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Database: UniProt
Entry: A0A0D9NQA1_METAN
LinkDB: A0A0D9NQA1_METAN
Original site: A0A0D9NQA1_METAN 
ID   A0A0D9NQA1_METAN        Unreviewed;      2519 AA.
AC   A0A0D9NQA1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJK76129.1};
GN   ORFNames=H634G_08535 {ECO:0000313|EMBL:KJK76129.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK76129.1, 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; KE384747; KJK76129.1; -; Genomic_DNA.
DR   STRING; 1291518.A0A0D9NQA1; -.
DR   Proteomes; UP000054544; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; 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; cd02440; AdoMet_MTases; 1.
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; 1.
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; 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; IPR013217; Methyltransf_12.
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; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
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; 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; PF08242; Methyltransf_12; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 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.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..426
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2438..2515
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2412..2437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2415..2436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2519 AA;  274113 MW;  7BEF8F4854BB486F CRC64;
     MDDSSAIAIV GHAYRAPGVG RKGLWDFLAE AKCAFSRVPE NRFDQDAFHD PDSQKQGCFA
     TKGGHFLPED VYAFDAPFFN LRPEEARAVD PHHRLLLECT FEAAESAGIS LTDLAGGNIG
     VFTAMSSSDF LEHSLLDLPT STMWTAVGIS GTMFANRLSY FFDLKGPSIA LDAACASSTY
     ATHLACKSLL RGECTAAVVG AASLLLGPEY WVTLDTMGAL SVEGKSFSYD SKASGFGRGE
     GAACFILKRL GDALEAGDPI HSVIRNSACN HSGRSDGITM PSGAAQIQLL RQVHEEIGLD
     PAETAVVEGH GTGTKVGDPI EAGAFAEALA QKRTPGNPLY IGSIKSNFGH LENASGAIAM
     TKATLMLQHG YVLPTAHFEE MNPNIQGKEK LMVAKTTLPW PKDAVKRVCI TNFGFGGSNS
     ALILDEAPKG TGSRHKLTNG VNGTNSNGMS NSICNGNGFQ RHDRAKKLFV LSAKSEKSLA
     SYLASFKEYL QTAPEDAAFA HDLSFTLGQH RTHHHWRTAA VASSASELQT QLSGIKLGKT
     KDQVISFVFT GQGAQHAQMA SELRQYHVFS TAMDEAEYYL RKLGATWSLT EELDKQASES
     RVNDAEISQP ACTAVQIALL ALLKSFAVEP SIVTGHSSGE IAAAYSAGML SFETAMAVAF
     FRGRAAVELA QKSTHKGAMV ALGVGYKDAM ALVQDNTAGY AGIAAINSPQ SVTVSGDESA
     IDNIFKKAEE SGMFARKLKV EVAYHSRHME QVAASYRASI EPFFTKAPDS CHKSGVRFIS
     SVTGRAADSV DASYWIDNLL KPVRFADSIS QIFSSGEGDT AVPGPYKTPT IVVEIGPHSA
     LRNPIKQTLS QLSQRADSNN MQFTYLPSLV RGTGADETML QLAGSLFSLG LPVDFTAINR
     TNRKNAHVLT DLPAYSWDRS TRYVNEGRAV QKRLHPGLPY DPLIGWKNPS SEGHDASFRQ
     VFTLDQMPWI RDHKVGGEVI MPMTGFMSMA IEAARKLSPT VPGSIVVSEF YVKRSLVIGE
     DEHIDMTVKL QPVVTGTDGI SSSVWRFDIM SWRKEDGWVD HCHGLVEAQE EDMDLESRTM
     KTAVPLVHSH DMKESSLFDE IYASGPREGT VYGPAFKSTI RYWEAPGWTV MESKLRELDT
     ARSCSPSGSP FSADPPTLDG FLQGFLPLQD AGRKCRALMP TYVGRLRVSN HIPVDHDKLR
     LFVVSRLMSH DVKTETLNIT VAAFAQLPHS LLPIAEWESV TFRSISSAHA SDALSRLPAS
     FYHELLPALD FASDADWPKF ITAAPADEDG LRKRVQHERV ALEYMKRAVD GTSDLDYSDL
     PEHLCKFMSW AKRCVAREEH RLMKEPLPDL SRIAKADAGG ELLCAVGEQM VPILRGQVQT
     LEIMLRDGLL ARNYEQDTSN MRAAVTLAKC ARHLSDINPE LRILEIGGGT GSATLPVLEE
     LWGDATGLAP FRDYTFTDIS AGFFENARVK LATWNQRIIY KKLDITQDPA TQGFAPGAYD
     LVIASNVLHA TADMTVTIGN VRSLLKPNGK VLLLEATKHS PVTLPFSLLP GWWYAVDEYR
     NLEEGPLLSD DGWQRLLHAQ GFSGVDVCIK DYEDPCSHLM SVMCTTKVGR PETCNGSLRS
     ITVCGLFMDE EELDFAQLVA SQVSEATGRH CKIQTFLDID AEDDDLCIFI DSPANSLLAD
     LSQETFEMLQ NILLETRGLL WVVLENAGPE SLSIQGIMQC LRMEMEPKNL MCFKNAPRSL
     VGADAIAKLA RRLEDAELAA SSDHDFVWQD GMIKVPRLRQ SVEAKEIFGA ETGVYVRKKQ
     NIWEDKASFE ITMDTAGAPE SLYFRQTDAL ARPLGDGEVL VKVEAAGLSS RDLQLVLGAV
     PWAPPGLEGV GVVCKVGSGV SSLGPGDRVY YGLHGGCLAT HVRMPAWQAN KVPDGWSNAD
     AASISIAYQV AYLALCHHAR LRKGETVLVH AASGAVGQAC IVLAQNMGAR VFATAGTREK
     RVFLRDTYSI PESCLFSSRT AEFRNGILCE TDGKGVDVVV NSLSGSLLQQ TWALMADLGR
     FVELGAKDSR MNSSLAMRPF DRNVSFSGID LCAYAEKRPD EVRQMAAELD GMLRRGVIKP
     IRSVATMPVS DLAAAMRKLQ SGQHMGKIVI SMGRHDDVVA ECHPELGPTH GTLLRPDATY
     VITGGTGGIG LFLAPWMVEH GARNIVLLGR SGDTRPEVRK VLQRYKDTDV EIRAIACHVA
     YREQLEAALN SITDLPPVRG VVHGALFLKD AMFMNATYQD WQDIRGPRVQ AAWHLDEMLP
     NLDFFIMLSS MLGSCGNVGQ AIYAGTATFF DGFVDYRRTR GLPATSIALP IVLDVGYVAD
     RNRTEELKES LGACLSRPHL EVLMRGAIIG SSSGLNFQGK AMSFHLETGA GTDGVAWQCY
     NARDFRRIAR TEQAGQAAGS DTQGKRRSQG LGDASSEGYS ENLLGALMDK VSSITMIDRD
     EVEADAPLAN YSLDSLVSVE LRNWIRRETG VDLPLAKLVR SANLRAVAAY IVPGVKTGA
//
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