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Database: UniProt
Entry: A0A369J7K9_HYPMA
LinkDB: A0A369J7K9_HYPMA
Original site: A0A369J7K9_HYPMA 
ID   A0A369J7K9_HYPMA        Unreviewed;       347 AA.
AC   A0A369J7K9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   SubName: Full=E3 SUMO-protein ligase nse2 {ECO:0000313|EMBL:RDB17908.1};
GN   Name=nse2 {ECO:0000313|EMBL:RDB17908.1};
GN   ORFNames=Hypma_000885 {ECO:0000313|EMBL:RDB17908.1};
OS   Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX   NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB17908.1, ECO:0000313|Proteomes:UP000076154};
RN   [1] {ECO:0000313|EMBL:RDB17908.1, ECO:0000313|Proteomes:UP000076154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=51987-8 {ECO:0000313|EMBL:RDB17908.1,
RC   ECO:0000313|Proteomes:UP000076154};
RA   Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA   Jeong J., Song E.-S.;
RT   "Whole genome sequencing of Hypsizygus marmoreus.";
RL   Submitted (APR-2018) 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:RDB17908.1}.
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DR   EMBL; LUEZ02000107; RDB17908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369J7K9; -.
DR   STRING; 39966.A0A369J7K9; -.
DR   InParanoid; A0A369J7K9; -.
DR   OrthoDB; 1355659at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000076154; 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:RDB17908.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076154};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          250..331
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  39085 MW;  5DCD66629E3434A3 CRC64;
     MPVSTFSRRK SSRRQMSSDI EEDRPSQSRA DEQVEEADEG PSRRRTNGVK KEKKPNISRR
     QERAPEVNGN RDEDDEDDDD DDEDGRIDIA NFRDQPLAKT DVVKLQGIAR DWNQMEITTR
     QNWRVVGDVA VAIADAAEGE DAEQGLAELD IIMKDLIDIG VEMQAHEKAL DDIAQKVGQG
     EDVDDAIERY GDGVQTRMEE YTKKTTRQKY AKSEEYTSFK HNIYEIQHPE KALPPITDFI
     PKEDGDASDD EDDLEMGGVS QVYTCPITLV ALEKPVTSSV CGHSFSSNAI LQSFQGSPTV
     KCPTSGCTKR FSRSDLKPNK ELEKKVKAWQ RRAQRAAENS DAEEIID
//
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