ID A0A194V930_9PEZI Unreviewed; 883 AA.
AC A0A194V930;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha, mitochondrial {ECO:0000313|EMBL:KUI60465.1};
GN ORFNames=VP1G_07658 {ECO:0000313|EMBL:KUI60465.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI60465.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN714751; KUI60465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194V930; -.
DR STRING; 694573.A0A194V930; -.
DR OrthoDB; 1932158at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:KUI60465.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT DOMAIN 43..137
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 95368 MW; 826E52F8D3089C35 CRC64;
MQSAMRHHMR PTARGHAPIS PSRCFTTSAP RHNYAATLKN LRIGRNTRVI FQGFTGRQAT
ANAQDSIKWG TNIVGGVVPD RQGEHLGLPV LPSVRMAMEQ LKPDATGIYV PASRAAQAIE
DAIEAEVPLI VAVAEHVPLH DMLRVHSMLR TQTKSRLVGP NSPGIINAAE GENCRIGFQP
LGSFSPGCVG IAARSGTLSY EAVAATTRAK LGQSLCIGVG GDILPGTDLV EALQVLETDP
NTKGIALIGE IGGDGEIMAA QWIKEYHDRT PAEKRKPIVA VIAGKHAPLD RVMGHAGAFW
LPGEPHPNQK IAALKNAGAV LVSHPAYIGR VLKDRIKLEP AQEDKDSTPH EFDNGASFES
VDDFARAASR RVPQQQHRGL HTSTRGSGLA PSRPRMSKSS VHHHQIRSLH LDRAASQSLL
RDEGKAAELR FQTYPIRYLA LDIDRTTRSQ CLVTAVIYKG QDWRNPASFN KILLPPSAKN
GVLSLNSKDS HTVITKLIEQ LQIMGHESVN YRSALGRILR DLTRVFNEKE ARHVSLQFAV
NQKGKQAFTM QDMRIDLDDS AYRSGGRLAE VHEAYGALEA RDPGARQAEK SGIVYHRLNP
RDRSCNIGTL VNGAGLAMNT VDALADAGGK AANFLDTGGK ANSDTVKKAI EIILQDDRVK
VIFVNIFGGL TRGEMIAAGL VHAYKNINIE VPIVVRIRGT NEWEARKVIE KSRLPMYAYM
HFDEAAAAAI DIAKGAMPPV QEPYLEGENE VSGLKDAIQL AAETITEEGG SGGESTAATH
AEESAHVPAE EAPEAVISKE TSQLPAEEVT EATDSEATSS EAIFEVTNSE ESSQPPAKGA
TEPAEDDFSQ PQDAEQETQK SQEPEKKVEG TTTAQSQGSD QVA
//