ID G1XTB2_ARTOA Unreviewed; 411 AA.
AC G1XTB2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGX43305.1};
GN ORFNames=AOL_s00215g41 {ECO:0000313|EMBL:EGX43305.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX43305.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX43305.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX43305.1}.
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DR EMBL; ADOT01000316; EGX43305.1; -; Genomic_DNA.
DR RefSeq; XP_011127545.1; XM_011129243.1.
DR AlphaFoldDB; G1XTB2; -.
DR STRING; 756982.G1XTB2; -.
DR GeneID; 22898835; -.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_679747_0_0_1; -.
DR InParanoid; G1XTB2; -.
DR OMA; WIKDATE; -.
DR OrthoDB; 2726194at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008784; 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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein 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 GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
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; IPR003613; Ubox_domain.
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 SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; 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:UP000008784};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 230..314
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT DOMAIN 238..325
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 322..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46774 MW; 47ECC00BCCB415C7 CRC64;
MPPHRRQDAP RRVKRAPLPD HISCVLPIHQ SCSGDLRALH ARLPPQSLHR WIKDATEALR
DSSSKFAESR RQRVFEQNLE RDEETEQKIA ELGVRVERNI RGLVDVDEQL KMMKTVLQDI
SEAEKNRGNN DGVQPVEEFL NQMKRGGRAY RRRDLKDRYG NSAEYIELRS LVHGLAKPTA
PQPQKKDWFK TPMFVCDGEA QISDEEPVSE SEGEDVEQDI EMANEDDDDS DDGIQAVAVT
RNLKCPLTMQ LFKDPVKASC GHVFEKEALV EVLRNYKQLK KENTCPTPGC GKLINVKDLK
PDALTKRLAE AKARERDLAE QRAVIAGAGN DESEDEEVVV SHSKKKRKPK PVIKEEEIPY
GEGSGDEEER VPDSHDEQNE DDEEEGENRV SDSNDEAEEE DDEEDDEMES E
//
