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Database: UniProt
Entry: A0A150VCU4_9PEZI
LinkDB: A0A150VCU4_9PEZI
Original site: A0A150VCU4_9PEZI 
ID   A0A150VCU4_9PEZI        Unreviewed;       661 AA.
AC   A0A150VCU4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Cullin family profile domain-containing protein {ECO:0000259|PROSITE:PS50069};
GN   ORFNames=M433DRAFT_61640 {ECO:0000313|EMBL:KYG48173.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48173.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG48173.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG48173.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00330, 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:KYG48173.1}.
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DR   EMBL; JPDO01000055; KYG48173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VCU4; -.
DR   STRING; 766039.A0A150VCU4; -.
DR   Proteomes; UP000075602; 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   InterPro; IPR044554; APC2-like.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          261..544
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
SQ   SEQUENCE   661 AA;  74691 MW;  5B1F9B6175C83BDC CRC64;
     MADVGFCGAE PTRIFVAALV KCVETVVRTR PCFAVDWIRR TTVVPRLRRW VDIQLAPAME
     RCLLILEGKD QQQSRTGFTN LLSDIVVRKL GEVRAELLFD YIKMWPNSEG AILDIRELIL
     LVPSEKLNIC HSFTTQIRHR LLHAGASTAE ILSIYISVIH AFRLLDARGV LLEKVSTPIR
     TYLRSREDTV GIIAASFLAE VDENGKISSP DPLKVCSEIT LHVANSTLED AKDHQMLNLD
     DMSWTPDPID AGPDYKGSKS EDILDYILSL FDPEDFIKEI TKVLAQCLLE STDPEFIKET
     RLIELLKSRK LDVMKLQAAE VMLKDVRDSV SLNKRINPCA KQRFAGPPQP KEIQAAIPDE
     GISLQSLYRI FERRVSVAEF QAALRLVAVR RGELYFPKRV LRSQDAADQG ESYMASDVEY
     GVQVVSSFFW PQMRSNSFNL PTVLAELDDS FNQHFSQLGN QRKLHFRRAV ARVTVDLQLE
     DRNIREEDVP AWRATVIDAF ASERGNAGAG DISYDPEEGL TVDLLVERAQ MEEDLVRDAI
     RFWVGKQVLY EKSPGVYGVL ERLDMEIMPA QQLPMPEDTV SAMVSQDAML RESAPMFEAF
     IMNMLQNGGP KEVGGFIGIT NTMKMVLPAF AYGDDEVVWL LREMEKKGQV ARNGEVWSIC
     R
//
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