ID D4B306_ARTBC Unreviewed; 510 AA.
AC D4B306;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Succinyl-CoA synthetase beta subunit, putative {ECO:0000313|EMBL:EFE30302.1};
GN ORFNames=ARB_02840 {ECO:0000313|EMBL:EFE30302.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE30302.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE30302.1}.
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DR EMBL; ABSU01000031; EFE30302.1; -; Genomic_DNA.
DR RefSeq; XP_003010942.1; XM_003010896.1.
DR AlphaFoldDB; D4B306; -.
DR STRING; 663331.D4B306; -.
DR GeneID; 9525059; -.
DR KEGG; abe:ARB_02840; -.
DR eggNOG; KOG1255; Eukaryota.
DR eggNOG; KOG2799; Eukaryota.
DR HOGENOM; CLU_015460_0_0_1; -.
DR OMA; HTRVIFQ; -.
DR OrthoDB; 1932158at2759; -.
DR Proteomes; UP000008866; 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; 3.40.50.261; 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; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 44..168
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT DOMAIN 386..505
FT /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00549"
SQ SEQUENCE 510 AA; 54549 MW; BCF09EFD9D811122 CRC64;
MLKTQSKSRL VGPNCPGIIS AIGKCRIGFQ PLPCFAPGNV GIVAKSGTLG YETVASTTRA
GLGQSLCIGM GGDVLAGTDF VDALKVFEHD DDTHGIIIVG EIGGEAEMEA AEWIKGYRRR
TSEAKPIMAL IGGIEAPPGR VMGHAGAWTA EGEPDARTKI QALQSAGVIM VDHPEKFGEG
MKALLAGAGR RSKPISRPSK PARFPQRRML YIKSSDAFWL LKEQDISVVE SKGPANFALA
IAIDRKTCGP CVTVSKGTDG NIRKFPFNYR ARNFDIASVK DTLGLTKYHP MATESLEKLL
HGLMNIFVTK EAFLLEVKAG IAPDAKDIQI IDARFGFDDA AYRSSGRQGD IHVLRNKAEE
VPAEVEAEKD GIVYITLPGE GRIGTLVNGA GLAMNTVDAL TLHGGSCANF LDTGGKATAE
TVKSSFRVIL SDPRVKGIFV NIFGGLTKCD MIAEGIMMAF RDLGMKVPVV VRLRGTNEEL
GQKMIAESGL PLHAFDSFEQ AAKKVISLSK
//
