ID A0A3F3PYX3_9EURO Unreviewed; 1056 AA.
AC A0A3F3PYX3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:RDH32144.1};
GN ORFNames=BDQ94DRAFT_145522 {ECO:0000313|EMBL:RDH32144.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH32144.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH32144.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH32144.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ852051; RDH32144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PYX3; -.
DR STRING; 1341132.A0A3F3PYX3; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 561..640
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 117246 MW; 295EEF2B9CDF5592 CRC64;
MGIPQYDGVT DQGPKPTTNT TDQVVARFGR LHLLDDLIRL RAADYIQHPI LAYPKPSQNG
SVSYEYFNGQ DLDCMIDYAV CTLMDYGFKP ARKEGATVAL FTLSDLNMVI TFFALSRLGY
TVMMLSPRLS ATACVSLLDT VGCNTILYGQ SPNIRATMGE VLRLKLIACR PIIERPSPEE
LSEDSDAVVI CRSRRPELQV EKTALILHSS GSTGTPKPLY LSHKALMTHP MRGPGFTSFN
SLPWYHLHGL STALQAMYMR RTAYMWDASL PLTASTAVAA LEAARPESVQ GVPYLLQLLV
DSPRGLKALR ACKSVTYGGA PCPDELGDRL VDEGVKFGGS FGLTEAGLVA ESISRPAGDP
FWNYMRFFDN IKPFIWMKPI SDALYEVVYL KGHPALTASN SNEPPGSYHS RDVFTPHPTL
ADRWKYVSRL DDRITLVNGE KVLPLPIEGC IKQSPLVQEA VVVGVNKAVP GLLVFRTESS
QMFSDEEFLD LLWPTVEEAN SRAEQFSQIS RDMILVLPHD CTCPRTDKGS MIRAQVYAKY
AETIENMYTT LEQTADGTLK LDLTATENHL IKLCHEELGF PISTPNSDFF AEGLDSLKAI
HLRRLILRDF KVEDPKDIGH NVAFETGNIV RLAEHIHLIQ SGQKDMVEDE VSMMPELIEK
YSVFQKHTPS PSSAATRKSV VLTGATGSIG AHTLYKLLND DSVSAVYCLT RRSQPKKAVI
DALAQKGLSV LPYRLQKIVA LNSSLEEPDL GVGESMMAEM RQSVSLIIHT AWPVNFNLPL
MSFESHIKGL QNLINFSLSV NLPDPAVLLF CSSISTALGA SSDVDERPIE DLASALEMGY
GRSKLIGEKI VSNARRAGAR TYSLRIGQVS GHSKKGLWND SEAIPLMIRS ALTLKALPDL
DITCSWLPVD KLACSMLELA RTCSFNSLED SCDDATSGKW VDDTIYNLCN PRVFTWSSLL
DTLKRSGFSF ETVPFENWLQ MLRESEARGE EMINPAVKLT AHYESMYSED APKPVRFLTE
KAERDSMTLR NGRLRIVQDG ILTRYAQDWL KRWKSA
//