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Database: UniProt
Entry: A0A0D9NWN0_METAN
LinkDB: A0A0D9NWN0_METAN
Original site: A0A0D9NWN0_METAN 
ID   A0A0D9NWN0_METAN        Unreviewed;      2410 AA.
AC   A0A0D9NWN0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJK77000.1};
GN   ORFNames=H634G_08042 {ECO:0000313|EMBL:KJK77000.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK77000.1, ECO:0000313|Proteomes:UP000054544};
RN   [1] {ECO:0000313|Proteomes:UP000054544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX   PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA   Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA   Ash G.J.;
RT   "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT   comparative genomics of Metarhizium species.";
RL   BMC Genomics 15:660-660(2014).
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DR   EMBL; KE384742; KJK77000.1; -; Genomic_DNA.
DR   STRING; 1291518.A0A0D9NWN0; -.
DR   Proteomes; UP000054544; 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; 3.40.47.10; -; 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; 3.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
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; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 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; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 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:UP000054544};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          64..492
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2327..2408
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2410 AA;  261696 MW;  1B66F66CD98B7364 CRC64;
     MTQVTDIHPS LPNGINGHMG HGSHNGSYPS NNSNHTNGTN GHGLLDAGAT KSNGHGPRAD
     PNVQTPVAIV SMACRLPDQC HNPQQFWQFL LDGKIAINTP PGTRYELATH YDGSLKSQTM
     ASPGGMFLQG VDPADIDAKF FRLSGVEATS MDPQQRQLLE VVYEGLENAG VTMEQLDGAR
     VGCFVSSFAS DYGDMQARDP ENRASATVVG VGRTMLSNRI SHSFNLKGPS MTIDTACSGT
     LIGLDLAMKY LHTGEIESAV VAGANLYCSP EHVMDHYMGA NGAASLTGKC HTFDAKADGY
     IKAEAVNMIY VKRLEDAIRD KDPIRAVVRG TATNSDGWTA GIASPNPVAQ SAAIRQAYKN
     AGIRDLSKTS YVEFHGTGTR AGDSIEASGI ADVFAEFQSP DRPLRIGSVK SNIGHSEPAA
     GLSGLIKTVL SLEHDVIPGN PTFIDPSPKI DFEKLRIWTS RTATPWPALP LRRASVNSFG
     YGGSNAHAIV DEAKGFPRHH VSSYDDQSRR SLVEEEQVDQ RQRIMVLSAN SEKSLQDQFS
     ALDKHLSNPG VVVKQRDLAY TLSERRSRHY YRGFVLASDH YLDAEAFETD RMRDEPLSIA
     FIFTGQGAQW PEMGRELLAS FPVAAKTVRH LDDVLQSSYG APAWTLYDEL TSPRSADHMR
     LPEMSQPLVT ALQLAILSIF DAAGVSCRAV AGHSSGEIAA AVAAGLLTPE QAIKIAFYRG
     KATSAVKHGS PLGMMAVGMG PDAALEYLDG SSVQIACFNS PQSITVSGLR SELEPMEQRI
     KDDGHFARLL QVDSAYHSRY MNAAAGAYRE LLDKHVEWET RPAPKGKIMF SSTTNKMLAE
     SPGADYWVKN MLSPVLFSQA VTSMVRAESS DINYLVEIGP NNALSGPVNQ IQKAAATSLD
     YSSAWKRGAG AMQTLLECAG KLFNAGSAMS LSPFNDDGLP VPPTFVLDLP NYQWDHSTKY
     WHESESSSDW RFRKFVHHDL LGSKILGTPW TRPIWKNFLR VSDVTWLKDH TLGDSIIFPA
     AGYMAMAIEA MYQKSKALGA IADDATVVDQ TYKLRNVAFP RMLTLNEHAG TKLVLSLEPC
     SSTKETWHEF TISSIPKDGN GALEEHCTGL VSVGHDVRHV AATADDVSPL KFGVPGSVWY
     KAMRDVGYFF GPAFQPCESI EAKADARNCR AVIKLETPSS RYPQSRYAMH PTAIDGCLQI
     ATVALNRGHR SALDTMMPPR LIDNLVIFPQ PDHVERGIVA SEAMWSGVGR PDDNKRFYSD
     IRTYAQGSNE ALFHLQGLRY HSIGASADAP HVFTQVQWAE DAGFLTPEQL STVMASDEEA
     PPMAAVAKAV SIMAHKKPTS KILEVVYRDG EAAVHSLWLD GLRQLSGPIA EGCAYALSAP
     AHTTSLALRE KYSTEANVTH VVHESDCITA GVDGDDEDDK IDVVILRAPA ITPDLIKAVE
     GARQAIADGG YLIVVKDDVT DGKTDQANEV VEASVPGFNA LKLSGNCVSD VIFFGIASDS
     ASQVQDSADK TVNLVRFTTS NHSTAAARGA IAKQGWQIVE KGLSLGGIED KSTVIVLDEM
     FSPVLADLQD EQFDALRGLL ERECKILWVT RGSQMTVRTP ELGLMFGASR SLKAEYPQSV
     FVCLDVEAND SHASFGAIDR VLKHLGTLTD VSKVDSEFVE RQGVLYISRV ISDAAVNKAE
     HDSQHGADKV NGIIGGHQST IRLISDRTGT LDTLTYTEIP EVPALKDDEV EIEVRAAGMN
     FKDLANAMGF VPANERLFGL ECTGVVTEVG KDVSTVKPGD RVLMVRRDGG CFGNKVRNRW
     HAVYLLEDDM SFEEGTTFGI AVHTAVYGLV TMANIQKGHS VLIHSASGGV GLAAIDLCKY
     IGAEIYVTVG TEAKRDFLAQ NYGIPRDRMF SSRSVSFGPE LMRATGGRGV DFCLNSLTGD
     LLHESWRCIA ENGSLIEIGK KDMLDRNTLS MEPFDRNCSY RPLDLSRPSI TDETTRKTGE
     YIMDLIAKKH IKPLHICKVF PFEQTAEAFR FMQRGKQIGK VVISYEKART TEIEYRPAAP
     QLRLRPDGSY LIAGGFKGLC GSLAVYLARS GAKNIVVISR SGYDDEKSQK TVYDCNSLGC
     SVDLVTGDIT KLDDVRRAFA SASKPVVGVI QGAMVLRDRM FTTMTPGEFR EPISPKVDGT
     WNLHKASLEQ PTPLDFFTML SSVSGLLGQL GQSNYAAGNC FLDSFAAYRI QQGLPANAIN
     LGPVEEVGYL KDKDMLSRIF ESRGWKPINE ALLHRIIRSS ILLQTNTINP AQAGQLITAI
     TPGNPPFEAV HRFSSLRPVA GTLAGSGGTA SSASSKLAIL KSAGKGDVAR ETLLAAATEL
     LNTVLMRSLG IDESIEPMRL LANYGVDSLV AVELRNWLRA ELNVEFSALE IVGSRTLTTL
     SESILKKLVH
//
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