (EC 2.7.7.7) (Exodeoxyribonuclease large subunit) (EC 3.1.11.1) [Cleaved into: Pho polC intein (Pho pol II intein)] (O57861)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).
Interaction partners:
- Proliferating cell nuclear antigen PCNA N-terminal domain-containing protein
- DNA polymerase II small subunit
- DNA polymerase sliding clamp
- ORC1-type DNA replication protein
- DNA polymerase
Sequence:
MELPKEMEEYFSMLQREIDKAYEIAKKARAQGKDPSLDVEIPQASDMAGRVESLVGPPGVAERIRELVKEYGKEIAALKIVDEIIDGKFGDLGSKEKYAEQAVRTALAILTEGVVSAPIEGIASVKIKRNTWSDNSEYLALYYAGPIRSSGGTAQALSVLVGDYVRRKLGLDRFKPSEKHIERMVEEVDLYHRTVSRLQYHPSPEEVRLAMRNIPIEITGEATDEVEVSHRDIPGVETNQLRGGAILVLAEGVLQKAKKLVKYIDKMGIEGWEWLKEFVEAKEKGEEIEEEGSAESTVEETKVEVDMGFYYSLYQKFKSEIAPNDKYAKEIIGGRPLFSDPSRNGGFRLRYGRSRVSGFATWGINPATMILVDEFLAIGTQLKTERPGKGAVVTPVTTIEGPIVKLKDGSVVKVDDYKLALKIRDEVEEILYLGDAVIAFGDFVENNQTLLPANYCEEWWILEFTKALNEIYEVELKPFEVNSSEDLEEAADYLEVDIEFLKELLKDPLRTKPPVELAIHFSEILGIPLHPYYTLYWNSVKPEQVEKLWRVLKEHAHIDWDNFRGIKFARRIVIPLEKLRDSKRALELLGLPHKVEGKNVIVDYPWAAALLTPLGNLEWEFRAKPLHTTIDIINENNEIKLRDRGISWIGARMGRPEKAKERKMKPPVQVLFPIGLAGGSSRDIKKAAEEGKVAEVEIALFKCPKCGHVGPEHICPNCGTRKELIWVCPRCNAEYPESQASGYNYTCPKCNVKLKPYAKRKIKPSELLKRAMDNVKVYGIDKLKGVMGMTSGWKMPEPLEKGLLRAKNDVYVFKDGTIRFDATDAPITHFRPREIGVSVEKLRELGYTHDFEGNPLVSEDQIVELKPQDIILSKEAGKYLLKVAKFVDDLLEKFYGLPRFYNAEKMEDLIGHLVIGLAPHTSAGIVGRIIGFVDALVGYAHPYFHAAKRRNCFPGDTRILVQINGTPQRVTLKELYELFDEEHYESMVYVRKKPKVDIKVYSFNPEEGKVVLTDIEEVIKAPATDHLIRFELELGSSFETTVDHPVLVYENGKFVEKRAFEVREGNIIIIIDESTLEPLKVAVKKIEFIEPPEDFVFSLNAKKYHTVIINENIVTHQCDGDEDAVMLLLDALLNFSRYYLPEKRGGKMDAPLVITTRLDPREVDSEVHNMDIVRYYPLEFYEATYELKSPKELVGVIERVEDRLGKPEMYYGLKFTHDTDDIALGPKMSLYKQLGDMEEKVKRQLDVARRIRAVDEHKVAETILNSHLIPDLRGNLRSFTRQEFRCVKCNTKFRRPPLDGKCPICGGKIVLTVSKGAIEKYLGTAKMLVTEYKVKNYTRQRICLTERDIDSLFETVFPETQLTLLVNPNDICQRIIMERTGGSKKSGLLENFANGYNKGKKEEMPKKQRKKEQEKSKKRKVISLDDFFSRK
Protein: Chrysophsin-1 (P83545)
Organism: Pagrus major (Red sea bream) (Chrysophrys major)
Function: Has antibacterial activity against Gram-positive bacteria B.subtilis ATCC 6633, L.garvieae ATCC 49156 and S.iniae F-8502, and Gram-negative bacteria E.coli WT-2, V.anguillarum ATCC 19264, V.penaeicida KHA, V.harveyi ATCC 14126, V.vulnificus ATCC 33148, A.salmonicida NCMB 1102 and P.putida ATCC 12633. Has hemolytic activity against human red blood cells. Seems to disrupt the membranes by adopting an alpha helical conformation. May play a significant role in innate host defense.
Subcellular location: Secreted.
Interaction partners:
Sequence:
FFGWLIKGAIHAGKAIHGLIHRRRH
Protein: Antiholin (Protein rI) (P13304)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Involved in lysis inhibition. Senses superinfections and inhibits the holin, thereby delaying the host cell lysis timing. The genomic DNA from the superinfecting phage bound to the complex holin-antiholin probably serves as a signal for the lysis inhibition and blocks the holin multimerization.
Subcellular location: Host periplasm {ECO:0000255|HAMAP-Rule:MF_04105, ECO:0000269|PubMed:34456892}.
Interaction partners:
Sequence:
MALKATALFAMLGLSFVLSPSIEANVDPHFDKFMESGIRHVYMLFENKSVESSEQFYSFMRTTYKNDPCSSDFECIERGAEMAQSYARIMNIKLETE
Protein: ATP synthase F(1) complex subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) (P06576)
Organism: Homo sapiens (Human)
Function: 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:25168243}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243}.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS
Protein: Cationic amino acid transporter 1 (Q9URZ4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Major permease specifically involved in arginine and lysine uptake.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18219492}; Multi-pass membrane protein {ECO:0000269|PubMed:18219492}. Cell tip {ECO:0000269|PubMed:18219492}. Note=enriched toward the growing ends of the cells.
Interaction partners:
- Uncharacterized protein C18H10.20c
- E3 ubiquitin-protein ligase pub1
- Ribose-phosphate pyrophosphokinase 1
Sequence:
MSHSDFNMEPEYVSFSDKDTKSILNESKSSLKDVKPSLEEKSYITPGLVDDVEPKGKNFVVRFFDDFKPAKATGEDGTALKRSLKSRHMQMISIGGAIGTGLYVGSGSSLADGGPASVIINYSLIGIMMFFIVYALGEMAVAYPVAGGFNTYATRFIDPAWGFAVSWNYFINYFVTFPLELTTCAITFRYWTDINSAAWISIFLVVIIIVNLFGVRAYGEVEFILSTVKVVATFGFIILAIIINCGGVPTDHRGYIGGSIIKHKPFRHGFKGFCSVFTTAAFSFSGTEVIGLAAAEVDNPQKALPHAVKQVFWRIAIFYVVSLILIGLLISPDDPNLMGNGSTSVSPFVLAIKEANIKGLPSVFNAVIIISVVSVTNSSTYTAGRTLHGMANLKQAPSFFKYTDRLGRPLLAMIVVLLFGFFAYINEADKNGNDVSDTVFNWLLALSGLSNFFTWGSICLCHIIFRLAFKKQGHSLKELGFVSPMGIWGSCIGLFFNILCLMAQFYVSLFPIGGKPNANDFFQGYLAAPVTLAFFIGYKIYDRSHIPSLDKLDITTGLKTYENLDEEEDEPTTASKRIFKKISSVFC
Protein: E3 ubiquitin-protein ligase RNF5 (EC 2.3.2.27) (RING finger protein 5) (Ram1 homolog) (HsRma1) (Q99942)
Organism: Homo sapiens (Human)
Function: Membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin,thereby regulating cell motility and localization of PXN/paxillin. Catalyzes ubiquitination of Salmonella type III secreted protein sopA. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses. Catalyzes ubiquitination and subsequent degradation of ATG4B, thereby inhibiting autophagy.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9533025}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:19285439}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19285439}; Multi-pass membrane protein {ECO:0000255}. Note=Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles. {ECO:0000269|PubMed:9533025}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 J1
- Cystic fibrosis transmembrane conductance regulator
- Derlin-1
- E3 ubiquitin-protein ligase RNF185
- E3 ubiquitin-protein ligase AMFR
- E3 ubiquitin-protein ligase CHIP
- Stimulator of interferon genes protein
- Mitochondrial antiviral-signaling protein
- E2 ubiquitin-conjugating enzyme
- Ubiquitin-conjugating enzyme E2 E3
Sequence:
MAAAEEEDGGPEGPNRERGGAGATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPERQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDTGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGTGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI
Protein: Bicoumarin synthase ktnC (EC 1.14.-.-) (Cytochrome P450 monooxygenase ktnC) (Kotanin biosynthesis cluster protein C) (A2QK67)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.
Interaction partners:
Sequence:
MHKSAALSLRDAQFADMNMYCDVTDRTPIEAVHSCNNAESLNILNKLLARETDTALSQIFEQPTGKDWKELNTLQTILSLCSTVTMALLLGPDTAPDPVLHHHSTSFGEAIMSSCYRRTGYPRILRPFVWRFSSECRNLRKHFSLVRERLVPEVARRVAAARAADKTKDVRPSSLLDALIAAAFDNGSLSPDDQGRNDAAQVQLLADDLIFYHFELCKPTAFNIIFQLYAIMDHPEYKAPLREEALQALKLTNGDWTVETLKHAPKLESFTKETFRLYDISGFVSFRRVMKPLTLNSIGLSLRPGTILLSPCRNVHLDPEIYEDPTTFNGYRFYDSSREVCSPRVATTSLTFLTFSHGAGSCPARVLATQICRTIFIKFLLQYDVEPVQKEILPYGFTSGPVYMPNPSVMMRIRPRSDGK
Protein: Conserved protein (I6Y242)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- PGL/p-HBAD biosynthesis glycosyltransferase Rv2957
- Conserved protein
- GDP-L-fucose synthase
- Secreted protein
- Methyltransferase type 12 domain-containing protein
- Probable transposase
- PGL/p-HBAD biosynthesis glycosyltransferase Rv2958c
Sequence:
MKSLKLARFIARSAAFEVSRRYSERDLKHQFVKQLKSRRVDVVFDVGANSGQYAAGLRRAAYKGRIVSFEPLSGPFTILESKASTDPLWDCRQHALGDSDGTVTINIAGNAGQSSSVLPMLKSHQNAFPPANYVGTQEASIHRLDSVAPEFLGMNGVAFLKVDVQGFEKQVLAGGKSTIDDHCVGMQLELSFLPLYEGGMLIPEALDLVYSLGFTLTGLLPCFIDANNGRMLQADGIFFREDD
Protein: GH01208p (Q7K3Z8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Uncharacterized protein, isoform C
- CG7953 protein
- CG7916 protein
- CG8997 protein
- GH07914p
Sequence:
MHKAIKNKSRLLCGLKNSKADLTTAKFILYYGPTVADSDIYDLTDFQSLLEDEHLDLGKNTVLYLHGYLEDPDVESIHVIAEAYLERKDTNLIVLDWGELADGNYMFDAFPNLKQLGPELAKVLLKMFDHGLDIEKFHIVGHSMGGQLAGLLGREITKRTKGVRKIKRISALDPAFPLFYPGTHLSANDAEFVDVIHTDAWLYGAPTSTGTADFWPNGGYSLQPGCPKRNYKMLSDNDLSSHRRSWWFWAESVSDRYPIGFDAVPAKKWSDFKQNKIVENCPPVVMGHHCPTTIHGDFYLQTNGHTPFARGKEGTVYVDPKDLLGNTHSITCDCPSEKTN
Protein: Uncharacterized ATP-dependent helicase IRC5 (EC 3.6.4.-) (Increased recombination centers protein 5) (P43610)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Is probably involved in a pathway contributing to genomic integrity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA repair protein RAD51
- DNA repair and recombination protein RAD52
- Benzil reductase
Sequence:
MSRCSNAALMTVVEDAVGARVAARTRNMSNGVNYREKEVNDLTADISDSDSDLDSEDNKHGKGDNDTAPIWLQDDVHSDEDIQLDSEDDSDTEAVQAQVVDKLAKDTKSEQKSLDDELSEMDTKTVSLKLKKLNEFVRQSQVYSSIIADTLLHRSNEVANANTKDNSNSDDEEHSSKKRKTKKKSITDFFKKQKKNEDTTTQNGAPDDAAIKQPRLLKNCILKPYQLEGLNWLITLYENGLNGILADEMGLGKTVQSIALLAFIYEMDTKGPFLVTAPLSTLDNWMNEFAKFAPDLPVLKYYGTNGYKERSAKLKNFFKQHGGTGIVITSYEIILRDTDLIMSQNWKFLIVDEGHRLKNINCRLIKELKKINTSNRLLLTGTPLQNNLAELWSLLNFIMPDIFADFEIFNKWFDFDSLNLGSGSNSEALNKLINDELQKNLISNLHTILKPFLLRRLKKVVLANILPPKREYIINCPMTSAQEKFYKAGLNGKLKKTMFKELIKDFFTLNDEYIGHVSNRSIRDFINYKLSGNETSNTDNKINPTLLQMDKLYKKNLQMEISNKKLQNMMMQLRQIIDSTFLFYFPYLHPEDLTLETLLKTSGKLQILQKLIPPLISEGHKVLIYSQFVNMLDLIEDWCDLNSFATFRIDGSVNNETRKDQLEKFNSSKDKHNIFLLSTRAAGLGINLVGADTVVLFDSDWNPQVDLQAMDRCHRIGQESPVIVYRLCCDNTIEHVILTRAANKRNLERMVIQMGKFNNLKKLALNEGSFLKANKAGVNVTNKDLVQELSMLLMSDESNIGFENGGQKENKATEGQLTDKEVEELTNRSLEAYKANRVVDLPHVKLFETTSGL
Protein: 30-kDa cleavage and polyadenylation specificity factor 30 (EC 3.1.21.-) (Protein OXIDATIVE STRESS TOLERANT 6) (Zinc finger CCCH domain-containing protein 11) (AtC3H11) (A9LNK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation. May interact with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition (By similarity). Mediates poly(A) site selection. Binds RNA in a calcium-dependent manner. Exhibits endonuclease activity with an ability to nick and degrade linear as well as circular single-stranded RNA that leaves RNA 3' ends with hydroxyl groups, thus mediating processing of the pre-mRNA as a prelude to the polyadenylation. Involved in the post-transcriptional control, probably via poly(A) addition, of the responses of plants to stress, especially genes mediating tolerance to oxidative stress. Plays a role in the regulation of salicylic acid (SA) production via the control of messenger RNA 3' end processing, thus being a key component of programmed cell death and plant immune responses required for resistance to virulent Pseudomonas syringae pv tomato DC3000 (Pst).
Subcellular location: Nucleus {ECO:0000269|PubMed:16500995, ECO:0000269|PubMed:19573236}. Cytoplasm {ECO:0000269|PubMed:19573236}. Note=Localized in the cytoplasm when not in complex or when associated with CPSF100, but move to the nucleus when associated with the cleavage and polyadenylation specificity factor (CPSF) subunits CPSF160 or CPSF73s. {ECO:0000269|PubMed:19573236}.
Interaction partners:
- Cleavage stimulation factor subunit 50
- Nuclear poly
- Polyadenylation and cleavage factor homolog 1
- Cleavage stimulating factor 64
- Pre-mRNA cleavage factor Im 25 kDa subunit 2
- Cleavage stimulation factor subunit 77
- Polyadenylation and cleavage factor homolog 4
- FIP1[V]-like protein
- Nuclear poly
- Cleavage and polyadenylation specificity factor subunit 1
Sequence:
MEDADGLSFDFEGGLDSGPVQNTASVPVAPPENSSSAAVNVAPTYDHSSATVAGAGRGRSFRQTVCRHWLRGLCMKGDACGFLHQFDKARMPICRFFRLYGECREQDCVYKHTNEDIKECNMYKLGFCPNGPDCRYRHAKLPGPPPPVEEVLQKIQQLTTYNYGTNRLYQARNVAPQLQDRPQGQVPMQGQPQESGNLQQQQQQQPQQSQHQVSQTLIPNPADQTNRTSHPLPQGVNRYFVVKSNNRENFELSVQQGVWATQRSNEAKLNEAFDSVENVILIFSVNRTRHFQGCAKMTSRIGGYIGGGNWKHEHGTAQYGRNFSVKWLKLCELSFHKTRNLRNPYNENLPVKISRDCQELEPSVGEQLASLLYLEPDSELMAISIAAEAKREEEKAKGVNPESRAENPDIVPFEDNEEEEEEEDESEEEEESMAGGPQGRGRGRGIMWPPQMPLGRGIRPMPGMGGFPLGVMGPGDAFPYGPGGYNGMPDPFGMGPRPFGPYGPRFGGDFRGPVPGMMFPGRPPQQFPHGGYGMMGGGRGPHMGGMGNAPRGGRPMYYPPATSSARPGPSNRKTPERSDERGVSGDQQNQDASHDMEQFEVGNSLRNEESESEDEDEAPRRSRHGEGKKRR
Protein: LD45549p (Q8SZZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGQRDNPFINPWANGGGGDVDGFGNNAGGAGGFAGNSFGGGAGGPFGGGSFGNNGFGGGPSDFGGNSGNFGQAQGTNSLPSLGSFSQNQGGTSSLPSLGSFGQNPGGPGGLGNGLSGGANGGVGTLGGANGAGGFNAVGGANGGPNGSPNAATNVPQGHDPNNSTQVTIPKELAGAIIGKGGGRIRRIRNESSAYITIDEPLPNSNDRIITISGTPKQIQMAQYLLQQSVHENGRRNI
Protein: Sporulation initiation phosphotransferase F (EC 2.7.-.-) (Stage 0 sporulation protein F) (P06628)
Organism: Bacillus subtilis (strain 168)
Function: Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Response regulator aspartate phosphatase H
- Sporulation initiation phosphotransferase B
- Sporulation kinase B
- Sporulation kinase C
- Sporulation kinase A
- Sporulation kinase E
- Sporulation kinase D
- Response regulator aspartate phosphatase B
- Response regulator aspartate phosphatase J
- Response regulator aspartate phosphatase A
Sequence:
MMNEKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLPLKSN
Protein: Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3 (Probable rhamnose biosynthetic enzyme 3) (AtRHM3) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)] (Q9LH76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II). Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose (By similarity).
Interaction partners:
- UDP-glucose 6-dehydrogenase 4
- UDP-glucose 6-dehydrogenase 3
- UDP-glucose 6-dehydrogenase 2
- Putative UDP-glucose 6-dehydrogenase
- UDP-glucose 6-dehydrogenase 1
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3
- UDP-glucose 4-epimerase 2
- UDP-glucose 4-epimerase 5
- UDP-glucose 4-epimerase 4
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1
Sequence:
MATYKPKNILITGAAGFIASHVANRLVRSYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASADLVNYLLITEEIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDASVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMNGKPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEVNHVYNIGTTRERRVIDVANDISKLFGIDPDSTIQYVENRPFNDQRYFLDDQKLKKLGWCERTNWEEGLRKTMEWYTENPEWWGDVSGALLPHPRMLMMPGDRHSDGSDEHKNADGNQTFTVVTPTKAGCSGDKRSLKFLIYGKTGWLGGLLGKLCEKQGIPYEYGKGRLEDRASLIADIRSIKPSHVFNAAGLTGRPNVDWCESHKTETIRVNVAGTLTLADVCRENDLLMMNFATGCIFEYDAAHPEGSGIGFKEEDKPNFTGSFYSKTKAMVEELLREFDNVCTLRVRMPISSDLNNPRNFITKISRYNKVVNIPNSMTILDELLPISIEMAKRNLRGIWNFTNPGVVSHNEILEMYKSYIEPDFKWSNFNLEEQAKVIVAPRSNNEMDGAKLSKEFPEMLSIKDSLIKYVFEPNKRT
Protein: Arouser, isoform C (Arouser, isoform D) (RE61916p) (Q9VPU7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVNHHSNGGGSAGNSSGSLRGGGAHGGGGGGGDYSGDDRSGGGEERERLESDLHDKPTYLLEHLATFTVNKESGIVYPADGMRRLLQLEKTTGIWSQKMQLCLDYQWVLIMDYETGNIIERFPASLVQEPTAFTSNDAMELYNNILVFIVSGGGGSRSEMHIFQSQSVSAVHLVEDLKQLRSGKMITQQRGATPTQSGGGGASSMAMMMSKTSSSSSHSRVELHQHREQRAERERERDRDRERESHHHMHQRSSMEQYGIRAGVGVSGDDVAHISGETDSEHGGIGGGGATERDETSSTSSEKYERDVAVLNHCFDDIEKFIARLQHAAAASRELERRRRNRKSKKRDPGEGLLTLRTRPPHEKEFVDIFAKFKLSFNLLAKLKAHIHDPNAPELVHFLFTPLALIVEASSDTYYESQLPARVVNPLLTREAINLLINCVTSKETELWRSLGDAWVIPRDQWKDDVGSYHPVFLDGWSPDYLINDELEPPPNSPPAHVSKRRLEVQAGSGLNGRGGGGYDDYDSGNGMNMAMGIEKYTIHHGNDGLRERERERDRERAGAISASDFNARSELSFDSIEGRGGGAAGHGHGHGHGPGAGPTLSAITAGLQNLHTRESRSGNGYGAGAGPGPSSELGGGGRGLPNVSDDQMLESWLEDLQATGAKIVLVTYPRTANNDKELSVMRGEYLEILDDTRKWWKARNMRGQVAHVPHTIVTPFNFGDGDGAQFYGQQQQPPTGPTGPGNKSRSGDNPGMEQRSPDPTDMMRSKHLGKKGEFRYF
Protein: Origin recognition complex subunit 5 (Q24169)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Double parked, isoform A
- Origin recognition complex subunit 6
- DNA replication licensing factor Mcm5
- Origin recognition complex subunit 2
- Cell division control protein
- Origin recognition complex subunit 4
- Origin recognition complex subunit 3
- Origin recognition complex subunit 1
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm2
Sequence:
MEAICSSLEPLFPCREAAIETLGELIGDSSETYPSAIYLFGHSGTGKTALTRAFLKECGKRQNVRTAHLNAIECYTTKIMLEILLDSLAPDQGDALKVDNMLDFVEQLRRQAATRVEDQGFLIAVDNAERLRDMDANVLPVLLRLQELTNLNLCVILLSQLPFEKFYNKTGLSEIVCLHLAQYNKAETQRILGSDFQQVRNQLLEQFAQDKKRLEICQEAVTEDFYNNYLNLFLSVFYKACRDVPELQLTARKCLSTYLEPVLDGTVDATDISRLWRHIAGPLRSALTQIYMRIEKPAEEVEDFTAIEDQSVRKLAQSLELPYYAKFLLIAAFLASHNAAKQDKRLFVKHHGKQRKRMQTVNARAKTTEKMSTTLGPKSFSIDRLLAIFYAILEEKVGLTCNLLSQISTLVHLNLLSFVSGEQNIMEGSARLQCTIGLEFVLQIGKVVGFNVRQYLCDFM
Protein: Pre-mRNA-processing factor 40 homolog B (Huntingtin yeast partner C) (Huntingtin-interacting protein C) (Q6NWY9)
Organism: Homo sapiens (Human)
Function: May be involved in pre-mRNA splicing.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:10958656}.
Interaction partners:
- RNA-binding protein 25
- Splicing factor U2AF 65 kDa subunit
- Cell division cycle 5-like protein
- U1 small nuclear ribonucleoprotein C
- Splicing factor 3A subunit 1
- Small nuclear ribonucleoprotein E
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-processing factor 39
- Small nuclear ribonucleoprotein F
Sequence:
MMPPPFMPPPGIPPPFPPMGLPPMSQRPPAIPPMPPGILPPMLPPMGAPPPLTQIPGMVPPMMPGMLMPAVPVTAATAPGADTASSAVAGTGPPRALWSEHVAPDGRIYYYNADDKQSVWEKPSVLKSKAELLLSQCPWKEYKSDTGKPYYYNNQSKESRWTRPKDLDDLEVLVKQEAAGKQQQQLPQTLQPQPPQPQPDPPPVPPGPTPVPTGLLEPEPGGSEDCDVLEATQPLEQGFLQQLEEGPSSSGQHQPQQEEEESKPEPERSGLSWSNREKAKQAFKELLRDKAVPSNASWEQAMKMVVTDPRYSALPKLSEKKQAFNAYKAQREKEEKEEARLRAKEAKQTLQHFLEQHERMTSTTRYRRAEQTFGELEVWAVVPERDRKEVYDDVLFFLAKKEKEQAKQLRRRNIQALKSILDGMSSVNFQTTWSQAQQYLMDNPSFAQDHQLQNMDKEDALICFEEHIRALEREEEEERERARLRERRQQRKNREAFQTFLDELHETGQLHSMSTWMELYPAVSTDVRFANMLGQPGSTPLDLFKFYVEELKARFHDEKKIIKDILKDRGFCVEVNTAFEDFAHVISFDKRAAALDAGNIKLTFNSLLEKAEAREREREKEEARRMRRREAAFRSMLRQAVPALELGTAWEEVRERFVCDSAFEQITLESERIRLFREFLQVLEQTECQHLHTKGRKHGRKGKKHHHKRSHSPSGSESEEEELPPPSLRPPKRRRRNPSESGSEPSSSLDSVESGGAALGGRGSPSSHLLGADHGLRKAKKPKKKTKKRRHKSNSPESETDPEEKAGKESDEKEQEQDKDRELQQAELPNRSPGFGIKKEKTGWDTSESELSEGELERRRRTLLQQLDDHQ