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Database: UniProt
Entry: A0A094EHA1_9PEZI
LinkDB: A0A094EHA1_9PEZI
Original site: A0A094EHA1_9PEZI 
ID   A0A094EHA1_9PEZI        Unreviewed;      3153 AA.
AC   A0A094EHA1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY77894.1};
GN   ORFNames=V498_09220 {ECO:0000313|EMBL:KFY77894.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY77894.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY77894.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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:KFY77894.1}.
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DR   EMBL; JPKA01003987; KFY77894.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000022_31_2_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1901362; P:organic cyclic compound 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; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 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; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
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; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF22; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF00755; Carn_acyltransf; 2.
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; SSF52777; CoA-dependent acyltransferases; 2.
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; PS00440; ACYLTRANSF_C_2; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..440
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2469..2546
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2550..2576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2853
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   3153 AA;  347705 MW;  762E744F8327A188 CRC64;
     MQVALATMHP NTQQPLSIAI IGMGCRYPAG SNSPEELWNV VAEGRSGWTE VPQDRFNHQA
     FYHPDPEIPG AINQKGGHFI NQNIADFDAG FFGIAQLEAE TLDPQQRVVL ETSWEAVENA
     GIPMHHFKGS DTGIFVAMFG HDFEQITHKD PVSFSKYHNL GVARPLLANR VSYVFDLQGP
     SVMIDTACSG SLVAVSSACQ SLRSGETYMA LAGGVGLIFS PDQMALMSMT GLFNDEGRSY
     TFDDRGNGYG RGEGVGMVAL KRLDDALRDG DNIRAVIRSS GINSDGRTNG IMLPSQISQE
     RLARNLFRNL PFTPADVQYA EAHGTGTKAG DDVEMKTIRN VFCQGRDSQN PIFIGATKPN
     IGHSEAASGT AGLIKTVMAM EKGLIPPNIL LKNFKPGLEP DQFVKVARSL TPWPSTTSSR
     KAVVNSFGFG GTNAMVVLES GNIRSGKYGH VVSMSPRLHN GAAGVNGIVN GHLNGDMNGL
     HNDDDVEKDK KAPRLFTISA RSEHSLRHAA DDLRVYLGRQ RDIRLDDLSY TLTTRRSKFQ
     WRSSIIADDV NSLIQSLEAE DLARIKAPNQ VANVFIFTGQ GAQSARMGYH LLSAEGNEFS
     RSISRSEQLL KDLGAQWSLV KELSRDENSS RLNDSKYGQP ASTAVQLALV DLLKGWNAQP
     VAVIGHSSGE IAAAYAAGAI SQSAAMSASY HRSFLANLAK QRTTQPGTMM AVGLGQSDAE
     RYIGKLDTCG LTVACVNSPS STTISGDASA ISDLKSVLDA DGVFARQLNV DTAYHSHYMK
     LVSPDYLDRL EGLEAGSVDP SIRYFSSVTG KEKLEGFGSS YWVDNLVSPV LFSAALQRLC
     QEVSHTPLNL IEIGPHTALS GPVRQTLASL QADGLYTYIP TLVRGESGIE SLMNTGSILF
     RSGSDLDIGA VASLGISSSS PPAILRDLPT YHWNYTTTFW TESRLSREHR QRKHSHHDLL
     GSRVVTSPDS QPSWRILLNT ESLPWLKDHV VDNFIVFPAA GYMTMAIQAM RQLDQDRRPD
     LKPNGYRMKN ISFKKTLTLP KDYKSVETII TFQCSDSNKF STFTVASMSD QGKWQEHCDG
     SISAVFEPDL DEVEQGREAE FGRKSQAARL ESAREACTKI ISHEDLYSQM AATGNQYGPT
     FAINNEARIS SFQSLNSLII PDIAASMPGK FIETHVIHPT TLDAVIQACL PVFQQYSIRG
     AVMPTLIGDM FISTDIANQP GKQFEAVCDL SDTFAHSTKM GTAVFQSDET GMPRCFLTMD
     NVEIRVVGES QTSSQKPRND NIFKLEWGLD SSSVTAEILE SVVIPLQSDE ASISQAEKVD
     LGSVACARYI DWAVRQMHDR GLAVKGDHRA NWWRLLEEFF NSETGQALIQ RSPKTKDELD
     QLTSKLGVEG EAIARIGPEL VPLLTGQTDP LTHFLKDDLL FRVYHSDEGA RPNRYMADYA
     KILTFQRRNL RILEIGAGTG GTTLQVLQAC SPRGEDFCSE YMYTDISSGF FEAVRTSRLK
     DWAHLLTFQT LDLEKDAAEQ GFEENSYDLI IAANVVHATR SLEKSLSTIH KLLRPGGVLG
     LVELTRTTPY INMTFGSIPG WWAGVDEGRT DSPLQSAEQW NTHLQKTNFS GVDLAAYDLP
     EPERHCAMLL STALGVNPTT NGHGTPRVEI LDSISWGLQE QHFSRQLADD LVKKGFEASL
     AEWANATVND SHSYIIMDSV QRPLLTQASD EQFDRVTTLL SKASKVYWVS FADGGNGITP
     DNALVTGFCR TARNENPNLH CFTIDIQDSL DQNFDQVLHA ITAFIRTTET KIASNEPCEF
     ELMYRNEKMQ IQRFVPSDKL LKAVSTSSED TEIHETTFHQ AERPLKIKVG KAGLMNSLVF
     VDDDLDDLGP DKVEIQSYAW GLNFSDVFIA LGQLPPAQPM VGESAGVVTA VGSNFASQYK
     PGDRVTAMFG TPYASRTRTN GHLIHKIPDG LSFTDAASIP LTFATAYYSL FDCANLQQHQ
     TILIHSASGA LGQAAIKIAQ RLGATIFATV GSASKRKLLM EQYGIPKSHI FSSRTTDFAA
     GIKRLTNGVG MDVVLNSLSG PMLHASWECV AAFGTFVEVG KTDISRRSQL SMKPFEKNLR
     FVSVDLVILS RQRSAYCQKL LRRIFADFET GLITPLPVTT MPIGDIEKAF RLMQSRTHNG
     KIVLEADDES TVYARAQPLR LRADGTYIIV GGLGGLGKHL CRHLQVKGAR HIALFSRKMF
     HDSAKNKIEK ELTIVPEAVI RIVTCDIGDS NTVLRVANEL YTTMPPVRGV LHCGMVLSDR
     TVSQITQKDF KIALQPKYQG TINIYNSFYN ADIDFFINFS SLCGIVGTLG QSNYAAGGTY
     QDMFSHAQLS VGHSKFVTLD FPLIKSTYTV TQEHTHSLAR QGIQLLPIEA ALPVVDYAMS
     GNAFKDDNHQ IAFGLDPQSF INLAKQGGRV PPLLSHITSN RGLGLARQAH QEKEQTAEEK
     IALASTTEDA EQMILIAIRE KISSLTAIDS QEVDLDPPIA NMGLDSLVAT EIKNWITNAL
     QAPVQTSDIM DAPSLRSLAA FVTKSSGLVK TTSRSKQESN GNEINGETNG DVQPNSSYGE
     VILPKYPLQS LETTLEVFLD SVRHLGNAEE LQHTHEAIDT FQKSDGIGQR LQARLARLSG
     EQGQNDEVVD IQDTARWPQA NQAARLSLTA YGYKLALDEG IVKQDYYNEQ PLDMATVHWL
     FSSNRTPDLD CDRYNRFPES DYLVAMKRGH AYKIPLRDHN GQTITYEKLK TIFQIILQQT
     PDGTSWASIF TTANRDEWAK AREDMMALSQ SNHDFVTTIE ESLFIVCLED ASPEIASERA
     DAFLLDGNSN RWLDKTLSFV VCANGVSAIW GEHTMVDGTT FGGLINALTT PAVEPDQASN
     ESSVTHVALD GDFTYLPFTM PPTLSNYITT LQVQHRCAHD GYTLANFTHT SYAAAYLRQH
     KLPPKTIIQL VIQIAIRRLF GHNPLGAVDV ISQRLFRGGR TDMIYVMTPP VQAFCAAAED
     PFISGMQKRR LLLEAVKSHT RLVTLSTRGR GFRWHLLALR ELLEPGEEMP AFYRDEIYMR
     TSERPVCTSF TEFGLPEMGR CQPHKGDVWV GVQVFEERIQ FTVINGEGKS DEFVRHLDEA
     TEAHHAIRVQ QHLSQHSKLD WKGHRKTDAG RSY
//
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