ID K1WGW3_MARBU Unreviewed; 613 AA.
AC K1WGW3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Ubiquitin-protein ligase molybdopterin-converting factor {ECO:0000313|EMBL:EKD16820.1};
GN ORFNames=MBM_05289 {ECO:0000313|EMBL:EKD16820.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16820.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16820.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16820.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921438; EKD16820.1; -; Genomic_DNA.
DR RefSeq; XP_007293178.1; XM_007293116.1.
DR AlphaFoldDB; K1WGW3; -.
DR STRING; 1072389.K1WGW3; -.
DR GeneID; 18761224; -.
DR KEGG; mbe:MBM_05289; -.
DR eggNOG; KOG2018; Eukaryota.
DR HOGENOM; CLU_013325_9_3_1; -.
DR InParanoid; K1WGW3; -.
DR OMA; SLNRHSC; -.
DR OrthoDB; 10004at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00755; YgdL_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF2; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE 1-RELATED; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EKD16820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 213..468
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67863 MW; 94D05EA128591DD8 CRC64;
MDWRYNQRAS SSRQSYNYNY DQYYYSDEED DEYPPRYQYQ SRNQELEPQP SYTQRSPSPD
SEIRHQPPTD VQGPKKGKES MSSWLSRTAS TSQAQFAATA LVSGAVVAGA IFGYQHVRRQ
ERVEDLKSSI PALGRSHQAD KGLLVLMDEV KLTDFGAAPS KTGMSKEDER SLEFAERAQR
GDYDDGLSWG NSRAVEGEVL TWEAELILEQ LARNRVFLKD EGLAKLRSAF IIVVGCGGVG
SHCTAALARS GVSRIRLIDF DQVTLSSLNR HAVATLADVG TPKVSCLKKR LQQVTPWVHF
DLCNELFGAS AASRLLGDWE GRKPDYVVDA IDNIDSKVAL LEYCYKNQLP VISSMGAGCK
SDPTRIFIGD ISASTEDPLS RATRTRLRKV GVASGIPVVF STEKPGPGKA QLLPLPEEEY
AKGSVGELGV LPDFRVRILP VLGTMPAVFG YAVANHVILQ VAGYPNEYVP AKGREKMYDS
ILAALQGSEE KLVRATVPGE DARGLKTGIT VADVGYVVEE VYRGKSAISG ISTRLTLVRW
RKPEGSMVEL GVEGQKSSKV KARELVCMTK EEGARHEREV VNGMKSPEEM YDRETVAYVE
ARIREEIGYE KYR
//
