ID A0A166R4C1_9PEZI Unreviewed; 1938 AA.
AC A0A166R4C1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Peptide synthetase (AMP-binding enzyme) {ECO:0000313|EMBL:KZL68741.1};
GN ORFNames=CT0861_07167 {ECO:0000313|EMBL:KZL68741.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL68741.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL68741.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL68741.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL68741.1}.
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DR EMBL; LFIV01000121; KZL68741.1; -; Genomic_DNA.
DR STRING; 708197.A0A166R4C1; -.
DR OrthoDB; 3305653at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19542; CT_NRPS-like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 772..847
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1416..1492
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1938 AA; 212994 MW; C0D19AABA30C5DC8 CRC64;
MHLRDSEGGG TAYQENGHAD GANGLTNGTA NPSSTRTIAV TPRTEAGGVS DFRHELLLAW
LLVLYRNNDD GLSRVNWGFR TREGQQPSSA THNSLSLSEA PFKNSDSISE ALEVIKDLGE
RELGSDAQTV PVIYFNNGAP ATQGNLEKTP SKRSHDWTYQ VETTINEKQM VIKAQWDRAV
LSHRHATFQL DSFVEILTTI LEKPYRQISD TIGPTAKDLE QLWTWNAELP ENMQRCMQDI
IAEVANNGPD RPAVESWDGN FTYGDVERLS TRLARHLVHR GVKVGSTVPM CFEKSRWTTV
ALLAVMKAGA AFALTDPSQP EARLRTIVEQ TGATIIVTSQ KQSELGRRIA PEGTLIVASD
ETLNQDTLEL APELPYIPPS SPLYIQFTSG STGKPKGVMI SHENFTSGAV PRGWAVGYRA
HSRCFDFASY AFDVAIDCML CTLAAGGCLC IPSDEDRMND LSGAIRNSKC NMAHMTPSVA
RVLDPDVIPS LEVLGLGGEA VSAGDASTWS KTTSVIIAYG PSECTVGCTI NSNVSSTSTN
IGKGCGGLTW IVDPDDHERL MPVGAVGELL IEGPVVGLGY LNDKAKTDEV FIEDPAWLLA
GGGPARGRHG RLYKTGDLVR YDPDGTGSIA FVGRKDQQVK LRGQRIELAE VEHHLRGKMP
SGVKIVAEVI KPGGSEPTLV AFVVEQNPVD NPESEGDVTV FSPEFSQAIA EIDIALGAEI
PRYMVPSAYI PLRKMPSLVS GKIDRKRLRE LGGSMSREQV ARLRVAPTEK NEPETEMEKA
LQQVWTKILG SEASIGLHDS FFALGGDSLR AMKLVAAARE AGIALTVASI FNFPTLKDMA
QNATKVSKED EAAVVPFSLL EEGWTPEEAC AESAKLCGID ESAIEDIYPC TPLQEGLMAL
SAKVKEAYVA QRVVDLADSA TADKLRNAFD IAAADCAILR TRIVQVPGRG LAQVVAKEDI
AWHVGDDLQG YLVKDREEGM DLGRPLVRYA LITEKETGKV KFILTMHHAL YDGWCMPLIV
DKVNKAFDGV RVQRPAEFKD FIKYLGSTDR NAAETYWRDQ LQGANGPQFP ALPYEGYQTQ
ADSLLEVYVP LSGRPASNTT VATVIRGAWA YVASHYSSST DVVFGETLTG RNAPIRGAEE
IEGPMITTVP FRLQINGETA VSDYLQDIQD QTIQQIPYEH TGLQHIRRLS PDALEACELR
TGLVLHPSAD DFDQEEFNKY PANRLVPAGD AEAAEEALKF NTYALMLVCS TDPKGFLVMA
SFDSKTVQKP LMEKALAQFS QVAQKLCQLT DTPLGDVAYL TQEDQAEVSR LSTESVKSVQ
EEYPEAEAVW IVNPADSGRL APLGVVGELV VGSKADLSLS TLEKPSWAED NEAGKFYRTD
RLAKFNPDGS LQITGKKSDL VQKSSTASKA PTKRISATSA KQRRLRTLWS RVLKIPEGDI
GLNDSFFRLG GDSIGAMKLV SEARLAGLTL TVNQVFSKRT LYDMASILQD SEPTQGSQDT
AKALAPFELL ENFGDAPAET LRPLLADPTW KIVDAFPARP LQEVAVKGTI EIPRFSARYE
AMYFESDVDR PRLFQSCQEL VNLNEVLRSV FVKHDGTCLS VVLEDVKTLV VEHEIDGDVE
TFVKDLCNLD VQTRMPLGSV FVKWFFVHSS SGQSALVFRV SHAQYDEICL PIMLHQLSAL
HEGKPVPKSL PFSSFVGHVV KSNVPQSIDY WKELLEGSSI NVLKPETPVT ERQHYAIDRT
FDISSRSKDV TIATLPTAAW ALTLARMQKT RDVTFGEVVS GRNIDFPNAD MVVGPCWQYV
PVRVKFEDDW TVLDLLNLVQ NQHIASSAHE GVGLPEIKKF CAPHWPEETD WFDTVVHQDV
EHVESLGFET ASSRMETIYP HQEPLREWKI QAFPQGDKLT IEIVTFESWK GHAKDLLDEI
ETTFKVLLGN PRALLFEQ
//
