ID A0A1B8EKE7_9PEZI Unreviewed; 2542 AA.
AC A0A1B8EKE7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Type I Iterative Polyketide synthase (PKS) {ECO:0000313|EMBL:OBT71813.1};
GN ORFNames=VF21_09372 {ECO:0000313|EMBL:OBT71813.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT71813.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT71813.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT71813.1,
RC ECO:0000313|Proteomes:UP000092096};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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DR EMBL; KV458907; OBT71813.1; -; Genomic_DNA.
DR STRING; 1622149.A0A1B8EKE7; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000092096; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 3.40.47.10; -; 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; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
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; IPR006162; Ppantetheine_attach_site.
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; PF00107; ADH_zinc_N; 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000092096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 41..466
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2456..2533
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2542 AA; 275207 MW; 5072745741A95227 CRC64;
MSPSSVPNGT FGPSLRNGST VHHAEEASSF NHNHSSSASP PVPIAIVGMS CRFSGDVNSP
EKLWELCAAG KDGWSPIPEA RFDIKSLYHP DKEKQGRTHV VGGYFLNEDV ALFDAAFFNF
SGEVASSTDP QIRLLLEAVY EATEDAGMPI EKLAGSNTSV FTGCFNKDYH ELQTKDPEVL
PHSFMAGTGT AMHSNRISHF YDLQGPSMSI DTGCSAGLVA LHQGCQSIRC GESNISVVGA
ASTLLSPDSF IAASSLGALG DDGRCYAWDT RAQGFGRGEG VAALILKPLD AALKDGDHVH
AVIRESGVNQ DGKTTTISSP SADAQIKLIQ ECYKRAGLDL SDTGYVEAHM TGTPAGDPIE
AAALASTFGK SRATHDPIIV GSVKTNVGHT EPVSGLAAVI KAAFVLKNGL IPPNLNYEKT
NPSIHLKEWR LQVPTALTPW PQDKALRASI NNFGYGGTNA HIIMEPAPKT HAKLNGALPS
ENGTQDSDKS HIYIFSAKDS AGAQAMASNF AAHVRHSITR GQALSPGGLA YTMAERRSLL
PWMVAVRARS LAELADRLEA PGCKALHASS RRLRLGFVFN GQGAQWHAMG RELIATYPVF
SMGIQEAGKV LKEYGAAWSL YDELMRDEQT TRVSDVNISQ PISVAVQLCV VDLLKSWGII
PSAVTSHSSG EMAAAYTVGA LSFKQALGVA YFRGELALKN VSSLAGGMLA AAISSETAEQ
YIANIPSGGV VVACINSPNS TTLSGDLAAI DEVESLLKKD GLFARKLKVS MAYHSSHMSH
MAQEYAERLR DILPGDDRWT GALFTSPVTG GIVTSPKAFT PEHWVRNLTS PVLFSQAFES
MCFSPTASSI QGSNVDIIVE IGAHSTLAGP IRQILESRNV KMPYTSCLKR SVNAVETMQD
LVCDLLGRGY PVALSSVNSP LGEKQTFPRI SKEMKNKRFP PHELLGALLA GTNGLTPTWR
NFIRLSDIEW LRDHQVDSKV VFPGAGYVAM AIEAVRLLVD PSEKTIHGYR LRDIDIVNAL
VIPESSAGVE TQLCLRRCSE KELDHKGWYE FELCSLGISG SWAENCRGYI TAETGDAIKA
ATTYEAERPC ENSYLPAGAA VTNIITEELF ASLRKMGIYH GPNFQNLIDS HAAGDRAKTN
LAIASVATET HDYVLHPTTL DSILQATYSS LPKDMGRDSM ALPRSIRTLF VPRSLRRQGG
EKLQVFSKLV RSDKRGFTSN VMVTNRDSDD TEPFLEMQDF FGQAVPRETD DPSPVAGICS
KSSWELDILH NVPTSVKNSM KIALDEDEAE LERKLVRVSY HFIHDTVNEF EGEDTESWPW
HHKRFYEWMK SVVALGKRGE LGSGSQKWSQ ASKGLKTMLA DELNAGDVSG QLTVRVGQKL
TSILRGDVTP LELMMEGNLL NQFYMNHQRF KTRSAKHLAK IAELYAVKQP GANVLEIGGG
TGGATGTVLD AFAARGDGSG TLLGHYTFTD ISPGFFEAAK HKLATWSSMM EFKKLDIEAD
PIEQSFTAGS YDLIVASMVL HATKNLHKAL SHVRKLLKPG GKLLMAETTR DRLDAQLIFG
TLPGWWLAEE PDRQMSPNAP LETWDRVLRE TGFTGVEFNI GDYSEEELES ASIILSSATE
TVATVTGPVT IVYEKTTTMV QPWLSQLAEE IRVQTGISPS IESLDEVQCQ DKICIFVAEM
EDPFVTGMDE EAFEKLRSLL LNCRGVLWLS CGGIIDCGQP SFAPTQGLLR SLRHGESSKG
FIHLDFERGP DGPWTSDNIK HIVLVLQRSF DGSIEMSSID WEYAVKDSML HVPRLFPDKT
RDAVASDNEV DPAPQMQPFH QQNRPLVWET PSSGIGGLDP YFVDKIDIVE DVPSGKVEIE
SKAFGLNFRE VMVALGQLDE PLVGYECAGI VTKLGPNTEQ SGLRVGDRVC ALCNGSRISS
KGQVSWLGVA KIPDDMSWEQ AASIPVAYVT AYSSLISIAR LQKGESVLIH AATGGTGQAA
VVLAQHIGAK VFATCSTAAK RDLLIEKYNI DPEHIFSSRD SSFGPGVMAK TNGRGVDVVL
NSLSGPLLKA TWDCIARFGR FVDIAKVDIE AARRLDTTPF RRCASYETLL ACLRICKERG
TQPIWPIIPY SISDMEKALR QMQGEAHMGK LVLVPGNEDL VKVVTRPRPF SLCNPNATYL
IVGGVTGICR AIAEWMMTEK GAQNLLIISR HATSHKYAAQ LKATAKDTGC NLQIRDCDAS
DELSLVELLA EASRSMPPVR GVVNGAMVLD DTILERMTFE QWQRGVKPKI GSSANLHKHL
PNVSFFIMLS SLTGVVGQVS QANYAAGNTY QDALARHRTK LGLSATVLDL GPVLGAGFVA
EKIAAGDNKM RARLESAGFG AVDIKGVLRG VLRLVGAAIS DSPRCVSLAD SQVIVGLADF
DAFPAGAIVR QDRRFSTLQL ASQRGRSSVA VASTSDTNSS AALVQLLSTA STTTEEATAL
LTEAITRKLA DIFNISAAEI NSELPMSRYG VDSLVAVELR NWLNGVVKAK ITVFEVLQSA
SLAEFGALVV VRSDLVSSKV ST
//
