ID Q0D1A9_ASPTN Unreviewed; 577 AA.
AC Q0D1A9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Succinyl-CoA ligase alpha-chain, mitochondrial {ECO:0000313|EMBL:EAU38921.1};
GN ORFNames=ATEG_00275 {ECO:0000313|EMBL:EAU38921.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU38921.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH476594; EAU38921.1; -; Genomic_DNA.
DR RefSeq; XP_001210361.1; XM_001210361.1.
DR AlphaFoldDB; Q0D1A9; -.
DR STRING; 341663.Q0D1A9; -.
DR EnsemblFungi; EAU38921; EAU38921; ATEG_00275.
DR GeneID; 4355026; -.
DR VEuPathDB; FungiDB:ATEG_00275; -.
DR eggNOG; KOG1255; Eukaryota.
DR eggNOG; KOG2799; Eukaryota.
DR HOGENOM; CLU_015460_0_0_1; -.
DR OrthoDB; 1932158at2759; -.
DR Proteomes; UP000007963; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
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; 1.
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; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EAU38921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 42..140
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 558..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 62184 MW; 752F585D7487050D CRC64;
MPQISSLAAR TRRIIPAAGN RLARFSTSSR SYDYADTLPN LKIGAHTRVL FQGFTGTSAP
TATANVKESL AWGTKIVGGV KPGVEGEHLG LPVFPSVKAA QEKARPDASA IYVPGNQTAQ
AIEEAVEAEI PLVVAVAEHV PIHDMLRIHS MLKTQSKTRL VGANCPGIIS AIGKCRIGFQ
PLPCFAPGKV GIVAKSGTLS YETVASTTRA GLGQSLCISM GGDVLAGTNF VDALKIFEDD
PDTEGMIIVG EIGGTAEMDA AEWIKDYNRR TANPKPIMAL VGGLYAPSGR IMGHAGAWTA
IGEPGPEEKY QALERAGAVM VNHPEKFGER MKTLLASRSR ASGAVATSNA AGQRRGLHTM
RRVIPRRQGM FPQNQKRSLF VKQFQALDML REKSIPVREA TPAESDIYLN LTVDRTALSP
CILASTSADF TPAATSRFPF PYATTQFTDG ENSIVEAVAS HLQLPPSAKG RLAELIQALW
EIFKEKEAYL LEVRTISVDG AFEVRGARFG FDDAAFRSSG RQEEVHRLRQ LEEEVHEEVE
AEKDGIVYVK LDGEGSIGTL GKIPTPSVQL HTKTNKQ
//
