ID A0A0V1HZW2_9BILA Unreviewed; 828 AA.
AC A0A0V1HZW2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN Name=Nedd4 {ECO:0000313|EMBL:KRZ15570.1};
GN ORFNames=T11_13882 {ECO:0000313|EMBL:KRZ15570.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ15570.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ15570.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ15570.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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:KRZ15570.1}.
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DR EMBL; JYDP01000017; KRZ15570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HZW2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
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; cd04033; C2_NEDD4_NEDD4L; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
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:SF443; E3 UBIQUITIN-PROTEIN LIGASE NEDD-4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
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; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 8..129
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 202..235
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 327..360
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 382..415
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 489..827
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 160..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ15570.1"
SQ SEQUENCE 828 AA; 95652 MW; 7C8D93F2EBD62FBE CRC64;
LLTHCIEVMS ETRIYGLPES AQGRTKILRI LVVRGIDLAK KDIFGASDPY VSVHLCQQGR
EVDKVHTKTI KKTLYPIWNE EFLFRVDPTN CKIVFEVFDE NRITRDDFLG IVEIDLQTVR
IPKERTGRDI REKNCLLRPR SLKSRVRGEL RLALSYLSDP NSEDELDTAE TETDSDSGDW
EMLPASSRSG LLAESPTAQQ IPPLPSGWEE RIDANGRTFY VNHTNRTTQW ERPSNSNLHV
ASRPDDLWLK QRSCFQQRWD ENKLENRGIP SSSGASTSTA STSRATSSST VQDELSQNRH
VHSAPSLETD SDWQEIGLLS EEDDGDGPLP LNWQVQVAPN GRKFFIDHNT KTTTWIDPRT
GKPTKLPERK TYRPKHQCDE LGPLPSGWEE RVHVDGRVFF IDHNTKTTQW EDPRFYNPQI
AGPAVPYSRD YKRKYEYFRA HLIKPENVPN KFDMHIRRDH THFEQSCQLQ QAEPTYSKRN
SGSNSTERQT GLDYGGVARE WFFLLSHEMF NPYYGLFEYS AMDNYTLQIN PNSGLCNDDH
LSYFRFVGRV MGIALHHGKL LDGKLTIRPF KTVQQYDLIF TAAFFIRPFY KMMLGKPICL
NDMESVDSEY YNSLLWIEDN DPSELELRFV VDEEVFGVTQ TRELKPGGAD ILVTNDNKNE
YINLVIKWRF VSRVTDQMNA LMSGLNEFIM QSLLTIFDPH ELELLMCGLQ KIDVKDWKDN
TLYKGGYNAN HPVIQNFWKC VLSFDNEMRS RLLQFVTGTS RVPMNGFREL YGSNGLQKFT
IEKWSTPEML PRAHTFNRLD LPPYTSYQDL KDKLVKAIEN SASFEGVD
//
