ID   A0A2C5WW85_9PEZI        Unreviewed;       755 AA.
AC   A0A2C5WW85;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Ubiquitin-protein ligase E3A N-terminal zinc-binding domain-containing protein {ECO:0000259|Pfam:PF16558};
GN   ORFNames=CFIMG_002974RAa {ECO:0000313|EMBL:PHH49894.1};
OS   Ceratocystis fimbriata CBS 114723.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH49894.1, ECO:0000313|Proteomes:UP000222788};
RN   [1] {ECO:0000313|EMBL:PHH49894.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH49894.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA   Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT   "Analysis of microsatellite markers in the genome of the plant pathogen
RT   Ceratocystis fimbriata.";
RL   Fungal Biol. 117:545-555(2013).
RN   [2] {ECO:0000313|EMBL:PHH49894.1, ECO:0000313|Proteomes:UP000222788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH49894.1,
RC   ECO:0000313|Proteomes:UP000222788};
RX   PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA   Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT   "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT   the plant pathogen, Ceratocystis fimbriata.";
RL   IMA Fungus 4:357-358(2013).
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:PHH49894.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; APWK03000161; PHH49894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5WW85; -.
DR   STRING; 1035309.A0A2C5WW85; -.
DR   OrthoDB; 1333844at2759; -.
DR   Proteomes; UP000222788; Unassembled WGS sequence.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 2.40.40.50; Ubiquitin fusion degradation protein UFD1, N-terminal domain; 1.
DR   Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR   InterPro; IPR032353; AZUL.
DR   InterPro; IPR042556; AZUL_sf.
DR   InterPro; IPR004854; Ufd1-like.
DR   InterPro; IPR042299; Ufd1-like_Nn.
DR   PANTHER; PTHR12555:SF15; FUSION DEGRADATION PROTEIN (UFD1), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G04640)-RELATED; 1.
DR   PANTHER; PTHR12555; UBIQUITIN FUSION DEGRADATON PROTEIN 1; 1.
DR   Pfam; PF16558; AZUL; 1.
DR   Pfam; PF03152; UFD1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000222788}.
FT   DOMAIN          642..670
FT                   /note="Ubiquitin-protein ligase E3A N-terminal zinc-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF16558"
FT   REGION          124..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  83983 MW;  8BB1E3946923AD7B CRC64;
     MAFPSEAPLP LKWSATFQLM HPDEARARNL VGDKIVLPQS ALEQLLAAAE RVNSDSSSPY
     RDYQGFQSSS HDQKLPHPLM FRLSNPVTGK TVFAGIQEFS AEESFIGLSP YLAETLGIDQ
     QATLHPANSN SPVDLTQDDD SANPSDNKFA ATTFPPIVVH AQQAPKGTFV RLRPLEAGYN
     SEDWRALLEK QLRARYTTLT KHAVLSFANG TAKYSFLIDQ LQPEGHDGIC VVDTDLEVDI
     QPLNEEQAKK TARILSERNS GSEGSSAGGE IDIWKAVDGQ VVPGDYVNYQ LPSWDHNRPL
     KIQVSGINSN TSIDLFVSPY STRHRAPPRS HEHVFGNYEP AKDGTKSITI QPSNVELENA
     DSLLIAVHGY QGPSTSSHSV AFSLRASAVS EPSNSPSSEP TPNSESRGDA DEQCKNCQQW
     IPKRAMLLHE NFCRRNNVTC PQCHNVFQKS SEEWANHWHC ARDDAFGSSP VSKSKHDTIY
     HTKYTCEDCK QEFESLPLLA QHRTSVCPSK FILCQFCHLE VPQDGDPANP SAEMILSGLT
     AHELADGGRT TECHLCDKIV RLRDMQTHMK THELNKVSRS PPPVCRNRRC GRTRFGVGPR
     GAVHSFAEPG SVDRLGFCPG CFEPLFATVH DPDGKAMRRR IERRYLTQLI AGCNKASCTN
     EWCKTGRKNQ GLEPKGSKTS EALPMVKPLL EKIWQEDTPM FLCVEDLNQK RWSLAEMLAA
     ENVFGLEWCI AAAEAENGDL DNMRVWLQNW APRKV
//