ID A0A151P2C7_ALLMI Unreviewed; 1608 AA.
AC A0A151P2C7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, 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=HECW2 {ECO:0000313|EMBL:KYO43173.1};
GN ORFNames=Y1Q_0017501 {ECO:0000313|EMBL:KYO43173.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO43173.1};
RN [1] {ECO:0000313|EMBL:KYO43173.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO43173.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO43173.1}.
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DR EMBL; AKHW03001210; KYO43173.1; -; Genomic_DNA.
DR RefSeq; XP_019338923.1; XM_019483378.1.
DR STRING; 8496.A0A151P2C7; -.
DR GeneID; 102574757; -.
DR CTD; 23072; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 2.60.40.150; C2 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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 183..319
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 834..867
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1020..1053
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1273..1608
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 350..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1576
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1608 AA; 181889 MW; BA3264CED348E18C CRC64;
MLLHLCSVKN LYQNRFLGLA AMASPSRNSQ NRRRCKEPLR YSYNPDQFHN MDIRNSSHET
VTIPRSTSDT DLVTSDSRST LMVSSSYYSI GHSQDLVIYW DIKEEVDAGD WIGMYLIDEV
LSENFLDYKN RGVNGSHRGQ IIWKIDASSY FVEPETKICF KYYHGVSGAL RATTPSVTVK
NSSAPQIFKS ITHEDSIQGQ GSRRLISFSL SDFQAFGLKK GMFFNPDPYL KISIQPGKHS
IFPALPHHGQ EKRSKITCNT VNPIWQGEQF SFVSLPTDVL EIEVKDKFAK SRPIIKRFLG
KLSMPVQRLL ERHAIGDRVV SYTLGRRLPT DHVSGQLQFR FEITSSIHPD DEEVSISADP
EPADVQESPM NNTPEESLGE PPCTSTVTSE SAAPEQLNGC NVNSVNVDSL GAVRSPWEVN
HDSLNEELTG NGEVDAMPAD ATEPLESIPG EVLPSLSAMD LTEQLALMAC TSPPETEVRE
NNEINSVTQG DDEILEALDI EEVSADVQAV KDVEKSQDEE GAAAQEEEDN KLQLRTTMKR
KNRPCSLPVS ELETVIASAC GEPETPRTHY IRIHNLLHSL PSAQMSSDGE EEQGGRGEND
EESTVKDVSE KDVVSETETV AADPPPENEA EENFSRGTMP RSTSVEHLSD LNGQLLDGEH
IRTESESELS PRPNGDHECD TCDTSCYSPS CYSTSCYSTS CYSTSCYSTS CYDSNNRFSS
HTRFSSVDSA KISESTVFSS QDDEEEENSA FESVPDSVQS PELEREQVDG SAQWPDELLA
HGGNPQRGTE NLDTPVAGPS SRREGDCPLL HNSQPVSQLP SLRPDHHHYP TIDEPLPPNW
EARIDSHGRV FYVDHVNRTT TWQRPTAAAT PDGIHRSGSV QQMEQLNRRY QNIQRTIATE
RTEDDAVTNN RVERLPTGGG SDSEAEPSQP SSEIRREGSL SPVNSQKITL LLQSPAVKFI
TNPEFFTVLH ANYSAYRVFT NSTCLKHMIL KIRRDARNFE RYQHNRDLVN FINMFADTRL
ELPRGWEIKT DQQGKSFFVD HNSRATTFID PRIPLQNGRL PNHLTHRQHL QRLRSYSAGE
ASEVSRNRGV SLLTRPGNSL VTAIRNQHHH EALPLAYNDK IVAFLRQPNI FEMLQERQPS
LARNHALREK IHYIRTEGAH GLEKLSCDAD LVILLSLFEE DIMSYIPLQA AFHPGYSFSP
RCSPCSSPQN SPGLQRASAR APSPYRRDFE AKLRNFYRKL EAKGFGQGPG KIKLIIRRDH
LLEGTFNQVM AYSRKELQRN KLYVTFVGEE GLDYSGPSRE FFFLLSQELF NPYYGLFEYS
ANDTYTVQIS PMSAFVENHL EWFRFSGRIL GLALIHQYLL DAFFTRPFYK ALLRLPCDLS
DLEYLDEEFH QSLQWMKDNI ITDILDLTFT VNEEVFGQVT ERELKSGGAN TPVTEKNKKE
YIERMVKWRV ERGVVQQTEA LVRGFYEVVD SRLVSVFDAR ELELVIAGTA EIDLNDWRNN
TEYRGGYHDG HIVIRWFWAA VERFNNEQRL RLLQFVTGTS SVPYEGFAAL RGSNGLRRFC
IEKWGKITSL PRAHTCFNRL DLPPYPSYSM LYEKLLTAVE ETSTFGLE
//
