ID A0A165QTG7_EXIGL Unreviewed; 176 AA.
AC A0A165QTG7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=EXIGLDRAFT_716064 {ECO:0000313|EMBL:KZW04051.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW04051.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW04051.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW04051.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV425882; KZW04051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QTG7; -.
DR STRING; 1314781.A0A165QTG7; -.
DR InParanoid; A0A165QTG7; -.
DR OrthoDB; 2785713at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0000795; C:synaptonemal complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042448; CCNB1IP1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14305; E3 UBIQUITIN-PROTEIN LIGASE CCNB1IP1; 1.
DR PANTHER; PTHR14305:SF0; E3 UBIQUITIN-PROTEIN LIGASE CCNB1IP1; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..48
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 107..159
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 176 AA; 19865 MW; 2B912C23168CAD1E CRC64;
MDTDLRCNRL ACRQTLVDRA VVTTCSHIFC ADCANEHFTE AQICPACETH LPEPDDCVIA
SLHPTNDYKT SVLSGLNPAT ILDICGRAVA FWSYQVQQEQ SFQQAMLKKA SETSSTMQKQ
LDNVIREANT ELTLMNNKLS TAEQELELER RKVRELQDAS LSKDKEYAKL KVRNPP
//
