ID A0A094ANC5_9PEZI Unreviewed; 3251 AA.
AC A0A094ANC5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFX99536.1};
GN ORFNames=O988_03805 {ECO:0000313|EMBL:KFX99536.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX99536.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX99536.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX99536.1,
RC ECO:0000313|Proteomes:UP000029329};
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:KFX99536.1}.
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; JPJR01000652; KFX99536.1; -; Genomic_DNA.
DR STRING; 1391699.A0A094ANC5; -.
DR HOGENOM; CLU_000022_31_2_1; -.
DR Proteomes; UP000029329; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
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; 3.30.70.3290; -; 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; 1.
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; 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; 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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2515..2592
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 463..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2977
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 3251 AA; 358056 MW; 88EC3F0C29D3425B CRC64;
MADLEPIAII GIGCRLPGDV GNAEDFWRLL SEGGSGWSVV PKDRWNVDSF YHPDGTSIQS
YNAKSGYFMS QDVTDFDSRF FGFAHNEANV TDPQQRILLE TTFEALENAG VPMESVKGSD
TAVYAALFAR DYDRIGYKNL EGLSQFHIPG TGEAIIANRV SHFFDLRGVS MTIDTGCSGS
LVALHEACTA LRTGQSRMAI VGGTEVLLHP DQNVIMSSGG MLNPDGKCYT FDSRGSGYGR
GEGVAVIIVK QLKDALADGD TVHAIVRNSG ANQDGKTNGV TLPNPDAQEA LIRRVYSDVH
LDPAETPYVE AHGTGTKAGD IAEVQSLGNV FTEKPRTRNL YVGSVKTNIG HTEATSGLAG
LIKSILILKH KQIPPNLNFI EPKPGLNLDE RQISVPLDLV PLLPEGSKGA HRVSVNSFGY
GGTNCHVILE SLDQYLSGHS GYLTNGSINR GTNGVVNGAN GHSDTNIGEG NSVQLTNGSS
GINASHGSNG AKEKSTTSAE SMPLIFPLSA TSEAALDETP AQIQKWLLGR DDSTSDLSDL
SYTLSCRRSL FKWRKAFVAS NVAELTAALG EGKISKNRSA PSAKVAFVFT GQGAQWAGMG
VELIGSSQVF KSSIESSSQL LKSLGCEWDL IQELSKSAAD ESRINESELA QPLTTIIQMA
LVDLLAHYDV KPDFVAGHSS GEIAAAYAAG ALTLEAAVKA SYLRGLQSAI AKRLNELPGS
MLAIGYGEHV ALQTIKAANI DSTIGRVVVA CVNSPSSTTL SGDEPAVDYV SEMLRSAGVF
QRKLKVETAY HSHHMERVAS SYLKSLEGLS STEIKSDVEF YSSVTGQTKN SDFGPEYWVE
NLVSQVRFND AMTALLNAMA ATGAPDAANI LIEIGPHSAL QGPINQILSS IPGFKSTYVA
PLARGKNSVS SFSTAIARLF ELGAEVNFEK LFAKPRRVID NLMPYPWDHR VKHWAESRLS
RDHRLRSFPY HDLLGVYDVM SPIEEPRWRH HLSIQRLPWL KDHVVDGMVI FPGSGYSAMI
TEAMKQLVHL KKPDSDAKIA NTIIRNVRIA RPIILPVEST DGPGDDIEVQ LILSPSKISD
ANPWYSIRIL SLQSDGTWAE HVSGTVRAEL ETTSVTGKER KATVDEAFEA FERIKSRAQE
KLNMETFYDE RRAAGNDWGP NFALLYEAHI GPWVGFSKLR IPDMTQCMPA GYFQPHLIHP
TTLDASNHMV PAVFHREIKN APLMPISTEE VLFTNNLSSK PGDEMIVAME LKAEGKSQAR
GNVWVFQNDH TTGEVTFVSS MRGLVMRAVG EGASTDEYKP FQRKHNYQVY WDDDPDHLSK
DSFTRLVEPH ARENSELLEQ LSTIEKATAI YLNRVKDMPM IQNPETAPLP HLRSFSRWIS
DYVNSDACLK ICESLSDSEQ AEVLDRSDSS DIEGEMLGRV GRNLAGILSN TADPLELLVA
DDLFERFHNQ GPLTPLYQQL VQYAGLLTNK NAQMNVLEVG AGTGSATLPL FKSMGEDASD
LVKKYTYTDI SSGFFETAKE RLDKWKSIIE YRTLDISRDP VDQGYKANTY DLVVASNVFH
ATKSICESLT NVRKLLKPGG ILLFVEINNS LVGASRSLGT IFGTLPGWWD FVDGRVGSPL
LTPDQWHEQL LQTSFGGIEY SSQDCDGPLA RASLIVSKAI EEQKPTDTAS LIDSVTVVHN
SVSPIGQSAS TALTSAFQQK GLSSSINHSW EALPEVDAEA CEGTMYMVLD SANSSVLEHP
TQEMFDRYQN LLVNCRNLIW ISFQEEGGLK EGSIKGLAGG LARVVRRENG GVKLITIDVK
NVLSTKDDVS RFVQKIQNVA LQLLQPDISN RAIVDEEFVV DGDKLLIPRA YADKKFNNWT
DLVNGRSNLS LQSFKNPNLP LRMEVGTPGL LSSIHFIHDT DASSPLGSEQ IQIDSKAFGV
NFRDILCALG QLQNGTFMGE CAGVVTAVGP GEFVQRTYKV GDRVVGMHAQ PFASYSRLSG
YDAHVMPDNM SFADAASMQV VFTTVYYSFV NVARLEAGQS VLIHYGSGGV GQAAIQLARH
FGAEVFVTVG SEEKKKFILD YFGVPESHIL SSRASPRDLK RHLLQLTQNK GVDVVLNSAS
GEMLAESWDC VASFGFHIEL GKTDIDKNTH ISMAPFKRNV TFSSVDLVTI AKERPKVFYD
VLDKTIALFA KGVLKPVYPL NIFPIDQVES AFRLISERKH IGKVVLDCEH EEKVQAVLPA
PAPTKLQSEG TYIIAGGLGA IGRMLVTHLA LRHAGHIITL SRGDLADEEL LPWQAEIAKF
GAKLHVLKCD ITDESSVQEV AEYCRQSLPP VRGIFHAGMV LRDRPLAKMT RDEWNAVLGP
KVRGTFNLDQ AFSSPNLEFF VTLSSIATTF GNPGQGNYSA ANAFQDYFAT HHDRTYPTRY
VSVDLPVVDE TQALAQIELG TRSFILQVSM LFDVRELMQL MDYAMNRSVE LDRPFLHAIM
GFDRKSMSQG TGDDLFSALF QTIPQMQTSN SQDQTSADAK QDIESLLTAV NSFDEAVKVI
METTIEKFVK FLNFEADDLR PDQPLSSYGL DSLVSIELKN WMVRAFKVTL QVSELTSSRN
IAHLAELLAT RSKILPAGLS KQSQGRKLEK NEIEDKADFQ EEQALLAQPD DAEIETLPCC
PLPTKEARQP VPNLVLGLQK HLENSSHFAH SEEEIESLRS AMKEFLEPGS VGEQVYKEIQ
KDARDPKFPD IKRARISDKN KVDGILRIIT VCQILWFVVD MAGRVAQHLA ITCGELTTAA
FIMRQALQYC SFMVMNHPVP VPHTQADRAA LLAETAFQFK QKIDNGTVEP MYILETPVCQ
AQLQWMFNTY RHPKIGGDEI IKTTGDYCVV FRRGRLFQVP LQTGDAPVSF DTLRATMAAI
LEHVQDEGTW AGILTSDNRD SWANIRTQLL AVSPANAHYF QVIEEAAFAM NLDDSSPINF
TEFAKQCKMG SGFNRWHDKP MQFIITANGE SGLLVEHSYL DGTTPAALYD RMHDAIRAYK
PTSQAPPQVP SPEEIPLVLP SNLDNHISVL REQWLSNNAL RDFISYELPT LSGQILGQSK
VPIKSGYDVL CQLAFFLYNG KRIAANWQPV MLSQFHDGRH DMVQMASPKV RAFCEAVVAT
GEDEVPILQK RNLMIEAARD ISRRLSEAKD GKGFFRLFVT IEQRWPKDQP KARVFDDTLH
KRTFDFPISN INHNTVESVT TPLDPSALRI RYTIHDDHTL ISLNCPTGAA DKLIEAVNEA
AIIIRELSLS K
//
