ID A0A2G8JZI9_STIJA Unreviewed; 303 AA.
AC A0A2G8JZI9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=E3 SUMO-protein ligase NSE2 {ECO:0000256|ARBA:ARBA00020923};
DE AltName: Full=E3 SUMO-protein transferase NSE2 {ECO:0000256|ARBA:ARBA00031731};
DE AltName: Full=Non-structural maintenance of chromosomes element 2 homolog {ECO:0000256|ARBA:ARBA00032533};
GN ORFNames=BSL78_21972 {ECO:0000313|EMBL:PIK41177.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK41177.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK41177.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK41177.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK41177.1};
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 -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NSE2 family.
CC {ECO:0000256|ARBA:ARBA00008212}.
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:PIK41177.1}.
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DR EMBL; MRZV01001043; PIK41177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JZI9; -.
DR STRING; 307972.A0A2G8JZI9; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd16651; SPL-RING_NSE2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330:SF1; E3 SUMO-PROTEIN LIGASE NSE2; 1.
DR PANTHER; PTHR21330; UNCHARACTERIZED; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:PIK41177.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 213..297
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 195..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 34446 MW; 09FEB78C30C72D3F CRC64;
MYVFEILLQA GTSKEASLAY QSRKLTEVSL LDSYLTSMIM NCQQLCNWTA YINLGVTRTR
DLMIRMANSG RAHFEVVNSA VRGLAKVQTY IEQGMSDVIE VSLDLAENGG ENEGSLHNLE
EMMKEYIALD ADLQKFNKAV GVVTQQMRQI DPKAEFNVQS KLRNQLEETE EPLQDPENHD
KMIELKEKLW QLQHPGEGMP TQETVAGSQS SQDEDEPTMT QVEVCTKCPI SQGEMVDPVK
NKTCGHSYER KAVAELMKQR RGMRCPVTGC HNKNPLLQRD LVDNKELKMF IERRNRQTGK
RGN
//