ID U1HQT8_ENDPU Unreviewed; 461 AA.
AC U1HQT8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=SP-RING-type domain-containing protein {ECO:0000259|Pfam:PF11789};
GN ORFNames=EPUS_04250 {ECO:0000313|EMBL:ERF72815.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF72815.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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}.
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DR EMBL; KE721034; ERF72815.1; -; Genomic_DNA.
DR RefSeq; XP_007801537.1; XM_007803346.1.
DR AlphaFoldDB; U1HQT8; -.
DR GeneID; 19239281; -.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_028753_1_0_1; -.
DR OMA; TWFSHLE; -.
DR OrthoDB; 2726194at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000019373; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 265..349
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|Pfam:PF11789"
FT REGION 133..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 51237 MW; CC98E32F35A9E2AF CRC64;
MPALPLVPQQ PPVAPLNAEA QKALADLQRQ QKITKRLNHH LAQAADQLAN VAVQLNDRGT
NYTLEYGRKR RRAEANGEEE DGQEKMVYED FRKKVEDLTR MMDNGVRSVV DDQTWVDTLP
EIMKRIARKA EAAAATAQQE TQNIDGEDDE DNEATAYPAA PAPEDAPSTL IKRAAEDVAT
KWCSKTLTER YSQHNTYVGF YRGVYDAKNP GEDGPPIPHH SLWFANEEDI NGSYIAPGTQ
PQTQRTRRQH RGASSNEEDP GHSSDIEIAR EKISIKCPIT FLPFTDPLSS TKCPHSFDRP
GVMDMLQRTQ TFLPLTEAQA AEVARAPNNA ARSRKTAEFR IKTIPCPVCS IMLAEADLKP
DPLLLRKVKR IQAAEAREME ARTSEADSNS DDSDEDEDDD EIVAPGTQRK RVGPGSSPPR
TGAKEGKRKS ALEIKMESAR SKSRGVSVVP QTQLDEDMED D
//
