ID A0A165GST4_9BASI Unreviewed; 422 AA.
AC A0A165GST4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cullin family profile domain-containing protein {ECO:0000259|PROSITE:PS50069};
GN ORFNames=CALCODRAFT_432704 {ECO:0000313|EMBL:KZT58431.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58431.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT58431.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58431.1,
RC ECO:0000313|Proteomes:UP000076842};
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 -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330, ECO:0000256|RuleBase:RU003829}.
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DR EMBL; KV423951; KZT58431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GST4; -.
DR STRING; 1353952.A0A165GST4; -.
DR InParanoid; A0A165GST4; -.
DR OrthoDB; 5474206at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; CULLIN; 1.
DR PANTHER; PTHR11932:SF126; CULLIN 4, ISOFORM A; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 51..293
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
SQ SEQUENCE 422 AA; 48594 MW; 3BF79E4F7E361250 CRC64;
MIPDLLALRK FAELIARDAF GEDPDDPAGE RVWRNSVLDA FEKGFAGRVK KPAEMIAKYI
DQAMRKGQRS ASDDEFNRLL NEALGLYRFT KDRDVFREFY IRALAKRLLL QKSASDDFEM
NVLKILIERE SLLCIYLHPS GIDRATDDKF FEKGHGMFSD LALSRDMIRE WQNLPSHRDD
KEPLNVMVLQ HSNWPTYGLG QVILPKDMER SLSSFVRFYK SKHAQRKLDW AHSLGTVTLT
ARFDAGTKEL SVSLYQAVVL LLFEDGGSMN FQDIKEATGI EDKELRRTLQ SLALGRKRVL
TKVPLSKDVD DTDVFEYNAK FTDKNRRLHI NSIQQAETAE EAKQIAEHIE EDRTHALDAA
IVRIMKARKR LGNNKLTEEV IIAVRAHFVP QPAQIKKQIE SLIEREYITR SDGDRNTFEY
VA
//