ID   E4V3Q5_ARTGP            Unreviewed;       887 AA.
AC   E4V3Q5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Cullin family profile domain-containing protein {ECO:0000259|PROSITE:PS50069};
GN   ORFNames=MGYG_07636 {ECO:0000313|EMBL:EFR04629.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
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   -!- 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; DS989828; EFR04629.1; -; Genomic_DNA.
DR   RefSeq; XP_003170392.1; XM_003170344.1.
DR   AlphaFoldDB; E4V3Q5; -.
DR   STRING; 535722.E4V3Q5; -.
DR   GeneID; 10025632; -.
DR   VEuPathDB; FungiDB:MGYG_07636; -.
DR   eggNOG; KOG2167; Eukaryota.
DR   HOGENOM; CLU_004747_7_0_1; -.
DR   InParanoid; E4V3Q5; -.
DR   OMA; NYQEQTW; -.
DR   OrthoDB; 5474206at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
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; 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; 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: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; SSF74788; Cullin repeat-like; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          514..760
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  101434 MW;  4E5D1FAF2D54A874 CRC64;
     MPTPSSGGNR KQMGKRKHKD SSRDESQEEQ EQKQRTIPDL FSRDHHSTNH KQAPPPSQSN
     KRLRRNECDS DRETPPQEVA PITVDKMYKF TSSDGKGSNG SAFGFARADN RTPLARTRQF
     NSSNPSSFTP HTGAKTLKVK NLRDTPKLDQ QLYFDKVWSQ LDSALTAIFN HEKLPFSLEE
     LYRGVEHVCR QGRATNLAKN LKDRCMEHIS GTVMESLLAK STSGDEAGVL RAVEAAWTQW
     NARLMTVRSI FYYLDQSFLL HSPNNPVISE MGLLQFRSSV FSDETLKSKI LQGACLLIEL
     DRLEDTYADP TLLRSSIKLF HDLKIYSSQF EPSMLESSAT YYKNWAATHV TEDDLASYVE
     KSYRLIEREM ARCDLLSFDR GTKQRLAELL DHNLMANQKL FLLQEADIIG LLRANNATAL
     ERLFSMLERK GMGVDVKSGF SKYIVDEGSA IVFDEARESE MVTRLLAFKQ SLDHIWKFSF
     HTHEQLGHTL RESFETFINQ HKKTDSNWGT DNPKPGEMIA KHVDLLLKGG VRALQNRPVE
     DITGNSSLTD EDAEINKQLD QVLDLFRFVH GKAVFEAFYK NDLARRLLMG RSASDDAEKS
     MLSRLKSECG SNFTHNLETM FKDMDLARDE MASYNALLRE KDERPKIDLN VNVISATAWP
     SYPDVPVNIP ASISEAITNF EKFYNNKYSG RRLHWKHTLA HCQLKARFPL GDKELVVSSF
     QAIVLLLFND AGSETLSYEV IKKASRLSDV ELKRTLQSLA CAKYRVLLKK PKGKEVNNGD
     VFAYNAKFED QKMRIKINQI QLKETKQENK TTHERVAQDR HLETQAAIVR IMKSRKVITH
     SDLVAEVIKA TKNRGQLEID GIKKNIDKLI EKDYIEREED NRYKYIA
//