ID U1HWI2_ENDPU Unreviewed; 2021 AA.
AC U1HWI2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=EPUS_01003 {ECO:0000313|EMBL:ERF73749.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73749.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE720941; ERF73749.1; -; Genomic_DNA.
DR RefSeq; XP_007800752.1; XM_007802561.1.
DR GeneID; 19236062; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; GMSCKFS; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000019373; 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: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; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 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; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
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; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 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; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 14..445
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2021 AA; 220455 MW; 9540A9AD7E49EF7C CRC64;
MDFKNSEWAS EPASEPIAVI GMSCKFSGSA SNPDKLWDLM AAGKTGWSEI PEDRYNLKGV
YHPNHERTST THVKGGHFLD EDVAAFDAAF FNYSAEMAQV VDPQFRLQLE STYEALENAG
LPLSQVMGSQ TSVFAGVFTH DYQEGIIRDE DRLPRFNVVG TWSPMSSNRI SHFFDLRGAS
MTLETGCSTT LVALHQAVNT LRNREADMSV VTGANVMLNP DTFKAIGSLG MLSPDGRSFA
FDSRANGYGR GEGVATIIIK RLSDALANND PIRAVIRETA LNQDGKTDTI TTPSAAAPGE
LMRECYRRAG LDPRGTQYFE AHGTGTPTGD PIEASAMAAI FARGEGRDDE DYYLRIGSVK
TNVGHTEAAS GLAAMVKGVL CLEKGLIPPT VNYETPNPKL KLDEWRLKVV RSMEHWPDSL
VDGPRRMSIN NFGYGGANAH VILESADPWT LTSGLDVNPI NGNGHTNGHT NGHTNGLTNG
LTNGHTNGHY IHDTTDDAKV LILSARDERG CQQMLSDLKA YLEKKKSLGQ DASEQLLRNL
SYTLGERRTL FQWVAAHQVR LDEDGTLEAA IRALETPRFK PSRRAADRPR IGMVFTGQGA
QWNAMGRELL TSYPIFRQSI DEAEAILKDL GAEWSLLEEL LRDKKTTKVH ATNISIPVCV
ALQIALVRLL ESWGITASAV CSHSSGEISA AYAVGALTHR QAMATAYWRA VLVADQTKRA
SGAPKGAMAA VGLGVEAVQP YLDRLTKENG KAVVACVNSP QSVTISGDDA AVQEIEDLCK
QDGVFARRLK VQQAYHSHHM DPCAADYRER LRLEMARDVE QRTKQQHLQA SKQELKAVFS
SAVTGGRVAD IKQIASPDHW VGSLVGAVEF VDAFTEMVLG DPDDPTGRSV DVLLEVGPHT
ALGGPIREIL SLSDFEGLDL PYWGCLVRDE HAGDSMRSAA LNLFRQGHPL VMDQINFPVH
AYDDESPQVL TDLPSYPWNH TMRHWQESRV NKAINERSQP PHELLGMRVA GNDPSSTVWR
RILRVSETPW VRDHMVQGSI VYPGSGYICH AIEAAKQLAE EDKSGKDISG FRLRDVNFLF
ACVIPDGAEG VEIRTTLQFV SEREIGARGW YRFEVSSVTL DNRWTLHAKG MVMAERGAAA
PEKTAKRRPL STYTRQPDPQ DLFANLRARS VNHGPLFQNT TRIIQDGREA RSVCDVTIRH
EASSDTDPLV AAKNTLVHPI TLDAVVVAFY SVLPNVGALQ DDPKLPRSVA SFWISNDIST
EVGRTLCCDT SLLHDDAQSG TANITIFDSE TDLAVLSIQG LEFASLGRGS GATARQDAAN
RGGAAFTPKW EQEVVSKLVW GPDFSLQNPL AIEQIKNELA TIESGATGIK QLSLLFRKVA
HKNPGARVLC IGSGTDALAT RSLLETLDQP LVGSWHITEP TSESLEDTHA QLAEWARVLE
FDQLNIEESP TKQKFTTGSY DIVVSVQALR SAKDMANALA NVRSLLKPGG TLLFAETANG
ISSWDGLLRD AGFRGVDLEV RDSELDSVDS KSVVMSTVPL PENKKSKLSN QEGFVVVTST
RTCPPSGFVD VLSLRIKALT GTDAEHLVLE QSSFDLYKGK ICVFVGEIET PIMADLDSVT
MEGLRAMVTQ CEGLLWVTVG ATVAGEIPER ALHQGFLRVL RNEYISRRFL SLDLDPAHAV
ERWSSGGETI VSTIVQVVEE GFCRVDSETG PQEFEYAERD GVLHIPRYYK DEQYNNMVAG
SLVPSWAELL PQVAKDEKEG VDGLANLPLE ALFQENKPLR LEVGIPGHLD TLAFVHHEDE
QLGSDQVEIT PRAYGVSSRD VLAAMGQLKD RSMGEDLAGV ITRVGNEAQA RGYNVGDRVM
ALSTGASFAS RALVPWHAVV KIPSSVDFLS AASIPLAFTI AYVALIDTAR LEAGQSVLIH
AASGAIGQAA IMLAQQMGVT EIYATAGSPE KRELLQREYG IPAEHIFNSR DASFAPAVLA
ATNGHGVDVA QLTSWRSSAG KPQHGCAFGS LDRNWQTGRR E
//