ID A0A3Q3AZN7_KRYMA Unreviewed; 960 AA.
AC A0A3Q3AZN7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=WWP1 {ECO:0000313|Ensembl:ENSKMAP00000017079.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000017079.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000017079.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_017292391.1; XM_017436902.1.
DR RefSeq; XP_017292393.1; XM_017436904.1.
DR RefSeq; XP_017292394.1; XM_017436905.1.
DR RefSeq; XP_017292395.1; XM_017436906.1.
DR AlphaFoldDB; A0A3Q3AZN7; -.
DR STRING; 37003.ENSKMAP00000017079; -.
DR Ensembl; ENSKMAT00000017316.1; ENSKMAP00000017079.1; ENSKMAG00000012712.1.
DR GeneID; 108248254; -.
DR KEGG; kmr:108248254; -.
DR GeneTree; ENSGT00940000154635; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000264800; 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 Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..114
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 388..421
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 420..453
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 495..528
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 535..568
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 626..960
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 169..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 928
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 960 AA; 107578 MW; 4916F47410F01A37 CRC64;
MATASLRAET SHNHTRTSQL HAIVSCAKLK RKKSVFGAAV YVEVTAEGES RRTAKSHSSS
SPKWDERLTL SVTPHTQVDF KVWSHHTLKA DGLLGKTTLD LSQALERHDR KLENVKEVLK
LDVEQKGVLV PVGELTVYLD GLAVTDQEEL APLTNGNAAN VTKVQQNGDA LHENGDSSSS
SSRAANSTVN GTDSGQRSGS CSASSGADGQ VASSSCSPAL DHAINGNATP NSTPVHQPSD
SDTESRMVNK ESSEAALRQT SATREEVLPP AEDHEDCAQS AAPPDAETAP TSTPQYLPTS
TPSPAVSVTA KPANGTAAAS TTFASPSPGT TTVTTSSPSS SSSPALGEMS TAGAVGNSSS
SSSSSSSAAV TTDGVKPRQQ VPNAAASDPL PPGWEQRKDP HGRTYYVDHN TRTTTWERPQ
PLPPGWERRV DDRGRIYYVD HNTRTTTWQR PTMESVRNFE QWQSQRSQLQ GAMHQFNQRY
LYSASMMSAE NDPLGPLPPG WERRVDSNDR VYFVNHNTKT TQWEDPRTQG LQNEDPLPEG
WEIRYTREGV RYFVDHNTRT TTFSDPRTGK SSVTKGPQIA YERSFRWKLA HFRYLCQSNA
LPSHVKITVS RQTLFEDSFQ QIMALKPYDL RRRLYVIFRG EEGLDYGGLA REWFFLLSHE
VLNPMYCLFE YAGKSNYCLQ INPASAINPD HLSYFCFIGR FIAMALFHGK FIDTGFSLPF
YKRMLNKKLI LKDLESIDPE FYNSLIWIRD NNIEECGLEM FFSVDMEILG KITSHDLKPD
GTNILVTEES KEEYISLMAE WRFSRGVEGQ TKAFLDGFNE VVPLQWLQYF DEKELEVMLC
GMQEVDLQDW QRNTVYRHYT RNSKQIIWFW QLVKEVDNEV RLRLMQFVTG TCRLPLGGFA
ELMGSNGPQK FCIEKVGKDT WLPRSHTCFN RLDLPPYKSY EQLKEKLLFA IEETEGFGQE
//
