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Database: UniProt
Entry: A0A1S8BM54_9PEZI
LinkDB: A0A1S8BM54_9PEZI
Original site: A0A1S8BM54_9PEZI 
ID   A0A1S8BM54_9PEZI        Unreviewed;       447 AA.
AC   A0A1S8BM54;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   03-MAY-2023, entry version 20.
DE   SubName: Full=E3 SUMO-protein ligase nse2 {ECO:0000313|EMBL:OMP88539.1};
GN   ORFNames=BK809_0005258 {ECO:0000313|EMBL:OMP88539.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP88539.1, ECO:0000313|Proteomes:UP000190776};
RN   [1] {ECO:0000313|EMBL:OMP88539.1, ECO:0000313|Proteomes:UP000190776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F98.1 {ECO:0000313|EMBL:OMP88539.1,
RC   ECO:0000313|Proteomes:UP000190776};
RA   Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA   Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT   "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT   in grapevine trunk diseases.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMP88539.1}.
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DR   EMBL; MSZU01000074; OMP88539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8BM54; -.
DR   STRING; 420778.A0A1S8BM54; -.
DR   OrthoDB; 2726194at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000190776; 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:OMP88539.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190776};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          262..359
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  49768 MW;  CB675B799185F754 CRC64;
     MSARARQSTA DPSASAIKDL PPYEPPENPL NAQSQRALAS ILRDHKHQKL EQHLRQAAQA
     LNDNANAINY RLTDRKARHV KRTQKYPDSL TDVDRQRAQH LEQFDVRVTA MTKRMEEAVR
     KTIDGQHFAG ALEEELSHVE NRAVANASAS QRMTQTQRRG DGDDDDMTDF DPTLPGETQQ
     QVQTLVPKDL FEERYQAQKD KYQSLSLPNR YSEHADYVGF KRAVHDGAYP HGEGPPLARP
     EAWFTSAGAP APGVTQVRDN DSDDDIAVAY ERISTKCPLS LLEFQDPVTS TKCPHTFERA
     NIAGLLQESN AFTGGSNRRG ARDGLRTIQC PQPGCDKMLT EDDLRPDPSL IRKIRRIQKA
     RQEGEDDDNV DNSQVQMIHS DNVDGYADID EPASQRVVPK IERVSGVSRD QGVGSSRSSG
     VGYDGTMEST MESTIVDLGS ESESDEE
//
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