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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//