ID A0A369HC86_9HYPO Unreviewed; 2419 AA.
AC A0A369HC86;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RDA93594.1};
GN ORFNames=CP533_6132 {ECO:0000313|EMBL:RDA93594.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA93594.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA93594.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA93594.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA93594.1}.
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DR EMBL; PDHQ01000024; RDA93594.1; -; Genomic_DNA.
DR STRING; 2039874.A0A369HC86; -.
DR Proteomes; UP000253071; 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 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; IPR029063; SAM-dependent_MTases_sf.
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; 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; 3.
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:UP000253071};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 25..453
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2329..2406
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2419 AA; 263754 MW; 8C52F9D94607700B CRC64;
MALNGTHVLA HSMSSQPQPL KRYVQEPIAV VGMACRLPGN SNSPHALWEF LEGGGIADNK
PPASRFRLDT HYGDPLKPGF MRTPGGMFLE SVDLHKFDAA FFGIAKIEAI AMDPQQRQML
EVTYECLENA GITLERLDGE AVGCFVGSFL VDFVDMQSRD PLDRVPSTIV GTSRAMMSNR
ISHFLNIHGP SMTFDTGCSG TLVGLDVACR YLSSGEISGA LVAGANLYLS PEHSQDNGVM
ETAWSLSGRC HTFDDKADGY VKAEAINCVM LKRLSDAQRD GDPIRAIIRG TATNSDGKTP
GITNPNWPAQ ADATLAAYAN AGIDDLSATG YVEMHGTGTQ IGDAAEVKSV ASVFAPSRRH
DAPLAIGSIK SNIGHSEPAA GLSGLIKAIL ALEKGRIPGN PTFVKPNPDI DFVGCRVRPS
RNAIPWPAQA GLRRASINSF GFGGSNAHVI VDEVPKEMQN HTSSFAKDSG KDSEKPVKAA
RPHVLVFSAN DDGSVKSFAE SLREHLLDPR VNVDLPTLAN TLSERRTRHF HRGYLVTKDL
ALDTGSIVHG KKKLGRPRIG FIFTGQGAQW PEMGRSLIDN FPEARATIER LDRVLQGLLH
PPSWSLLNEL YEARSPEKLG EAEFSQPLTT ALQIAILTVF RTWGVTARSV VGHSSGEIAA
AHAAGLLSED NAIKAAYYRG YAAKASRGAQ PCKMGMMAVG LGGQEARDYI AKAALAKPSA
ITVACYNSPT SVTLSGTLVD LEALREELVA DKVMARMLRV DMAYHSPFMA AAVDENRRCL
LAEAFSAFQP HGDNEVKMFS SVNGNLINCL TDIDYWSKNL LQPVLFDQAL YEMLSDKENA
PDFLIEIGPS NAMAGPTAQI KKRLPRGGSD VQYCAAMTRG QGAERAIFDV SGRLFLAGHG
IDLTVVNGTG DVRKLLTDLP NYSWNHDTEY WYENEASREW RDKPFAEHDL LGSKVLGSAW
QAPVFKKTLR LEDLPWLRDH CLGTDIVFPA AGYMCMAVEA MMQTDAMLRL ELTTELRNDQ
QIRLRNVSFD RALILEEGKT KRVMLTLAPH MGQKNSWSHW VVRSRGESSW IDHCKGQIRV
EEDSASVAKP FDISPLQHPK PGSLWHEALS DVGYTFGKSF QKLTMVEATS GSRKSRAMVD
ILPPPSKYTQ SRYLMHPTAL DGCLQSCFPG LWRGIRSSVN ALLVPARIDD MVVRAGVESA
GRAISVSESV FVGIGRVDLA KDYSSIAKIY DSETGDLMLK MDGLRYHSVD FHDTPYAAHR
YCRLFWKPDV TFSPQACAAG DSRGWDKVQD IAELIAHKKP NARVVEASLL TGDSASVWLE
GISTESKARN AFGSYSFVNS DAEAVDTARA KYGATSQTAF QLSDISKPTG NVPEGSLQST
DLVILHLPAQ MEEADMMQVL EKTGKMLRAD GHVLVLEQAG AWDTAADDRP TGGGEPMTDE
RISDWNRILK VNGWDTLYTL DCPESLSLHR AHLATPTTPA AEPAGKSLDV LHLAEPGSTC
RKIVKALVDL DWDVREHHMS QSLAEIRADS IVLVITEVEA PQLPKMGVEQ WAVCRELLQM
RNRIVWVSRS AQGTLANPDG AMIYGLCRTV RREDPSMGIT NLDVEDPNND AAVPCIDLLL
RSIQRQASIK EADTEYLERG GVLHVSRLLS DDAINAADKG ETRVKMRLHE ASCTVRLIAD
RVASLDSMQY AQVDAQELPL ADNEVEVELF ASGLNFKDVL VAMGVVPGNP VLLGSDGAGT
IRRTGANLKT HHDVGERVAV IEMGSCANRI IVTSERAMAI PDWLTYEDAA TLPSAYITAL
YSLCYLSNVK RGHRVLIHSA TGGLGMASIQ ICQAVGAEVY ATVGQDAKKQ FLMEKFAIPE
DHIFHSHDAE FEPRIMEMTN GRGVDIILNT LTDDLLEASW RCVAEGGTMV ELGKKDLLDR
NTLAMEPFAR GASFRCFDLS LAYNTEPFIV DTMKKMMSMV TSGTLKPIDP VTLFPYSDVL
SAFRLMRSPN HMGKVVISNK GLDSQDPIVE VRSAPRKLRL RNDVSYLLIG GLKGLCGSLA
VDMARHGARY LVAMGRSGFD DARSQAVLKD LVAEGCHADL IRGDVSSLED VRRAFREATK
PIGGVIHGAM VLRPAPFDSI SHDDYLAVIQ PKVAGTWNLH NVALEMRREL DFFTMLSSLI
GFAGHNAMAN YAAANAFLDG FAYYRRGLGL KANSVNLGAI EGVGYLGTNA EKMTTLDRSF
AMHINEPIFL KSVHFSILQQ EDEPVNAASC AQLITSFMVP IPASSTFPHM DARFQTLDFG
HGERASNGEK YASGLEPLED SDMQALLSNI RSGASVDGVD DATRMGTEKP AAAVVVNFIN
RHLTKTLGLD QPMEPARPLP SYGIDSLVAL EMRNWCRGRL GVVLTTLEIS NATSLSALAD
KILAKLRQQS AGEKTGKQA
//
