ID A0A317XJP9_9BASI Unreviewed; 357 AA.
AC A0A317XJP9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:PWY98505.1};
GN ORFNames=BCV70DRAFT_193248 {ECO:0000313|EMBL:PWY98505.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY98505.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWY98505.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY98505.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819198; PWY98505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XJP9; -.
DR STRING; 1882483.A0A317XJP9; -.
DR InParanoid; A0A317XJP9; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000246740}.
FT DOMAIN 60..156
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 357 AA; 36968 MW; C1B657A2DD930AF7 CRC64;
MAIASSTTKL AAVRGLLKPP SASAPASASA SAAISASLRR TFASSSRAAG SYSDTINHLA
AGPHSRVIVQ GFTGKASSVH TKISIDMGTN VVGGVSPGKG GQTHLDRPVF NTVREAAEKL
KPDCTSVFVP PALAADAIIE AIEAEIPLIV SVAEGVPAKD QMKVMAALHS QSKSRLLGAN
SPGYCNPAGC RMGISPMITC ARGPVGIASR SGTLSYEAAY ATKHLGQSYI LGLGGDFYPG
TRTVEALQFL LDDPHTRAVV IAGEIGGSME EEVYDLLADP ASPYRVGDSF VKPIVGFIAG
LNTPPGQMFG HAGAIWRDST SSALQKRELW EKAGIRMADA IADVGKLVEQ ELAAARQ
//
