ID A0A093V2C9_TALMA Unreviewed; 822 AA.
AC A0A093V2C9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Cullin-3-A {ECO:0000313|EMBL:KFX46330.1};
GN ORFNames=GQ26_0190760 {ECO:0000313|EMBL:KFX46330.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX46330.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX46330.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX46330.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX46330.1}.
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DR EMBL; JPOX01000019; KFX46330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V2C9; -.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_7_1_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
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;
FT DOMAIN 441..687
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 822 AA; 94122 MW; 792CAC049C0A8617 CRC64;
MAMRARQKVR APRRALGSKN DDFEAIWAVL GSALREIHTK NASSLSFEEL YRSSYRIVLM
GKGDELYERV KQLEQQWLSS LVSHNIMSSV SPVLLLNIEP TDTTDQANER RAAGERFLTA
MRGAWEDHQL CMGMITDVLM YMDKVMNNDQ KPSIYTVSMC LFRDHVLRSA VPDSSLTIYK
ILESTILFMI QLERTGEMID RPLVRHCIYM LEGLYETLEE EESAKLYLSV FEPAYLQIST
IFYQNEGRRL LETADAATFC RVSSERISEE EERCRATLSS YSEQKIKAVI DEQLISKNIT
DVINLEGSGV RYMLDHDKVQ DLANVYELNA RIDPKKSALT KSIQTRIVQL GNEVNAAAKA
FATAPPPAKS TEADGEKKSE KEKPAAPPVN QQTAAAIKWV DDILNLKKKF DTIWERAFAS
DQGMHTSFTN SFSDFINSNN RSSEYLSLFF DENLKKGIKG KTDAEVDSLL DNGITLLRYI
RDKDLFETYY KKHLSRRLLM KRSVSMDVER QMISKMKMEV GNQFTQRLEA MFKDMAVSED
LTNNYKAHMS RTAADSKRFE LEISVLTSTM WPMEIMSSSK DDDAQLPCIF PKDVDTVRQS
FEKFYLDKHS GRKLSWQASM GTADIRATFP RAEGKYARHD LNVSTYAMII LLLFNDLPLD
DSLTYEEIQA RTRIPDHDLI RNLQSLAVAP KTRVLKKDPM SKDVKRTDRF FYNASFKSQF
TKVRIGVVSS GGNKVENQNE RSETEKKMNE ERGGTIEAAV VRIMKQRKKL AHSQLLTEVL
SQLAARFVPD VNMIKKRIES LIDREYLERI PDSDPPAYSY VA
//