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Database: UniProt
Entry: U1HWI2_ENDPU
LinkDB: U1HWI2_ENDPU
Original site: U1HWI2_ENDPU 
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).
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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
//
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