ID U7PX49_SPOS1 Unreviewed; 751 AA.
AC U7PX49;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=HMPREF1624_03605 {ECO:0000313|EMBL:ERT00234.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT00234.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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DR EMBL; KI440844; ERT00234.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PX49; -.
DR STRING; 1391915.U7PX49; -.
DR eggNOG; KOG1255; Eukaryota.
DR eggNOG; KOG2799; Eukaryota.
DR HOGENOM; CLU_015460_0_0_1; -.
DR OrthoDB; 1932158at2759; -.
DR Proteomes; UP000018087; 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:UP000018087}.
FT DOMAIN 53..147
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 355..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 78859 MW; 91C5AAF1D81094B0 CRC64;
MLPVRPQLSR QARLGRPCVV CRSLRRYSSI SSLTAPSPVT SLSTDATLPN LRIGRHTRVI
FQGFTGRQAT ANARESLAWG TNIVGGVTPG RSGEHLGLPV LPSVCAAVET LKPDATGIYV
PAPLAPAAIE EAIAAEVPLV VAVAEHIPVH AMLRIHAMLK TQSKSRLVGA NSPGIISAVG
ACRIGFQPLP CFSPGSGPGT RVGIAAKSGT LSYEAVASTT RAGLGQSLCI GVGGDIVAGT
DLRESLTVLA DDPETDAIAL IGEIGGTSEL EAAAWIEAYR KRAQAAGAVP KPIVALIGGT
HAAVEGRIMG HAGAFVLPGE PTAQEKIQAL ERAGATVIDH PEKFGQAVKA RLDALSPSGS
GANSSSLFGQ AGPTSQRRSM HTSTLSRNGN SKRPMIQRGL MLRRPSQTIA QKRSIYIGQD
ATFDLLRKEG VNAAPYSGQG TQRYLAITID RSSKMPCVLA APNYNDSVSS IRNLRRFPFG
YRAGVDGLLA ARVADHLGLD TTSSTSETES LRKLLRVLYA IFLEQEAYLV ETAIVARLAD
VKVVHARLGL DDVAFNQRKA TGDETTLRLA SVTPPMEANE REAAAKKDGI VYVTLHDNDD
SNNNDNDNSK QGRQGAAAPA TIGTLVNGAG LAMNTVDALA GLGGQATNFL DTGGKATSET
VKTCFQVLLQ DPRVRVIFVN VFGGLTLGDM IARGVLLAFK ETNVAVPVVV RIRGTNEAEG
QEIIRTSGLP LFAYDSFDEA AAKAIELSKA A
//
