ID A0A093V637_TALMA Unreviewed; 537 AA.
AC A0A093V637;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000313|EMBL:KFX47650.1};
GN ORFNames=GQ26_0140780 {ECO:0000313|EMBL:KFX47650.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX47650.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX47650.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX47650.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX47650.1}.
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DR EMBL; JPOX01000014; KFX47649.1; -; Genomic_DNA.
DR EMBL; JPOX01000014; KFX47650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V637; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
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; PF00549; Ligase_CoA; 2.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KFX47650.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 50..174
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT DOMAIN 412..531
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT REGION 191..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 57913 MW; 58991EE35C738A77 CRC64;
MLRIHSILQT QSKTRLVGAN CPGIISAVGK CRIGFQPLPC FAPGRIGVVA KSGTLSYEAV
GSLTRAGLGQ SLCIGMGGDV LAGTNFIDAM KIFENDLDTD GIVLVGEIGG TAEMDAAEWI
KDYHKRTADP KPIMALVGGL EAPKGRVMGH AGAWVAPGEP DARAKYVALQ KAGVTLVSHP
EKFGPGMKTL LGNSGRLSNS STSPSAGQRR GYHTATRTRT RVQPIQRRFL HIKQHQAFDM
LQEANIQTQA KQASPEDFHL SITVDRTSRS PCITVSSGSK STESSLRILF NYTNPEFSTN
TTSAVQSEIV SFLGYETDHQ ETLGKYLQGL YKIFKTNEAF VLETRASFSS EKNIVVHEAR
FGFDDAAYKS SGRHEKLHQL RDVAAEVPEE VRAEKSGIVY VKLNGDGSIG TLVNGAGLAM
NTVDALILKG GKPANFLDTG GKATTATVKE CFSILCEDAR VKTIFVNIFG GLIRCDMIAE
GIMEAFKELD MKIPVVVRLR GTNEEKGQKL IAESGLPLHA FDSFEEAAEK VISLTKA
//
