UniProt: A0A0B4I6X1

Database: UniProt
Entry: A0A0B4I6X1_METMF

LinkDB:  A0A0B4I6X1_METMF 
Original site:  A0A0B4I6X1_METMF

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Ontology (6)   
   GO (6)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (41)   
   InterPro (22)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (50)   

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ID   A0A0B4I6X1_METMF        Unreviewed;      2688 AA.
AC   A0A0B4I6X1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KID98721.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_05377 {ECO:0000313|EMBL:KID98721.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID98721.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID98721.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID98721.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KID98721.1}.
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DR   EMBL; AZNE01000022; KID98721.1; -; Genomic_DNA.
DR   RefSeq; XP_014577715.1; XM_014722229.1.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000031176; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031176};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          18..443
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2598..2675
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          508..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1710..1733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID98721.1"
SQ   SEQUENCE   2688 AA;  291626 MW;  A647C0AE7A0A76C8 CRC64;
     MSGRPSSHAS SGTDGDGLMP IAVVGMSCRL SGIATNPEGL WQMLARGLTG WSSNGSSRFQ
     MNSFWHPQSD LNGSFNARGF HLIKQDPALF DHLFFGVTSI EARAIDPQQR MLLEVAYEAF
     EAAGITMQSL KGSDTGVYCA VSHHDYDKIL GRDPELSPGY RFTGTGPALV SNRISYVLDL
     HGPSITLDTA CSGGLVAVHE ACKAIRAGDV PQALVGGTNL ILDPDQVNMI SSMDFLSPHG
     RCYAFDSRAD GFGRGEGVAA VVLKRLDMAL GDGDPIRAVI RGSNVCSDGR TPGVTMPSSD
     IQRRMIQRAY RQAGLDPRDT TYVEAHGTGT KAGDKAEATA LRETFCKARQ KGNRLFVGSV
     KGNVGHTESV AGLTGLIKTV LMLEKKMIPP NATFVKPNSD IPLESWGMEV PKRMLKWPDN
     AARRASVNSF GYGGTNAHVI LDAADDYLDN MKHMCPPVDA RAYCEGKVDG DSAREVAKVT
     ETSSLSMTMT VSDPTGAEPT THVVHGHSTL QHRGSGSPKA SSTNATTRPR LFPLSHNQEG
     GVAKLAANFK RFILDKLPDT NESLDSLAFT LSDRRSMHRF RWCVAASSRD ELVDGLERIV
     EGADRALQQA EERRRICFAF TGQGAQWAGM GRELLAAYPE FAKSMERSEK YLAHLGADWQ
     LLAELDKPLE TSRINEAALS QPCCTAIQIG LVDLLETWGI RPALVCGHSS GEIAAAYAAG
     IVTAQDCLKV AYFRGHWVKR LKEQNPTLSG GMLAVGLSVG EAQEVCLDNN DATRGNKVVV
     ACVNSPASIT LSGDEAALSS IQETLAARGV FNRKLAVDVA YHSHHMNMIL EEYVHAIQDI
     KPLHRGQHVQ MVSSVTGKAV VRGEELNAAY WGANLTSPVL FADALAEIIF DNEKRGNSLA
     VVEVGPHSAL QGPVKQTIKA SRTAASISYH SVLSRNQDAS RTAVALAASL FVKGGVTVVD
     FGRVNDPRGD AKRNVLTNLP TYNWHHNTTH WVESRRSAQY RHRKFPKHDL VGVPSSDSIP
     SEPTWRNYIR LKELPWLGGH RIGGNTIFPA AGYVTMVLEA LKQQILGGGN PWKKMRIRFR
     QVHFGRALLV ADDDSVGVET FVTIRPCTYT ARESSSSWNE FRIFSVSANG ESTEHSRGLV
     TAIISPLLAP NQDDDENNNM TDAESLAFIE QVSGKSRVVV APKQLYKELR DVGIEYSHPF
     DGQEHIRASE SASTCRIKIP DIQALMPLRH QQPHCIHPAT LDVCFQAAFS SIKVGENLRG
     TFVLGGFDDL EISSEIPSQP GKHMSVAASL RRLGHANFAS DSVISGSSAD DDGKSDVFIK
     IKGLILARTS GPSRQTSSSS SQQHLAGESL CHRLEWSLDP TCAEPHSIIK RCLLDSDVLA
     VAGRTGMCEQ YCRAVVARAL TELSPDDEAK ITGHFSQWLL WMKKSIIGTG SHQPLETSNA
     LDDDDDDDDD DDDKIKSLGI YGEVLVDMAP RLVGILRGDV DPQALLLEKR RLYRLCTRDN
     IKRCHRQLAE YVKLLRFKTP NLRILEIGAA AAAGGSVPVL EALYGNKGGV AGEARSESYT
     LACAPTAFFQ DAEKEWDTSQ ESLGWKRLDV EISPEEQGFE LGSYDLVIAA NVLHATREVN
     VALRNMRGLL RSNGKLALVE TTAPKIHDGV VFGMLPGWWL GATDGRAHSP LLDASGWRDR
     LSHCGFSGID FEMRDYDSAE DHQVSVMVSS ATSHPEPWPT RGVSSSTPES ELPVSKYPTN
     LTGSEGGGPR QTILVIISDG KEESSSSSSS LADHVADLLT SVESGVHAKK TVLAEAQVSP
     GQVAVVLLEA VDPFLATCCQ ADWGKVRHIL SDADGVLWVS CGGAVEGTNP FQSLIVGLTR
     CLRSEDQHRK VVTLDLEPNH GGSSGLETAE QIRRVYHHVF GPHGPPPPPP PPSSGLPEFE
     YAIRNNGEIL IPRLMRDGPV DEYVRDSVST YHPRHDEQGI KPGRALSLKI HEPGLLNTLY
     WADSERHARS VGAEEVRVDL QYVSLNFKDV MIAMGQLEGH TAMLLEGSGK VVEVGEALRH
     QYSVGDLVLA TDPDGVATTS VVDKCNVHPI PGKLSMQVAT ATSLAYATAL YSLRNVANLQ
     EGESILIHSG AGAVGQAAIS LAQHLKAGEI YVTVGSADKR ALMRERFNIP DDKIFSSRGL
     GFYRQILRKT NGHGGVDVIL NSLSGEALQK SCSLLAPFGR FVEIGKKDVI SNARLEMASL
     ENNATFTTVD LALLAKRKPL VHQELYRTIF ELVGQDKIKV LSPITVNPVS ELEASFRLMQ
     AGKHVGKLLL ELDPDMTISV QPPRPPTPRL KGDCSYLVVG GTGGLGRATM KHFASLGAKH
     IFTLSRSGPD SPIMRELVEE MRLAGVCVVV VKGSVTDTVA IESIKGQAGE FPIRGVVQGA
     MVLQDSRVDN MSYEQWRAAM EPKVVGTDNL HRVFGDTLDF FILLSSSAGI IGSYAQGNYS
     AGNTFQDSLA RHRASLGLPA RSIDVGSVEG EGYTANNEAA AEFVSRQGLR PYKVKEFLAT
     INEAIRNPVA SGPSAAQLIC GTRRVDPSSQ AKEAALQRPD PKFSHMWTKP HRQASAKADS
     NHHFNIQAMF ESATTADEAE KVMQVAIKKK LAYLLGLPEK DVSTNRSVVS YGVDSLIAVE
     LRNWILSQLE SHVQIFELMS PMSFAELANM VARRSRLVAT GLFGDVKV
//

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