ID A0A367LQV1_9HYPO Unreviewed; 2484 AA.
AC A0A367LQV1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RCI16826.1};
GN ORFNames=L249_1723 {ECO:0000313|EMBL:RCI16826.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI16826.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI16826.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI16826.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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:RCI16826.1}.
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DR EMBL; LKCN02000001; RCI16826.1; -; Genomic_DNA.
DR STRING; 1330021.A0A367LQV1; -.
DR Proteomes; UP000253664; 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: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; cd05274; KR_FAS_SDR_x; 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; 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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 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 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.
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:UP000253664};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..425
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2399..2476
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 435..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2484 AA; 271185 MW; 02C5163F16F6A59D CRC64;
MTQQPPLSPI AIIGMGLRLP GGVSTANEFW DLLINKQDGR RRVPPDRFNI DGFHGEAAHR
QKVASQHGYF LDANIKAFDN DSFPSNAADL ERLDPQQRLL TEVAWEAMES AGQASLRGSD
TGVYVGVFGE DWHNIMHQDR QRTGNSRSIA SGDFALANWL SYALDVRGPS MTIRTACSAS
MSALHLACLA LRNGDCQSAI VAGCSIIMEP SMTLVMSEQQ VLSPTGSCKT FDASADGFAR
GEAINAILIK PLDAALKAGD PIRAVIRATA ANSDGRISSM GCPSAEAQEV MIRNAYKAAG
IDDISLTPYI ECHGTGTPVG DPIEVAALAG AFGRRGAFIG SVKPNVGHGE GASGITSIIK
AALCLENSTI PPNINFCTPS PRIPWDDYKF EVPLEPMPFP QGRPARISVN SFGIGGANAH
AIVESAAAYG IPARLTNGHS TGSPEEKRQE GDDNTSWPSV LPVSANTENS LQRRIADIKA
YIEAHAGSVD DVVYTMGVRR LHLAFRSFSI VQDGVARPPE FSSVEKAGAC KAVFIFTGQG
AQWEGMARSL MLSSPSFRRD IKEMDDGLRM LDEPPRWTLQ DLLESGVEEN DNYINEAEFA
QPLCTAIQIA LVNFLAKCGV TPYAVIGHSS GEIAAAHAAG ALTVSEAIMC AYLRGQTTRL
KTRDGLMAAV GLGRDATVPY LVDGAIIACE NSPKSVTISG DAEAVRQTLE EIKAKEPDTA
SRMLHVNVAY HSHHMREVGA VYQERLSPCM KQIREPRIPF FSTVYGKAVD SETRLGAEYW
RKNLESPVLF HGAVSNLLTG LPDVATVVEI GPHSALQGPL RQIFQERTSK KPPSYVATLI
RSKECVESIL GTVGQLYARG YDIDFSFLNP KASTLVDLPT YPWDHGSDFW KESRVSKAWR
MKENPHHELL GDRCPESSTL EPVWRNVLHH SDVPWLADHK VGTNVVFPCT GHVGIMGEAV
RQALGGEKGY VIRNLTVKAA LVFPETDPIE IMTTMRPSRL TDLTNSSSWH EISISTLNGE
TWTENCTGQA MARIEEATST NDGTGLDPGG SYSRQMAKGY FYDHMRHMGL RYGPRFQGLT
DISTDPKRSV AMASLKDSSA EKETPYLVHP ATLDCCLQLP VVAGCRGVAR SIDTLMLPVS
IRRIVIHPGG ETDLEASAVV DLDASDVRVV VVSRRSRRPV VEMDGIRGIP FDTGDAAGGR
NGLMSACLEW LPDIDCLSAV ELTMERRDNK REPRKIGEKL TSLGILQTLD VIESLDVSPS
GHLAKYIVWL EEEKQAMIRG DRPLAFPEEQ EWALMKPSAL KDLAKTMLVE LEATEERTVI
NVGHMIYDMS QQETIEPIFR GTNPVELIVA DDRINDFYTF QCSASAAEFF RLCGHAKPTM
KILEIGAGTG STTKDVLDSL VSEHGVRLYE QYVYTDISPW FFTAARERFK DRNNIVYKVL
DITKSPEEQG FELESFDVVV ASNVLHATPS LHETLRNVRS LLKSDGRFYL TELVKPLSWR
FINFITGRLP GWWVGEADGR ADVPFVSVER WDAELRAAGF SGVDASVLDD DEPYCTCAHM
TSRAVAAAAA AKPETVVMLY RHEKNEFACG LADIWARGGI DVRWAQLGNH GEDLVGVEHV
ISAVDLEGPF FHDLAETDYQ AFMALLKKLQ RGVLWLTRPA QIACIDPRYG LVNGVARTVR
VELSLDFWTA ELQGLDETTT AAVLSIARKF FSRPSLSRGM DTEYAVHDGI VRVARCHWSS
VAGALEPAKD GGCARQLVVG QYGVLDSLTW IRAEEQTVGE LDVEVDIRCV GLNFLDIMVA
MGLVPKPKDS LGAEAVGVVS RVGSAVKHVA VGDRVWAVRL GVFATRKVVP GVFVYRMPDG
FTFEEAVTMP IVYATVIYTL MTLGGLRRGQ SVLIHSAVGG VGQAAVHICK MLGAEIYATV
GSETKVDYLI KNHGIPRDRI FNSRNDSFRD DLTQATDGKG VDIVLNSLSG DLLHASWECV
AKGGKMMEIG KRDILERGRL ALNMFQDNRT FYGFDLVALL RDRPEVFPEL IGQFLGFIAE
GHIKPVQPIH QFSAQNVADA VRFMRSGDHI GKIVITIPED PTEISCTKLA YTGGLLSETS
SYLLVGGLGG LGKGVTRWLV EKGARNFCFL SRSARKSEGD QVFFRELEEQ GCRVAAVAGS
VANMAEVQRA VGAAPTPIAG VLQLSMVLRD NSISQLGFDD WRAAQQPKVQ GTWNLHKALV
HTKLDFFILA SSLSGTFGQP GQVNYASANS FLDSFVQYRH GLGLPCSVVD LGAVEGIGYL
SDKQSKLNVY KSFGADLLHE QNIMDAIQLA MKRSLPPNTM GLTSPRGPLA NKSQILVGLT
SSKPLNDPTN RIPFKHDARL GLLNNMVTAS ETTLQSRDQG ISQLINKFEA NPGLLSDPDA
ITQVSHEIGR ILFRLLLLPE DTLDTSMSLA SIGIDSLASI EIRNWWRRTL GVDKSVLEIM
NAGTIEGLGK LAISSLKKKH EGDD
//
