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Database: UniProt
Entry: V7CNQ5_PHAVU
LinkDB: V7CNQ5_PHAVU
Original site: V7CNQ5_PHAVU 
ID   V7CNQ5_PHAVU            Unreviewed;      3750 AA.
AC   V7CNQ5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=PHAVU_002G189700g {ECO:0000313|EMBL:ESW30875.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW30875.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034494}.
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DR   EMBL; CM002289; ESW30875.1; -; Genomic_DNA.
DR   RefSeq; XP_007158881.1; XM_007158819.1.
DR   STRING; 3885.V7CNQ5; -.
DR   EnsemblPlants; ESW30875; ESW30875; PHAVU_002G189700g.
DR   GeneID; 18638423; -.
DR   Gramene; ESW30875; ESW30875; PHAVU_002G189700g.
DR   KEGG; pvu:PHAVU_002G189700g; -.
DR   eggNOG; KOG0939; Eukaryota.
DR   OMA; ADEMKYG; -.
DR   OrthoDB; 1214833at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000226; Chromosome 2.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd14327; UBA_atUPL1_2_like; 1.
DR   Gene3D; 6.10.250.1630; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR   InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF06012; DUF908; 2.
DR   Pfam; PF06025; DUF913; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF14377; UBM; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50330; UIM; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1298..1339
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          3409..3750
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          910..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1521..1559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2036..2057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2153..2221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2385..2405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2425..2457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2629..2653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2956..2978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3028..3069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1521..1551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2037..2051
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2157..2189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2204..2221
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2425..2441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2629..2652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2959..2973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3028..3057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3717
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   3750 AA;  411775 MW;  19F7F8B1176FD624 CRC64;
     MKLKRKRALE VPPKIRCFID RVTSVPLEKI EEPLKGFVWE FDKGDFHHWV DLFNHFDSYF
     EKYIKPRKDL LIDDDFLDLD PPFPRIAILQ ILRVIRTILD NCTNKHFYSS YEQHLSALLA
     STDPDVVEAS LDTLATFLKK TVGKYSIRDT SLNSKLYALA QGWGGKEEGL GLIASCVPDG
     CDRIACELGC TLHFEFYALN ESERDIKVAE PLVQGLQIIH LCDIDKRVET DLELLHKLVT
     EYKVPASLRF SLLSRLRYAR AFGSLASRQQ YTCIRLYAFI VLIQACADAD DLVSFFNAEP
     GFINELVSLL SYEDAVLERI RILCLHALAA LCQDRSRQQS VQTAVTSGGH RGILSSLMQK
     AIDSVISDTS KWSVYFAEAL LSLVSVLVST SSGCSAMREA GFIPTLLPLL KDTNPQHLHL
     VEKSVRILEA FMDYSNPAAA LFRDLGGLDD TISRLKIEVS HVENGGKQPD EKSEFSSRSV
     NMVRSSSRLD DVQQPLYSEP LISYHRRLLM KALLRAISLG TYAPGNTARI YGSEENVLPH
     CLCIIFRRAK DFGGGVFSLA ATVMSDLIQK DPTCFPVLDA AGLPSAFLDA IMDDVLNSSE
     AITCIPQCLD ALCLNSNGLQ AVKDRNSLRC FVKVFTSKTY LRALAGDTPA SLSSGLDELM
     RHAASLRGPG VEMLVEILES ISKIGSAVES SSLSSDPSSS TSVPMEMDGE EKNLILPNNE
     SSKADDAGHI SEPSPDMSIM NVESFLPDCV NNIARLLETI LQNADTCRIF VEKKGIEAIL
     QLVTLPLMPA SVSVGHSISV AFKNFSPQHY VSLARAVCSF LREHLRSTNE LLDLVGGTQL
     ALVESAKQTK VLKYLSSLEA VLTLSVFLLK GTSTVVSELS TSDADVLKDL GKTYKEIIWQ
     ISLCNDSKAE EKKNADQEPE VSQVPPSTAV ERESDDDSNI QTVRYTNPVF GRNGSHSLWS
     GEREFLSVVR AGESLHRRSR HGISRIRGGR TGRHLEALNI DSEAPPSGLE APSSQDMKKK
     SPDVLVSEIL NKLASTLRSF FTALVKGFTS PNRRRADSGS LSSASKTLGA VLATNFLEAL
     SFSGHSTYAS GLELSLSVKC RYLGKVVDDM AALTFDSRRR SCYTAMVNNF YVHGTFKELL
     TTFEATSQLL WTLPCSLPSP DNDVGKKGEG GKLSHNTWLL DTLQSYCRLL EYFVNSSHLL
     SPTSASQAEL LVQPVAVGLS IGLFPVPRDP EVFVRMLQSQ VLDVILPVWN HPMFSSCSPG
     FIASIISLVT HVYSGVGDVK RSRSNIVGST NQRFMPPPPD ETTIATIVEM GFSRARAEEA
     LRRVETNSVE MAMEWLFSHT DDPVQEDDEL ARALALSLGS SSESTKAETA EKTIDVLTEE
     GHVKKPPVDD ILAASVKLFQ TSDSVSFQLT DLLVTLCSQS KGDDRPKVIS YLLQQLKLCP
     LDFSQDNCAL SVLAHILALL LFEDVSTREI AAQNGIISSI IDILTNFKGR QELGKELPVP
     KCISALLLTL DQMVQSRPKV ENVEGTQTGS LPDSSGEHGS LQISDTVVPK EKNSNGNEKE
     PAVAFESILG KSTGFATVEE SHKLLDVACD LIKQHVPAVV MQAVLQLCAR LTKTHALALQ
     FLENGGLAAL FNLPRICFFP GYDSVVSAIV RHLLEDPQTL QTAMELEIRQ TLSGNRHSGR
     VSPRSFLTSL APVISRDPNV FMKAAAAVCQ LETSGGRTVV VLSKEKEKEK SKSSSIEAGL
     SSNECVRIPE SKSHDGQGKC LKSHKKVPVN LTQVIDQLLE IVLKYPPMKG MEESERDSTF
     MEIDEPTMKV KGKSKVDEAA SIEPESEKST GLVKVTFVLK LLSDILLMYG HAVGVILRRD
     SEMCQFRGSN QPSGHSGIIH HVLHRLLPLS VDKSAGPDDW RGKLSEKASW FLVVLCGRSG
     EGRKRVTNEL VKELMSFSNF ESNSMRNSLL PDKRLFTFVD LVYSILSKNS SSGSLPGSGY
     SPDIAKSMID GGIIQCLTSI LQVVDLDHPD APKIVNLILK GLEGLTRAAN ASEQIFKSDG
     TEKKRSTGLN DRSDDQITAP SATEAVAHDQ NVGSQEAIID TMDNAHDQGT SQGDNCVDNP
     NQSVEQDMRV DEGGTLAQDP PMELGMDFMR EEMGEGGVLH NPDQIEMTFH VENRADDDMG
     DEDDDMGDDG DEDEDDDDGE DEDEDIAEDG GGMMSLADTD VEDHDDVGFG DEYNDEMIDE
     DDDDFHENRV IEVRWREALD GLDHLQILGQ PGFIDVAAEP FEGVNVDDLF RLQSFERRRQ
     TGRSSFERSA TEVNGFQHPL LVRPPPSGDF VSMWSSSGNS TSRDSDTLSS GNLDVAHFYM
     FDAPILPYDH VPSSLFGDRL GGAAPPPLTD YSVGMGSLHL PGRRVLGNGR WTDDGQPQGS
     AQAASIAQAV EEQFLAQLNS VAPASSPVER QLQNSGEQEN KSDALASHDG PILTAGTDST
     CQQIESPEQE NGNGEEINVD SVARDTGEDL PANEPMSVQP VSLNIMPNGI DCTVIEGNVT
     PDENVEIFVN SSNAAAIQCE RAADVLTSIH DVPVESMECN GSSTADGQHT NLELGGSGFE
     TPNSGDCHIP SIYASADVDM AGTGAEGNQS EQPTVSEDRR DELLSAQNTE VAPDASQADQ
     VSANNEASGA NTIDPTFLEA LPDDLRAEVL ASQQAQSVQP PAYAPPSAED IDPEFLAALP
     PDIQAEVLAQ QRAQRVAQQA EGQPVDMDNA SIIATFPADL REEVLLTSSE AVLSALPSPL
     LAEAQILRDR AMSHYQARSL FGSSHRLNNR RNGLGFDRRP VMDRGVGVTI GRRSALTDSL
     KVKEIEGEPL LDATALKALI RLLRLSQPLG KGLLQRLLLN LCAHTVTMAT LIYLLLDMIE
     PEAEGSVSRS ATLNSQRLFG CHSNTVYGQS QLLDGLPPLV FRRILEILTY LATNHSAVAK
     LLFHFDQSII SDSSRPVNVH TNEKGKEKVT EEGPTLNPSK AETGVVPLVL FLKLLSRPLF
     LRSNAHLEQV MGLIQVIVDT AASKLESQSQ SEKEMADTQN LSASEAPSNT EKDAPLVESD
     SNQQDKRADM RVCHSEGKKN VDMYIIFLQL PQSDLRNLCS LLGREGLSDK MYMLAGEVLK
     KLAFIVPSHR KFFTVELSES AHALTGSAIS ELVTLQKTNM LGLSAGSMAG AAILRVLQAL
     SSLTSLNTVG EMDMDNGVDQ HDDQATIWNL NTALEPLWQE LSNCISAAEM QLGQSSFSPN
     MSNINVAENL QGSSTSPPLP PGTQRLLPFI EAFFVLCEKL QANESFMQQD HGNATAREVK
     ESAGCSASTS VKGGGDSLRK LDGAITFTRF AEKHRRLSNA FIRQNPGLLE KSLSMMLKAP
     RLIDFDNKRA YFRSRIRQQH DQHLSGPLRI SVRRAYILED SYNQLRMRPT QDLKGRLNVQ
     FQGEEGIDAG GLTREWYQLL SRVIFDKGAL LFTTVGNNAT FQPNPNSVYQ TEHLSYFKFV
     GRVVGKALFD GQLLDVYFTR SFYKHILGVK VTYHDIEAVD PDYYKNLKWM LENDVSDVPD
     LTFSMDADEE KHILYEKNEV TDYELKPGGR NIRVTEETKH EYVDLVAEHL LTNAIRPQIN
     SFLEGFNELV PRELISIFND KELELLISGL PEIDLDDLKA NTEYTGYTVA SNVVQWFWEV
     VKTFNKEDMA RLLQFVTGTS KVPLEGFKAL QGISGPQRFQ IHKAYGAPDR LPSAHTCFNQ
     LDLPEYTSKE QLQERLLLAI HEASEGFGFG
//
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