UniProt: A0A0S3RMD6

Database: UniProt
Entry: A0A0S3RMD6_PHAAN

LinkDB:  A0A0S3RMD6_PHAAN 
Original site:  A0A0S3RMD6_PHAAN

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (10)   
   Pfam (5)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (25)   

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ID   A0A0S3RMD6_PHAAN        Unreviewed;      3644 AA.
AC   A0A0S3RMD6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-JUN-2023, entry version 32.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=Vigan.03G147800 {ECO:0000313|EMBL:BAT81688.1};
GN   ORFNames=VIGAN_03147800 {ECO:0000313|EMBL:BAT81688.1};
OS   Vigna angularis var. angularis.
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; Vigna.
OX   NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT81688.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAT81688.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(2015).
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; AP015036; BAT81688.1; -; Genomic_DNA.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000291084; Chromosome 3.
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:SF398; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF06012; DUF908; 1.
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; 2.
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:UP000291084};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1304..1345
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          3303..3644
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          931..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          996..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1722..1762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2040..2062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2093..2123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2144..2198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2484..2516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2532..2568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2585..2604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2702..2721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2959..2984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1023
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1733..1753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2043..2062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2151..2179
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2484..2499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2586..2603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3611
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   3644 AA;  401512 MW;  BA06825195548F95 CRC64;
     MTTLRSSWPS RLRQLLSNEG AIGPSVKLET EPPPKIKGFI EKIIKCPLQD IAIPLSGFRW
     EYNKGDFHHW RPLLLHFDTY FKTYLSCRND LTLLDNLEDD SPLPKHAILQ ILRVTQIILE
     NCANKSSFDG LEHFKLLLAS TDPEILIAAL ETISALVKIN PSKLHGSTKM ICCGSVNSYL
     LSLAQGWGSK EEGLGLYTCI MANEDAQDEA LSLFPSDITK IGHDQSNYRI GTTLYFELHA
     PSAQSKEQSA EAVSTGTTVI HMPDLHLCKE DDLSLMKQCI EQYSIPSELR FSLLTRIRYA
     RAFRSPRICR LYSRICLLAF IVLVQSGDAQ DELVSFFANE PEYTNELIRI VRSEEVVSGS
     IRTLAMLALG AQLAACTSSH HRARILSGSN LTFAGGNRMI LLNVLQRAIL SLKSSNDPSS
     LAFVEALLQF YLLHVVSTST SANNIRGSGM VPTFLPLLED FDPTHIHLVC FAVKTLQKLM
     DYSSSSVSLF RELGGIELLT QRLQKEVHRV IGLVGEIDSM MLTGESFRHN PDQLHSQKRL
     IKVSLKALGS ATYAPANSTR SQHSHDSSLP TTLSLIFQNV YKFGGDIYYS AVTVMSEIIH
     KDPTCFSALH EMGLPNAFLL SVGSDILPSS KALTCIPNGL GAICLNAKGL EAVRESSSLR
     FLVDIFTSKK YVLAMNEAIV PLANAVEELL RHVSSLRSTG VDIIIEIIHK IASFGDGKII
     GSSGKAESTA METDSKNKEN EGHCCIVGTS SSAVEGIGDE QFIQLCVFHL MVLVQRTIEN
     GETCRLFVEK LGIEALLKLL LRPSIAQSSD GMSIALHSTM VFKGFAQHHS IPLARAFCSS
     LRVHLKKALE GLGATSEPLL LDPRMSSDGG FFSSLFVVEF LLFLATSKDN RWVTALLTEF
     GNGSKDVLED IGLVHREVLW QIALLENRKP EDDEDGIYSS NSQQAEGDAS ESEEQRFNSF
     RQFLDPLLRR RTPGWSIESQ FFNLINLYRD LGRSPGSQHR SISIGPSNMR SSSSNQVQHS
     GSDDTSETAH KKESDKQRPY YTSCCDMVRS LSFHISHLFQ ELGKVMLLPS RRRDDVVNVS
     PASKSVASTF ATIAFDHMNY GGRCVNLSGT EESISTKCRY FGKVIDFMDN ILMERLDSCN
     PILLNCLYGR GVIGIVLTTF EATSQLLFTV NRAPASPMDT DDANAKQDDK EDSDSWIYGS
     LASYGKLMDH LVTSSFILSS FTKHLLAQPL TNGDTPFPRD AETFVKVLQS RVMKTVIPVW
     THPQFVDCSY EFISTVISII KHVYTGIEVK NVNGSGGARI TGPPPNETTI STIIEMGFTR
     SRAEEALRQV GSNSVELAME WLFSHPEETQ EDDELARALA MSLGNSESDS KDAAAKDNTQ
     HLEEEMVQLP PVDELLSTCT KLLSKDPLAF PVRDLLVMIC SQDDGQHRTN VVSFIVERIK
     ECGLVSNNGN YAILAALFHV LALILNEDSL AREAASKSGM IKITSDLLFQ WDSSLDSREK
     QQIPKWVTAA FLALDRLLQV DQKLNSEITE QLKKEPVNNQ QVSITIDEDR QNRLQSACGL
     GMKYTDIHEH KRLVEIACSC MKNQLPSDTM HAVLLLCSNL TRNHSVALTF LDAGGLSLLL
     SLPTSSLFPG FDNVAASIVR HVLEDPQTLQ QAMESEIKHS LVVASNRHPN GRVNPHNFLS
     NLASVVSRDP STFMLAAQSV CQVEMVGERP YIVLLKDKDK DKAKEKDKVQ NSDGKVSLGN
     TTSPAINGKI HDSNTKSAKG HKKPSQSFVN VIELLLESIC TFVPPLKDDI ASNALPGTAA
     STDMEIDVSL AKGKGKGKAV ANMSEDNETG SQDASASLAK TVFILKLLTE ILLMYSSSVH
     VLLRRDAEMS SIRGSYQKSP AGLSMGGIFY HILHNFLPYS RNSKKDKKVD GDWRQKLATR
     ANQFLVAACV RSTEARKRVF NEISYIINEF VDLCHGIRSP GNEVQVFVDL LNDVLAARTP
     AGSSISAEAT TTFIDSGLVK PFTCTLQVLD LDHPDSSEVA TGIIKALELV TKEHVHSVDS
     SKGDISAKPS VLSQPGRTNN IGEISQSMET TSQANPDSLQ VDHVRSYAVR SYGGGSEAVT
     DDMEHDQDLD GSFAPGNEDD YMHENSEDAR DLENGMENVG LQFEIQPRGQ ENLDEDDDDM
     SGDEGEDVDE DEEDDEEHND LEEVHHLPLP DTDQDEHEID DEDFDDEVME EEDEDDEEDE
     DGVILRLEEG INGINVFDHI DVFGRDNSFA NEAFHVMPLE VFGSRRPGRT TSIYSLLGRT
     GDTALPSRHP LLLEPSSFPP LTGQSDSSLE NNSVGLDNIF RSLRSGRQAQ RLHLWTDNYQ
     QSGGTSAVVV PQGLEELLVN QLRRPSAEKS SNQNIAEAGS HAKVGITQAQ DAGGAMPDVP
     VESNPILEVS TITPSVIDNS NNVDARPIGT GPSQANVLST QSQAVEMQFE HNDGNVRDVE
     AVSQESSGSG ATFGESLRSL DVEIGSADGH DDGAERQVSA DRIAGDSQAA RTRRANIPLT
     QFSPVVGRDA SLHSVTEVSE NSSHDADQDG PAAAEQPVNS DAGSGAIDPA FLDALPEELR
     AEVLSAQQGQ AAQPSNVESQ NTGDIDPEFL AALPADIRAE VLAQQQAQRL HQSPELEGQP
     VEMDTVSIIA TFPSDLREEV LLTSPDTILA NLTPALVAEA NMLRERFAHR YSRTMFGMYP
     RSRRGETSRR EGVGSGLDAA GGTISSRRSG GAKVVEADGA PLVDTEALHA MIRLFRVVQP
     LYKGQLQRLL LNLCAHSETR ISLVRILMDL LMLDVKRPVS YFSKVEPPYR LYGCQSNVMY
     SRPQSFDGVP PLLSRRILET LTYLARNHLY VAKILLQFRL PHPAIKEPVD ERGKAVIVGE
     GEENISESNE GYISIAMLLG LLNQPLYLRS IAHLEQLLNL LDVIIDSAGN KSSDKSLIST
     TLPSGPQISA VEADVNADSN ILSPRDDTST DVEGSSKPTS SGHNVECDSH GVLSNLRKVE
     LRLLCSLLAQ EGLSDNAYTL VAEVMRKLVA IAPNHCELFV TELAEAVQKL TSSAMNELHV
     FGEAMKSLLS TTSTDGASIL RVLQALSSLV TLLTGKENDK GIPALSEVWE INSALEPLWH
     ELSCCISKIE FYSESASESL TSSSTFVSKP SGVMSPLPAG SQNILPYIES FFVVCEKLHP
     AQPGASHESS IPVISDVEYA STSAPQKASG TSAKVDEKHA AFVRFSEKHR KLLNSFIRQN
     PGLLEKSFSL MLKVPRFIDF DNKRAHFRSK IKHQHDHHHS PLRISVRRAY VLEDSYNQLR
     MRSTQDLKGR LTVHFQGEEG IDAGGLTREW YQLLSRVIFD KGALLFTTVG NESTFQPNPN
     SVYQTEHLSY FKFVGRVVGK ALFDGQLLDV HFTRSFYKHI LGVKVTYHDI EAIDPGYFKN
     LKWMLENDIS DVLDLTFSID ADEEKLILYE RNEVTDYELI AGGRNIKVTE ENKHQYVDLV
     AEHRLTTAIR PQINSFLEGF NELIPRELIS IFNDKELELL ISGLPDIDLD DLRANTEYSG
     YSAASPVIQW FWEVVQGLSK EDKARLLQFV TGTSKVPLDG FSALQGISGS QKFQIHKAYG
     SPDHLPSAHT CFNQLDLPEY PSKQHLEERL LLAVHEGSEG FGFG
//

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