ID U1GED5_ENDPU Unreviewed; 2402 AA.
AC U1GED5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERF75982.1};
GN ORFNames=EPUS_01348 {ECO:0000313|EMBL:ERF75982.1};
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:ERF75982.1, 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; KE720795; ERF75982.1; -; Genomic_DNA.
DR RefSeq; XP_007786831.1; XM_007788641.1.
DR GeneID; 19236406; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; KDVQHYT; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine 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; 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; 3.40.366.10; 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 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; IPR013154; ADH-like_N.
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; 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
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; 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; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
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:ARBA00022679}.
FT DOMAIN 29..456
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2320..2400
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2402 AA; 261920 MW; C4A355A945E852A1 CRC64;
MGFNHADNKG PTRASPPETS GKGSEGFVQE PVAVIGLACR LPGRNTSPRT LWNFLERGNV
ASNSVPESRF NLKGHYDGSK KPGTMRPPGG MFLEDVDLET FDASFFEISR AEAVSMDPNQ
RQLLEVIYEG LENAGVSLES IDGAPVGCFI GSFAADYHDM QGRDPEDRPP SIEVGIGRAI
LSNRISHFLN IKGPSVTVDS ACSGSLVGVD MACRYLQTGE ISSAIVAASN LYLSPEHVMD
TGPIGMAHSP SGRCHTFDAK ADGYIKAEAV NAIILKRLDD AIQDRDPIRA VIRGSSTNSD
GRTPGIASPN PAAQAAAVKS AYSNAGIESF EATSYLECHG TGTPAGDVLE TQGVSAVFAG
GRSASAPLIV GSIKSNLGHS EPAAGLSGVF KAILAIENGI IPGNPTFETP NPKINFEELR
IRASRTAIPW PKSDFRRASV NSFGYGGTNS HVILDELKTL RPEQNANHVS SYLSQDDDIY
DEEVSARPYT LVFSANDAAS LQAYVATLDQ HVSSLDVKVK PRDLAYTLSE RRSHHFYRGY
IVAHGNEIDS KTMVSGKKSG EKPRIGFVFT GQGAQWSQMG KAVVDTLPSA KPLLEKLDAA
LRQLPNPPSW SLLGELTESR PSEHLRLPEF SQPLVTALQL VLLDVLRRWG VDPQSVVGHS
SGEIAAACAA GYLSEEDAIK AAFYRGQSAK NCRHEGEKTL GMLAVGLGPD SVKEYLVDVQ
EKVQIACYNS PKSVTLSGAA DALEIVKGKL VKHGHFARML LVDLAYHSNF MSEIGEDYET
LLQQNFKPLD AKRGSVDMFS SVLGQKMSGL TDAKYWRSNM ESPVRFEEAC REMLSGRTGA
DYLIEIGPSG ALAGPVSQIK NIMGADGLKV QYCATLSRGA DSINSLFDMA GKLFISGASI
ALSEVNNDQD SSLSLPSVIV DLPNYVWNHN NKYWHESQAS KDWRFRQFPE HDLLGSKILA
TPWHAPAFRK TLLLERLPWL KDHRMGTDII FPASGYISMA MEALYQTSTA QGIHVDKPSA
AFLQYRLRSV KFEKALVLEE GTESKVVLSL NPLAGTKNTW YEFQVSSSND GISMTHCTGL
IRTEDVNVKI APREDLAQLK YPTPAHLWYK AQTEVGYGFG PGFQKQLFVE TVAGQRESRS
ITSLTEPESA HSPQSLYPMH PACIDGCFQT VTPSLWAGER ATINAVLVPA TLDNLVVYPK
VSGVEEGLSL ARSQYTGRGR REEAKSFFSD CSVFDQASGK IMLKMNGLRY YKLDMGSDMH
DRHTYNRTIW RPDITFLSQD QLYSLAHRDS SRGIQHLIDL IAHKKPALKV LEASCLAEDS
TSLWFSSETS VIRSGVAQYS YVSSDAKALL SAKEDYDVMK RTSFHLTDIL RPGSSLPEID
YDLAIVKVSD LNEETVTKVA ASIRAGMSDD AFVVFLEQQT EAATPVSESD SDSSTVFVHG
HELATKTTEN TRMACEDHAI VSSIANCGYS NVLRAPQSWA PKAYMGKVVN QTIDTATAKR
VSVMHLSDHS RLSDGLKTIL EQSDWQLTEH FHPYSHVQAK SIVLVIDETI SPVLNSISES
RWDGLRRIIS QRNRILWVTE GSQMEATKPD NALVHGLFRT IRAEDRAADL VTLDVEYSES
PSTYLAIERV LRLFLKSPSK TQIESEFVER GSIIHVNRVV PDEPINTAKN NEKLGGPPVA
RSLQDIDGVA MLRAERLGTL DSLCYSEMSS EELPILENHI EVDIKAAGLN FKDVAVTMGI
VPENEHLLGL EGSGVVRRVG KGAERFRVGD RVALLKNGTF ANRIQCPVDR AHHIPADMSF
KDAATIPLVY LTSMYSLFDV GGLSKGHSVL IHSAAGGVGL SCIQLAQWIG AEIYVTVGTE
DKRQFLHENF KIPFERMFSS RTTEFAPKIM AATEGRGIDV IINSLTGELL DESWRICADG
GNMVEIGKKD IVDRNFLSME PFDRNCSFRA VDFSFSKQIK DSLIASLLER TFKLVSEGHL
KAIHPVTTYS FSQVPAAFAF MRSGRHIGKI VITDEEDTKV PVQVRPPPRA VSFEDHASYV
IVGGLKGLCG SLAIYLAKHG AKNIVAMSRS GCSDERSRNV IVNCNALGCE VQEAAADVSS
LSDVKKAFQS AKYPIAGIIQ GAMVLKDKPY EMMTVSDYHT TLSSKVAGTW NLHHASLDLK
KPLRFFTLLS SVSGVIGQKG QANYSAANVF LDAFSSYRLA QGLPAHSVDL GVIEDVGYVA
EQGGMQKHFD DRQWIGINEY VLHKILGLSV LQQTAPIKHA SASQLITGIL VPQPADSELA
YDARFSALFH SNADGQELGS TASSAEKDVQ ALLLLRGSGA EPAAMLGAAA VAVGSKFERT
LRLPEPMEPG KSLSTYGLDS LSAVELRNWI RMELGVEVTV LEITSANSLT ALCEKIVAKM
QA
//
