ID A0A0D2AVP3_9PEZI Unreviewed; 691 AA.
AC A0A0D2AVP3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=PV09_05448 {ECO:0000313|EMBL:KIW03224.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW03224.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW03224.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW03224.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847545; KIW03224.1; -; Genomic_DNA.
DR RefSeq; XP_016213093.1; XM_016358954.1.
DR AlphaFoldDB; A0A0D2AVP3; -.
DR STRING; 253628.A0A0D2AVP3; -.
DR GeneID; 27313421; -.
DR VEuPathDB; FungiDB:PV09_05448; -.
DR HOGENOM; CLU_015460_0_0_1; -.
DR InParanoid; A0A0D2AVP3; -.
DR OrthoDB; 1932158at2759; -.
DR Proteomes; UP000053259; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053259}.
FT DOMAIN 40..135
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 351..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 74170 MW; 537CA4BEEB51802E CRC64;
MLCHSCRRSF RTQLRRSIAA NRGYANISRG KYDETIKNLK IGKDTRVIFQ GFTGKQATAN
ARESIEWGTN IVGGVRPGKS GEHLGLPVLP TVRKAMEELK PDATGIYVAA HQAPAAIEEA
IEAEVPLIVA VAEHIPLHDI LRIHQMLATQ SKSRLVGANA PGIISAIGRC RIGFQPLMTY
TPGPIGLVAK SGTLSYETVA SLTRAGVGQS LCISMGGDVV AGTDFIDALK VFETDDDTKG
IVIAGEVGGT AEEEAAEWIK DYKKRVKNPK PIAAVVGGIC AKQGRVMGHA GAWAAPGEGS
ALTKIKALES AGVTMVDHPE KFGPVMKELM AGIGYSFPSS AGSGTIGNQK RGYHTMRSRP
QVTTSTRQAQ AKRSLHLRTD QASDLLKQYD IVTSQAPSDE SDSRLLVLTV DRSARAPCII
VSPTTKKEAI YARSVHIPYD YVAGPESEHL KLALEKLQLS SSPPSVQAAV SNLITKLSKL
FKDKEAVSLE VRLTVSGTSQ SLVVYEPNFT FDDAAFRSTK RHGELHALRD TSLEDPIELA
AEPHGIVYVK LDSPTEGNAP RNIGTLVNGA GLAMNTVDAL ANYGGYATNF LDTGGKATSE
TVKKSFELIL RDERVKVIFV NIFGGLTLGD MIARGVILAF KELDMKVPVV VRIRGTNEKE
GQKLIAESGL KLFAYDDFAD AARKVIELAN A
//
