ID A0A1E3HZP5_9TREE Unreviewed; 327 AA.
AC A0A1E3HZP5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=SP-RING-type domain-containing protein {ECO:0000259|PROSITE:PS51044};
GN ORFNames=L202_02112 {ECO:0000313|EMBL:ODN81718.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN81718.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN81718.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN81718.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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:ODN81718.1}.
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DR EMBL; AWGJ01000003; ODN81718.1; -; Genomic_DNA.
DR RefSeq; XP_018996037.1; XM_019135634.1.
DR AlphaFoldDB; A0A1E3HZP5; -.
DR STRING; 1295533.A0A1E3HZP5; -.
DR GeneID; 30153421; -.
DR OrthoDB; 1355659at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000094065; 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: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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 219..304
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 36279 MW; 37D0A3EF867F7F0C CRC64;
MPPTYASTNI NTIRNANGHG SYSAGPSNGA HEDIDMEDDE APVGDLSDDE EGEEEDEAGW
TEEMFTDKPI ARAGASVVRG LSDAMRDAIK RLDDVIDSIK ETAYILEEAV PDDPALKNVE
ASLFKAFDQR AVLKIKANAL DELSKSLLEG REHTNIQADF ENLSEPRIQE YMGKSQHAKF
KKDREYADFK SELWSRSHET ACPPISTFLT KGPNDEDDSD DDIDMGGQTQ NYRCPITLTL
YQDAVTSVKC NHTYSKEAII NLITNSQKNR SVARCPVTGC SIAISKADLK DNPAIQKRAN
DFSRRQQEKE DDRDDDAASV EDDSDGE
//