ID A0A318ZAQ2_9EURO Unreviewed; 682 AA.
AC A0A318ZAQ2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=BP01DRAFT_424199 {ECO:0000313|EMBL:PYH44426.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH44426.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH44426.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH44426.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ821237; PYH44426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZAQ2; -.
DR STRING; 1450539.A0A318ZAQ2; -.
DR OrthoDB; 1932158at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11117:SF6; SYNTHETASE SUBUNIT ALPHA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G10830)-RELATED; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 2.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT DOMAIN 45..139
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 682 AA; 73603 MW; 899FF4CCE06E5D2E CRC64;
MMTRLCSLPA RRATLQQLKA PLVRPHQFST SVRTDNYATL PNLRIGAHTQ VLFQGFPGRQ
STANVRESLA WGTKVVGGVK QNARGENLGL PVFRSVREAQ QNVRVDASAV YVPGGSAAAA
IEEAIEAEVP LVVAVAEHVP IHDMLRVHSM LKTQSKTRLV GANCPGIISV TGKCRIGFQP
LPCFTPGKIG IVAKSGTLSY EAAASTTRAG LGQTLCISMG GDVLAGTNFV DALETFESDA
ETEGIVLVGE IGGTAEMDAA EWIRDYHRRT TNPKPIMALV GGQHAPSGRV MGHAGAWTAP
GEPDARDKYQ ALESAGAVMV NHPEKFGPGM KTLLESRGRA QSANFTKGVS QQRGFHTLRR
ASLSTNHSAR QQQQARNLYV KPFQALDMLR KKSIAVKEAA STDADFFLAL TVDRTALSPC
ILASSTAAFN PEHTGRFPFP FQNADFSSTN PLTQAVASHL RLPSTQQERL TELLRALWQI
FTEKEAYLLE VRANSTDALE VREARFGFDD AAFRSSGRQE DIQSLRNPAE EVPEEVLAEK
DGIVYVKLDG EGSIGTLVNG AGLAMNTVDA LTMHGGHCAN FLDTGGKATS ATVKASFQII
LSDPRVKAIF VNIFGGLTRC DMIAEGILLA FQDMDVRIPI VVRLRGTNEQ EGQRMIAESG
LPLEAFDEFE AAAKRVIELA QQ
//
