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Database: UniProt
Entry: F9XNI1_ZYMTI
LinkDB: F9XNI1_ZYMTI
Original site: F9XNI1_ZYMTI 
ID   F9XNI1_ZYMTI            Unreviewed;      1308 AA.
AC   F9XNI1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Non-ribosomal peptide synthetase-like protein {ECO:0000313|EMBL:EGP83163.1};
GN   ORFNames=MYCGRDRAFT_77312 {ECO:0000313|EMBL:EGP83163.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP83163.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP83163.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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DR   EMBL; CM001207; EGP83163.1; -; Genomic_DNA.
DR   RefSeq; XP_003848187.1; XM_003848139.1.
DR   STRING; 336722.F9XNI1; -.
DR   EnsemblFungi; Mycgr3T77312; Mycgr3P77312; Mycgr3G77312.
DR   GeneID; 13396079; -.
DR   KEGG; ztr:MYCGRDRAFT_77312; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_002751_1_0_1; -.
DR   InParanoid; F9XNI1; -.
DR   OMA; GVWCESY; -.
DR   OrthoDB; 1949608at2759; -.
DR   Proteomes; UP000008062; Chromosome 12.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR012728; NRPS_C.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR02353; NRPS_term_dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        580..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        818..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        851..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1058..1081
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1087..1108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          493..566
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1272..1293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1308 AA;  140767 MW;  3B660C2D8836CE04 CRC64;
     MGSIRSGTAT PVGSNSRANS TVAGLTPRTL TANTSELSLP YKLSLSDDLA IYPYEEPASA
     RTLVDLLKAT ITRHPDTLAI DNGTSRLSYA ELSDSIDLKV KALREAGVVA GDRVGVRLTS
     GTLDLYVSIL GVLFAGAAYV PVDVDDPDAR ADLVWSEAGV SAVLSDNGID SKLPSRRSEG
     PENRPAIEDD AWIIFTSGST GKPKGVAVTH RSAAAFVDAE TRLFLPKAPL APGDRNITVV
     STVPTLAAMW PAEALSNIRL LILGGEACPP ELADRLARNV DAVWNTYGPT EATVVSCGAR
     IRSKQPVAIG LPLAGWRLAV VGADGNAVRW GEEGELVIGG VGMARYLDLE KDRAKFKSVP
     DFSGERGYHS GDLVRAEREG LFFVGRNDEQ IKFGGRRIEL GEIDAALLKL PGVSGAACAL
     QKTEMGTQVL VGYVVRTREP ETKDRDLLQS MLPPSLIPVI VPVDSIPVRT SGKVDRKALP
     WPLPASMMGG DSTPADGTMG RLSEQWRRVL GVSPSAESNF FELGGTSLGA AQLVSQLRKL
     CPAMSVADIY ERPTLEAMSA RLDELTGPMQ ETRQVKPVPW WTFLLQLPFL FVLLIFEGFR
     GVSILLLTKK FSNLRLPADS WAAQHNVDWA VGIVLYILFI TVPGRMLVTV LLVRPLTLGL
     SPGTYARGGL THIRLWAAER IVATGRLQNI AGTFWARLYA RMLGCRVEER VQMHALPPVT
     GLGTFSRGAV VEPEADIAGW WLDGDMLHIG SITLGQGSRV GTRAMLMPDT ILAPLADVQP
     GTCAQGMVDA PPGAIPTDLS AELPREPFFT GLRHTMTLLL LDALVVIMVL PIFGLAAAVT
     PDWGNFRQLN LGFIIMALPG TVVGLVIYAT SVVLLVRLAS LAMTPGTHSW HSRAAWAAWL
     TRVLMLDART ILFPLYASLA TPVWLRLLGA RIGHNVEIST VVPIPCLLRV HDNAFLADDV
     LVSPYELQSG GIVLGTTTIG EKTFIGNTGL VKSGTNVPER VLIGVHGTAP DEAQMSPGSS
     WLGRPPISLP RQAESCVDSK LTFNPPLRLK IARASVEVWR LLPLLFLGML TTLVSLGNLY
     MLVKHGVGWA ILASGGFVLA AALIACIITT AAKWIITPFV GAGQQNPLWS HFVWRNELSD
     TFVQSLVVPF IDKFYGTPVL SLWMRTLGAK IGRGVWLESH LLPEADLVTL GAGVSINRQS
     LLQTHLFHDR LLRLDRVCLQ AGATLGPNSM ALPGTDIGCG VTIGPKSLVM RGEHLPAGTC
     WLGNPVRPWA RDSSETSSRK ISVPSSNQSI ESDFSEKHFG KDLEKQDV
//
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