ID   F2PUE9_TRIEC            Unreviewed;       819 AA.
AC   F2PUE9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=SCF ubiquitin ligase subunit CulC {ECO:0000313|EMBL:EGE05517.1};
GN   ORFNames=TEQG_04526 {ECO:0000313|EMBL:EGE05517.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC       {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC       ECO:0000256|RuleBase:RU003829}.
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DR   EMBL; DS995740; EGE05517.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PUE9; -.
DR   VEuPathDB; FungiDB:TEQG_04526; -.
DR   eggNOG; KOG2166; Eukaryota.
DR   HOGENOM; CLU_004747_7_1_1; -.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 4.
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; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11932; CULLIN; 1.
DR   PANTHER; PTHR11932:SF168; CULLIN-3; 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; SSF74788; Cullin repeat-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EGE05517.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          441..684
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          361..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  93693 MW;  06F13273CF07A1C4 CRC64;
     MKPRAKVRVP RRGMTGRSEN DDFSSIWNIL ASSIREIHTK NSSQLSFEEL YRNAYKLVLR
     KQAMDLYEKV AELEKDWLYN DVRKQVASLI TPALLTITDS ADATEHANER KAAGERLLAK
     LKEVWEDHQL CMGMITDVLM YMDRVVMQEL RNQSIYDTSM GLFRDCVLRA DIGGEENGTI
     GSVFENTLLF MILLEREGVI IDRALIKHCV YLLEGLYEDG IEDSTGKLYH TTFEPAYIEA
     SRRYYAAEGQ RLLTTTDAAT FCKRVTARIR EEQSLCQQTL SPVTEAKVME VIDDRLIRHY
     IGEVIRMDDS GVKYMIQNDR LEDLKNVFEL IARIDAKKVA LTKVVQQTVI EYGTAVNTAA
     KELSQNPPVP SATDQGKKSS APDEKQPVAN LQTAAAIKWV DDVLKLKAKF DRIWEEAFIK
     DQALQTSLTL SFSDFINVNP RGTEYLSLFF DENLRKGIKG KTEEEVDALI DNGITLLRYI
     RDKDLFETYY KKHLSRRLLM KRSASMDAER QMITKMKMEV GNTFTQRLES MFKDMAVSAD
     LTSSYRDYIA NNSKIELEMS VLTSTMWPVE IMSSHNRDGQ VQLPCIFPKN VESLKQSFER
     FYLDKHSGRK LSWLPGMGTA DIRATFTRPN GKVERHDLNV STYAMVILLL FNDLPSGESL
     TFEEIQEKTR IPTNELIRNL QSLAVAPKTR ILRKEPMSKG VQPSDKFSFN EQFTSKFTRL
     KIGVVSASGN KVENKEERTD TEKKTSEERG NTIEAAIVRI MKQRKTLAHS QLITEAISQL
     AARFTPDVNM VKKRIESLID REYLERITDS DPPAYSYVA
//