ID A0A2G8JN16_STIJA Unreviewed; 534 AA.
AC A0A2G8JN16;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=BSL78_26041 {ECO:0000313|EMBL:PIK37127.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK37127.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK37127.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK37127.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK37127.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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 -!- 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:PIK37127.1}.
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DR EMBL; MRZV01001554; PIK37127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JN16; -.
DR STRING; 307972.A0A2G8JN16; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Signal {ECO:0000256|SAM:SignalP};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..534
FT /note="HECT-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013573864"
FT DOMAIN 201..534
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 76..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 501
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 534 AA; 60514 MW; 9D5501F054624030 CRC64;
MVQLCGFQGL SLWFFASASF GLFRSSVYTG PKVRNRVPES RYPSGIRTED VSVVDDTLQE
CFICHVEIPE TKLKQHRESC NGKRDDSALP GPSTPVISAP QRLPTSGPVD RYVADYIDLL
EPDDSSDDEL QHVIEDSLKD IDNNRDDTIL EARMQEKLGQ YHLLREEEKF HVVVRRRKIL
KCAADAINSQ AGFSFFKDPV ICFSGEEAVD LGGPRREFFT LATQQLSHLG IFEGKTGKLY
FTHDIVVLEK GLYRLAGQII AWSILHGGPG FPTLHPWLYS MMCDNKPSEE FSTEDVTDSD
VMGHLQKIEN CSSEALLEDT ITMVGDWAAN NGCPAIYSMS MANKEDILQT LFKQHIYYRC
KSEIDDFKRG LDSVGKLWSM IHEDPAPFRC LLVMCDHPLT FSSVKKLFHI RWSENCAHRD
KEEETIYCWE EFLRKAWTGD CSQDIELDDG TTDNIKIELH HILRFCTGAD GIPPTGFHKQ
IDMEFFSVRD GTKPLPIAST CGLELHLPRG VEDTKFFADM MMEAILCSPG FGKM
//