ID E4USX9_ARTGP Unreviewed; 603 AA.
AC E4USX9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Short-chain-fatty-acid-CoA ligase {ECO:0000313|EMBL:EFR01428.1};
GN ORFNames=MGYG_04435 {ECO:0000313|EMBL:EFR01428.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS989824; EFR01428.1; -; Genomic_DNA.
DR RefSeq; XP_003174258.1; XM_003174210.1.
DR AlphaFoldDB; E4USX9; -.
DR STRING; 535722.E4USX9; -.
DR GeneID; 10029550; -.
DR VEuPathDB; FungiDB:MGYG_04435; -.
DR eggNOG; KOG1177; Eukaryota.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; E4USX9; -.
DR OMA; KQSDMKA; -.
DR OrthoDB; 2596785at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF29; ENZYME, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G08470)-RELATED; 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 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EFR01428.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669}.
FT DOMAIN 59..459
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 514..573
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 603 AA; 65659 MW; 06B2FDE37F94F6D1 CRC64;
MAALQTDRKP TEDEMELSQL IWSASESECI WPELCSRPVR GFFDFLSPPL FEQTVGGYFA
DTVRKHGDRT AVISRHQGQR VTYAELDQRS NSLARGLAST GVRKGDRVAV SLGNGLEYAI
TTYALFKLGA VLVPLNPSFN FNQVASALSH LEASHLIIST EVNLPRRDPQ SNIPLLQEII
PNLQSAKLES TIGSLKQVVL VQNDGGRIDT SALKCITPYT SIYSELPQDM KALPDQGLSP
NDVVNIQFTS GTTSMPKAAC LSHRSILNNG VQIGDRMLLT PQDIVCCPPP LFHCFGCILG
YMATATHGSA IVFPAESFNA IATLKAVQEE KCTALYGVPT MFIEELDLIA DGVVPYEGFQ
YLRTGIAAGS SVPSELMKKL HKTLNLTELT ICYGMTETSP VSTMTATDDP IEKRLNTVGK
LLPHVEAKVV DPLDYSQILP LGEQGELAVS GYHVMKEYWD APEKTAAVMV PDSEGKVWMH
TGDEASMSVD GYITITGRIK DLIIRGGENI HPLEVENCLL AHPGVSNVSV VGVPDERYGE
AVAAFVVAHA EGEEGRVTTE EIKSWVRTKL SHHLGKSSVA ESSYPICTCT THRYPHPDPG
HLP
//