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Database: UniProt
Entry: R4XGI6_TAPDE
LinkDB: R4XGI6_TAPDE
Original site: R4XGI6_TAPDE 
ID   R4XGI6_TAPDE            Unreviewed;       281 AA.
AC   R4XGI6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   03-MAY-2023, entry version 29.
DE   SubName: Full=E3 SUMO-protein ligase nse2 {ECO:0000313|EMBL:CCG83611.1};
GN   ORFNames=TAPDE_003930 {ECO:0000313|EMBL:CCG83611.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG83611.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG83611.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
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:CCG83611.1}.
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DR   EMBL; CAHR02000162; CCG83611.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4XGI6; -.
DR   STRING; 1097556.R4XGI6; -.
DR   VEuPathDB; FungiDB:TAPDE_003930; -.
DR   eggNOG; KOG2979; Eukaryota.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000013776; 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:CCG83611.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013776};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          174..262
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          256..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31125 MW;  5F9E01BCC9AEAD10 CRC64;
     MPSVMPAPTQ SQLVLPARIK RSALHRLATS RNPLEDHCAT CLETLAFVGE CEATWNGSGS
     RVEEVEEAVK EVIEVREDGV RVKDSVAALM ADHNDGDDDD DDGVAVGDAA TAVLERIEVG
     KGEYRDKSAV ERYGAVPAYD AFKRRVFDVQ FPESPYPGTA SFLLPRRARR TTGDDDDGEP
     EMTYRAKRNL KCPITMMTLH HPMRSTVCVH VYSRDALAEM LARNRGTIHC PVAGCDKTLT
     ADTVERDRVM ERRVRVQEDE EAREGEELSS DVDGSAVLDV F
//
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