ID G2WRN8_VERDV Unreviewed; 517 AA.
AC G2WRN8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peroxisomal-coenzyme A synthetase {ECO:0000313|EMBL:EGY13539.1};
GN ORFNames=VDAG_00221 {ECO:0000313|EMBL:EGY13539.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY13539.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; DS572695; EGY13539.1; -; Genomic_DNA.
DR RefSeq; XP_009649893.1; XM_009651598.1.
DR AlphaFoldDB; G2WRN8; -.
DR STRING; 498257.G2WRN8; -.
DR EnsemblFungi; EGY13539; EGY13539; VDAG_00221.
DR GeneID; 20701684; -.
DR KEGG; vda:VDAG_00221; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_0_1; -.
DR InParanoid; G2WRN8; -.
DR OMA; FRGYYRS; -.
DR OrthoDB; 3109088at2759; -.
DR Proteomes; UP000001611; Chromosome 2.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR CDD; cd05926; FACL_fum10p_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045310; Pcs60-like.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
FT DOMAIN 26..371
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 422..497
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 517 AA; 56280 MW; 3757F760DF7D1365 CRC64;
MALTLQTAIK GAGSSTAIII PSKPNPLTVT YNDLIKETAS FQQKLAAIGI TKGAPVSIAT
VNSYEFIISF LAASWQRGIA APLNPAYKQD EFEFYIEDVK SAIVLVPRGA YQSNAPAVKA
AKKFNAAIAE TYWDASKKEV ALDVKELGQL QGKPKEQILK PEPSDVALVL HTSGTTSRPK
VVPLTHANLT RTMSNIQKTY ELTDKDRTML VMPLFHVHGL LCGLLAPFLS GGSMIVPTKF
SAGEFWQDFA AHKANWYTAV PTIHQILLKN PTPNPLPAIR FIRSCSSPLS PTVFHNLEKT
YKAPVLEAYA MTEAAHQMTS NPLPPAKRKP GTVGLGQGVE IKILDDQGNE LAQGAEGEIS
IKGENVTHGY LNNAAANASS FTSSGFFRTG DQGKLDEDGY VIITGRIKEL INKGGEKISP
IELDNVLTRH PAVSEAVSFA IPDDMYGQDI GVAVVLKSGE KLEQDELRKW IADKLAKFKV
PKKVYFTETM PKTATGKIQR RIVAEIMQKQ DVPKAKL
//
