ID A0A2G8KZK6_STIJA Unreviewed; 386 AA.
AC A0A2G8KZK6;
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=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BSL78_09657 {ECO:0000313|EMBL:PIK53427.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK53427.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK53427.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK53427.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK53427.1};
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004374}.
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:PIK53427.1}.
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DR EMBL; MRZV01000287; PIK53427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KZK6; -.
DR STRING; 307972.A0A2G8KZK6; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022170; MUL1-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12183:SF32; MITOCHONDRIAL E3 UBIQUITIN PROTEIN LIGASE 1; 1.
DR PANTHER; PTHR12183; MITOCHONDRIAL UBIQUITIN LIGASE ACTIVATOR OF NFKB 1; 1.
DR Pfam; PF12483; GIDE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:PIK53427.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 50..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 337..374
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 386 AA; 43452 MW; 1D60F52B0A188CE6 CRC64;
MYMYSSLRQE YSQHRFKLTL STGGQQVCIA QCCDQLHIQR GKNQVTRMDL LLVAGSATVT
GVFTYLWLKK SKTLAAIEDA PILDLNNELY KVIGDSPDKA IPYAVIQGYV AANNRPIVSQ
YVADAFGVIQ TLICKEHKTE WSTSTRLWYD KTRSITDHTK TVPFAITSDS TLVHVEDPLQ
ASCLELELIY DKFEPTESSV SENILSWASG EKTKGFQRVE LMLPEGVCLT GIGELSLKDD
RVLIRPPHSG AEYILTTASP SAIIRDFQSK IRRWKILAII FGSVTIIFII WGLRKWYKRH
RQTAAYDDYL QRVVESRASE GTDVDDGSVV RREMDPCVVC LTRNRDCVLL DCGHVCGCSS
CIAAIQPPHC PICRQRIVRV VPLFHA
//
