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
//