ID M3CDS5_SPHMS Unreviewed; 1286 AA.
AC M3CDS5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=NRPS-like enzyme {ECO:0000313|EMBL:EMF11166.1};
GN ORFNames=SEPMUDRAFT_150169 {ECO:0000313|EMBL:EMF11166.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11166.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF11166.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF11166.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
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DR EMBL; KB456266; EMF11166.1; -; Genomic_DNA.
DR RefSeq; XP_016759287.1; XM_016905997.1.
DR STRING; 692275.M3CDS5; -.
DR GeneID; 27903134; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_000022_2_17_1; -.
DR OMA; VYSACET; -.
DR OrthoDB; 3305653at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
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; 2.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 538..615
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1286 AA; 139414 MW; A250FFC2F0CF7484 CRC64;
MADAATLKMT VIDTTKDLSA LFDKQVQISP HAVALEDEKA TYTYSELATK VNDLARRLRL
HGVKRDSLVG VLLPRSADYV IACLAALKAG GAYLVLELAY PPDLLADVIE DAAPTVVILN
ESETGKIKPE IPLIVLDEER EGLTNGHVEQ DDNVSDPSDL EKLAFVAYSS GTTGKPKGIA
NPHRASVLSY NLRFGISDVQ PGERVACNVF FVWEIFRPLL RGATVVTVPD EVSYDPQALV
QLLVAKKITE TLMTPTLLAA VLARFPDIGS RLSGLRSLWL NGEVVTTDLA RRALKAMPKV
RLLNCYSACE THEIACGDIG EMINDDMLNC PVGKPMEPDF IHLLDEDGKE VEPGKSGELY
VGGSLLARGY LNRPESTAAA FLPDPYNSSN PDARMYRTGD LAILHTNGLL EITGRTGTMI
KLRGYSVVPA KVEDTITKYL GVRQCVVTAY GEGLERQLVA YFVKDEEATS ERAFVEVDES
NHSSAARKIV APYLAQYMIP TLWVALNELP THSVSGKIDL KSLPSPIPAK AANGEKPAKD
PISIEDVAEI WAATLGVSQK SLKPEDSFFD LGGHSLSLAA LAAKLSRRFG FRMPVGRLAD
PPTLESHLLT VREVRDGTIA AVQSDLPAAL RKDSYLDRDI EPNNAKICSL KDAKTVLLTG
STGFLGAFLL NELLESTSAK IICLVRSPDA LEEDKPSCTA RLRKNLIDLG LWSDSIMERV
EVLPGDLPRK RLGLSPEKFN DLGERVQVIV HAAAQVNLVY PYAALRGSNV DGTKEILRLA
CLGGATVQYV STNGVLPPSE SGHGWPEDAM LYVDAVPEKI PDGYGQTKWA AEQLVLEAGR
RGLPVRILRA GTISGHSMTG AANAWDLLTA LFVESIHLGF YPNVQGWRAE MTPVDFVSKA
IVHLGNQTHA KQLVFHLGDP DPIETKTVFE HFAELGYPTE PMDFDEWVNL WTEKRGSAKG
GDGAFTVDIM RSGMPSVGFL RDIVVLNNAQ TRPYRAIVER PKVDSVLLET YARHWFARGW
MNQAPLRNSA PGGSALSVRK SILTGRVAVI TGASSGIGAA VASALAVEGC HLVLAARRTA
ALENLKRRLV VREGKVIIKQ TDVTDKAQVD DLFKTAEKEL GPVDILVSCA GVMYFTMMAN
VQMQEWNTTV DVNCKGLLHC LSASVPSMLD RGTGHIVAIS SDAGRKVFPG LGVYSASKFF
VEATLQSLRL ETAGKGLRVT SVQPGNTQTD LLGMSTDAEA IQKFGQPSGA KILDPVDVAN
AIVFGLKQPD YVAVNEILIE PRDEPI
//
