ID A0A3B3QN31_9TELE Unreviewed; 959 AA.
AC A0A3B3QN31;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000008117.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000008117.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3B3QN31; -.
DR STRING; 1676925.ENSPKIP00000008117; -.
DR Ensembl; ENSPKIT00000032190.1; ENSPKIP00000008117.1; ENSPKIG00000023753.1.
DR GeneTree; ENSGT00940000154635; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd04021; C2_E3_ubiquitin_ligase; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF299; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
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; 4.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..117
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 337..370
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 369..402
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 444..477
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 484..517
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 575..959
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 150..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 927
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 959 AA; 106762 MW; 27714A1B2E71B8A5 CRC64;
MASAPLTSDC SNNHAETLQL HATVSCARLK RKKNWFVGTA IYVELEASGE IWRTAKSHSS
SSPKWEERLT VNVTSSSQLD FRVWSHHALK ADSLLGKAGL DVRRVLEQHG RKVENVKEVL
KLTLESKGGQ STVGELTVIL DAPAVGREIL PNRTNSAPKV QQNGGAVRDN GDDTPARSQS
GSQGSGSGSG SGSASGSASG SDSIDGPGAS ASPVINGDAA SSSPTPRAAE AQQDPSPGPT
DGQVTNGVVN GETVNSAVEE MLPPAGSSGD GVGGAPSDSG SALAASALTV SDGPSGNPAS
SSSPSSSSVT ASAAGNKAGG KSASEAKPNH GNTGNADHLP AGWEQRKDVH GRTYYVDHNT
RTTTWERPQP LPSGWERRVD DRGRIYYVDH NTRTTTWQRP TMESVRNFEQ WQSQRSQLQG
AMHQFNQRYL YSASMMSAEN DPLGPLPPGW ERRVDSNDRV YFVNHNTKTT QWEDPRTQGL
QNEDPLPEGW EIRYTREGVR YFVDHNTRTT TFNDPRTGKS SVTKGPQIAY ERSFRWKLAH
FRYLCQSNAL PSHVKITVSR QTLFEDSFQQ IMALKPYDLR RRLYVIFRGE EGLDYGGLAR
EWFFLLSHEV LNPMYCLFEY AGKSNYCLQI NPASAINPDH LSYFCFIGRF IAMALFHGKF
IDTGFSLPFY KRMLSKKLTI KDLESIDPEF YNSLIWIRYC PTRCLARGFF QALPCSPCPA
APALQPLPCS PCPAAPPHLH AANHPFLRDN NIEECDLEMY FSVDMEILGK ITSHDLKPDG
ASLLVTEENK EEYIGLMAEW RFSRGVADQT KAFLDGFNEV VPLQWLQYFD EKELEVMLCG
MQEVDLQDWQ RHTVYRHYTR NSKQIMWFWQ FVKEVDNEVR LRLLQFVTGT CRLPLGGFSE
LMGSNGPQKF CIEKVGKETW LPRSHTCFNR LDLPPYKSFE QLKEKLLFAI DETEGFGQE
//
