ID E5A5P4_LEPMJ Unreviewed; 2419 AA.
AC E5A5P4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE SubName: Full=Similar to nonribosomal peptide synthase GliP {ECO:0000313|EMBL:CBX98942.1};
GN ORFNames=LEMA_P081810.1 {ECO:0000313|EMBL:CBX98942.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
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DR EMBL; FP929134; CBX98942.1; -; Genomic_DNA.
DR RefSeq; XP_003842421.1; XM_003842373.1.
DR STRING; 985895.E5A5P4; -.
DR EnsemblFungi; CBX98942; CBX98942; LEMA_P081810.1.
DR GeneID; 13282411; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1176; Eukaryota.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_0_5_1; -.
DR InParanoid; E5A5P4; -.
DR OMA; CCIKEVF; -.
DR OrthoDB; 1949608at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd17653; A_NRPS_GliP_like; 2.
DR CDD; cd19537; C_NRPS-like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
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; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF11; NONRIBOSOMAL PEPTIDE SYNTHETASE 5; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 534..610
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1570..1646
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2106..2179
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2202..2286
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 2292..2419
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 16..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2419 AA; 269304 MW; 41E8BB7BC6BA6614 CRC64;
MHITKDIDTI FHRSLEGLTG DDHSPESRRD FPMSQSSGCR NGTDATVCHI FERIASQFPE
SVAAEDGGRN ITYGELHYAS NHLANHLSQI GIQSGQKIVI ISNRSLEMIV ALLGIMKSGA
CVVPIDFETW SQDRIQTTLE TTQCRYAIST KCIEIPNQEL ILFQEGDLQH VLDNRRDQPA
SFSTRGFQLP SADDLAYTIF TSGTTSKPKG VMVPHSAIAH YVQQVSDEAP FNLNVQASSR
VLLVFSVAFD ACLGVVLSTI CNGGTLILAT SMNFATVATT CTILPLTPTI LSTLRPGAEY
DSIKSIFLGG ESPSPNLLRP WLNGERRIFN CYGPTETTCT SLIKEVLPDE PNHLRYTVAG
SSVVLLDGNL REVSEGEIAI SGPGLAVGYF NNQALTAEKF IVYKGVRHYL TGDYGRKTSF
GIDFLGRKDR VVKNRGFLIN LEAEVEAVIT NMKLANSAAA LMHEGRLIMF VTPETIDVSS
LRSRLLEIRD SFLVPDRIYA ICSFPITSNG KVDLASLRQL LQEEKFTGVA THQSSPSSNL
YVVLEGFSKV LGLPPSALCG SSSFLDNGGN SLSAVSLASH LRERGLSITV REIFESDTAQ
RICDTLSATI LSTSDSEEAD LESLRENVVR AGYPLTPRME VAYMTAIQVN MIQSTIKMPS
MNYIQLSITF DLSSGLFKPE VFRRAWEIIV QRHSILRATF IPALEATVIA ADPTMDWREQ
LVDSSEWDSA VADAREKILC SMAPLDAEYL KPRSIFRLIT EPKSRTEFIW TIHHSLVDGW
SIAVIMRDLQ CILSQEELPK VAQFTSVATV QKALAQRSLS RGKQQSWEEK MQNYIPAPRL
RLPKPQGWAR AARAERRQLL GVHRSQVQRF VQEYRVSDAS IFLASWALVL SKYLSTDRVL
FGVVLSGRNL PMAAVDQVVG PLLDTVPFPV NTTSTQSTAE FLRTIHGTLH EMNESPWEMK
LQKSSMGPES LETLVALQYD LPDSTWNVDP KTWPSPQSMK HNETTELPLH ILIDMQNGGD
LEARYLYDCS HFEAAMIDQM LSHFSNMLKA ILMHPTVELV KSSMMNQLEI NDLLYSSPHM
HDAYDGPQSL KQAFEEVVDT WPDAIAVESV SDSISYKELD HRSSAISNAL LPLVGPGQIV
GILSDGSVSW ITAILAVLKA GAAYCPIDIA LPEERIKVML RESRCSLLLC TTEDLCELWA
NHSDLTCFSI GRLLSETLQT PERLPERCSP HDPAAVIFTS GSTGVPKGIL LEHIGILSLL
DFPNARLRSG PGRRNAQFLS LGFDCCVNEV FATLCYGATL VLRDPLDPVQ HIKRVHATMC
TPSFLATLDV NDFPNLELIA LAGEPVPQKL VDTWGHNRVL LNVYSPSECT ISTVYPQLYP
GVQVTLGSPV PRQAIYILDK DLNPVPVGVP GEICISGIQV TRGYLNRPEE TLVKFLPNPF
QKGWRLYRSG DLGRLTNSHE IEYIGRIDNQ VKVRGFRIEL EEIESTIAAL NPEVRQAAVI
VVNDVLIGFV TPSSLDTLAI QAIISRHLPS YCRPSYFVAL DNMPMSSNQK IDRKKLVSMK
AERNHFTKVP IEGTTERIIQ EIWKDLIPEL GEVSALDNFL QIGGHSLLQA RLTRQLGMAL
GNRIPLRIVI QNPVLRDLAL AIDKHILDGG SEDISRGQPE QNTVLSHLEE EMYTVHMLSS
EPSAWNIPYI ARLTGPLNLA AFEASWNNII RSNSILRARY QIKDGILTRS ISTSISPVTR
RYCKVTDDAL LDIVNRAFDL ANDQPIRLDL CLDRPTMSYV VLNMSHMIGD RSTMGEILRL
LEEEYAQMIL NDNFNLHEPL SESLPYSVWT AMRRKREVDA GLTHVLQKSL NPSLINPPLF
GTFKQELACS AHRDKRIEGD LFSSLKNLRG RFKASGHQLA IAAVGLTLHR LSHREDFIIA
APIEDRTEAG TENMFGLFLD RLLIPLRFNL HSPHSADDLI HMVKSASEQA MANYIPFADL
KNVLGMVGKS HSLCEIMVTY HASDLQGPNL TGVDALGIPV QPKGVKFPLM LEFSEFPESI
GIDLAYDSHA IDNATMDEFE VQLMAAFRYL ADETCSSTCT TYPPRLFPLI WSQKDTNTVA
PISEDQEMID LVREAMAECV GLNRCDISCS RSFFELGGSS VDCLRLQDRL IKSGVSVSLS
SIIHLQTAEL IAGAMENVNN RCIHRFTMTE RPKDIPEDKL VLYVVKATPT STANTVKPLI
VMNELSIDHE IYVVPSPTRD EWFHQINPHK MVPAIESAET RDGKRLNIWE STSCLTYLTD
AYDHEGLWKG SDLWERTQVN NWLTLHTAAL GATGKYWLYF SAIHPEKIPA VIEKLANNIK
VQYDILERRL SEKGQKYIAL PDRPTIADVA NLPFVTEELA LKAGLRLGDW PNLQAWSEKM
LARPSVQKAL SQVQTFGHD
//
