ID K2QYA2_MACPH Unreviewed; 748 AA.
AC K2QYA2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=AMP-dependent synthetase/ligase {ECO:0000313|EMBL:EKG14906.1};
GN ORFNames=MPH_07946 {ECO:0000313|EMBL:EKG14906.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG14906.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG14906.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG14906.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG14906.1}.
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DR EMBL; AHHD01000335; EKG14906.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QYA2; -.
DR STRING; 1126212.K2QYA2; -.
DR VEuPathDB; FungiDB:MPH_07946; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_002220_2_0_1; -.
DR InParanoid; K2QYA2; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 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 InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR43201:SF31; -; 1.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 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; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EKG14906.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 504..583
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 748 AA; 81526 MW; F24B5B04C4DF2E97 CRC64;
MDTNYFICTL GQAAALDREE PKFNNINEFI DHQAEGVGDK PAVGFFEPSK DRKSPWKRHV
LDFSSLRKGS LSAANLLSRK FGEKLRQRQT VGLLCPSSPT FLFAWLGLMR LGHAVLLIAP
QSQPSAIAHL CMECQVSILL SDYPDKDLKS PEHQSRNTKT SSAQHPACSI FHLSDILPTD
ILHTISSSAT PQPTIPTAHN PTQTDTAYLH HTSGTSSGLP KPIPQSHRAA VRVLPHLPTS
PPKATFTTTP LYHGGIADCF RAWASDAPAW LFPGHALPIT AANVNACLRT VQQAGERVAY
FASVPYVLQL MAADAEAMQN LRGMELVGVG GAALPAEAGD RLAKTNREDG SFATADLVVP
HPEIENAWKY HSRADSQLTL ITGKKFDPAP LEAAIGASPF LDDALIFGSG RPFPGALLFR
SKDFDTTSEQ ELIDSVKPLI EQLNEESQDH ARIPRNMLIP MPHDPSALEK SSKGTVMRGS
AEDKYRDQIE HAYSKLSTGD GSKLPDDEVP RFITDLVEST VSKSKAPAEN DDLFAFGVDS
IACMQIRHGL RQLLPKTSPE LPLSVVEDCG TVKRLNEFVI KLRHGESFAD DEDEHDLMFK
LAEKYSKFEE SSANKQTAHG TTTRTEAPEV VVLTGATGAL GAHILHNYRR SDTTSKVYCL
VRGADEHAAK ERVNKALSQK GLPVLNSSHP GNSKVAVLQA QLGQPDLGLS AATYEKVAAE
ATIIMHVAWS VNFRMRLRSF EKDNIAGG
//
