ID   A0A1D2VIX3_9ASCO        Unreviewed;       963 AA.
AC   A0A1D2VIX3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Cullin-domain-containing protein {ECO:0000313|EMBL:ODV61569.1};
GN   ORFNames=ASCRUDRAFT_91011 {ECO:0000313|EMBL:ODV61569.1};
OS   Ascoidea rubescens DSM 1968.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Ascoideaceae; Ascoidea.
OX   NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV61569.1, ECO:0000313|Proteomes:UP000095038};
RN   [1] {ECO:0000313|Proteomes:UP000095038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV454479; ODV61569.1; -; Genomic_DNA.
DR   RefSeq; XP_020047876.1; XM_020195067.1.
DR   AlphaFoldDB; A0A1D2VIX3; -.
DR   STRING; 1344418.A0A1D2VIX3; -.
DR   GeneID; 30968703; -.
DR   InParanoid; A0A1D2VIX3; -.
DR   OrthoDB; 5474206at2759; -.
DR   Proteomes; UP000095038; 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; 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: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; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000095038};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          519..799
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  112142 MW;  95851C5207B01337 CRC64;
     MCASMHVNKS QRTSTHTTQN SIRHGLRAKI RPPRISSLNQ ANLSDSWNDL SIAITEIQNK
     NASNLSFGEL YTKAYNMVLR KHGEKLYNNV KNQIKNYLLN VYKDIVKSFD YQPIVIYPLF
     ESSIKTGGDN IDTEADFNDS NDPNDTLINI STDEPIVLKE NIDRNIRFLE KIVTIWEDHI
     FSMKMISDVL MYLDRVYAKE NSLPSVYDFG ISLFNDFVIT YNNNKIGEML NQIVIDQFYL
     TRKNLTTNSE NNLIKSAMKM FESLQEDYLT RNKLRNSRLK AKEGSTTAVN YYLRYFEPFF
     LKKSSDYYEV FAKKLLSFHD GSIYIESISS LINEEENRFL LIVPDETYPK LVQLMDNILI
     NNNFNQILDF EGNSLNYWLY NLDFKKLKLT YKLAKRIDSE FKLLREKLRN YIFLNGQKLE
     VKVKLFIQNI NNNNNNNNNN NNGDNKNNNS HNNNKSNRLN VKKRTLKETQ TLFANEWIKL
     ILKFREKLKT SLKTCFENNN NFSATIENAF SEFINLNPKV SECLAIYMDD YIKKSLKQST
     SISSKVSNNI SNGINNSAIA NGNTAISTIN SSSNNKLGSM NDDIKTWIEG SVILLKFIND
     KDLFEKYYKN YLGKRLLTSR NSFNSVVGNI DNNIESFAII KIKEETGTSF TSKLEGMFRD
     IKKSKELNDE FNSNIGKDSL ELEVNILTST FWPQTNSREI DSKIIYPEFL KSKQEEYNEF
     YYKKYSGRFL NFTSNFGTMD IRIQFNKKRH EIIIPIYGGL ILLLWSDLDQ RNLKFTMKEI
     EEKTMIPRND LIRHLQSISV APRTRLLKKE PMSKGINETD LFSFNESFEA PTFKVKVLTI
     SMISSAATNA KANQAANKKE DQAGGKNRNV EMDVEIEDKK REDQQIMRDV LLDRKYEIDA
     AIVRIMKARK RLEHNELMSE LIKLLIGRFK PSPQSIKQRI ESLLEKDYLK RDEQNINLYE
     YVA
//