ID A0A094EN24_9PEZI Unreviewed; 2405 AA.
AC A0A094EN24;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V499_00977 {ECO:0000313|EMBL:KFY80141.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY80141.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY80141.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY80141.1,
RC ECO:0000313|Proteomes:UP000029295};
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 -!- 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:KFY80141.1}.
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DR EMBL; JPKB01000102; KFY80141.1; -; Genomic_DNA.
DR HOGENOM; CLU_000836_0_0_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..415
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1201..1277
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2323..2403
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1279..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2405 AA; 265277 MW; 144111EB1634F9CC CRC64;
MNEPIAIIGS SCRFPGESST PEKLWELNQR PRDLLRKFPK KPRQADNSDD QEQLLYGTGN
IAGSYFISED VRGFDHHFFR MHPMEASTMD PQYRLTLECV YEALESAGLP MEKLRGSSTA
VFAGLTGTDY SNILTRDPLE VPRYTATGAY KSMFANRISY FFDLSGPSIT VDTAFCGANL
LLDSEQYLTA GNLGMLSPSG RCHMWDTKAD GYARGEGVGV IILKRLDIAL RHGDNIGCIV
RETGVNQDGR TLGITRPSPA AQSALIQRTY TRAGLDCKKF EDRCQFFEAH GTGTSGDAVE
AEAIQSAFFD DREPNSSQEK EPPLYVGSMK TIVGHTEGCS GLAGILRASL AIQKGYIPPN
FGFERLHPDI APFYKGLEVP QRIKPWPALP QGIPRRVSVN SFGFGGTNAH AILEQHLLTP
KQTGSRHIQE DTELATALPF VLSADSDWGL ASQLASYSKF LKENPKVNME HLAWTLCARR
STLSVRAIFT ASTVKELSDK IDHVVFLSRL VGHEAPGIHP HVSLHRPRIL GIFTGMGVPW
KGISDLIRTS SIVRQTVSEL QNSLSILPQK FRPSWSLRQE LKALTSERSI EYAATQPSLS
QSLSTSIQII MVDLLRSSGV QLNAVVGHSA GEIAAAYAAG FISRVDAIRI AYYRGFFMSL
VKKNGAMLAV NLSLQEALSL IQTSGIPLEV AAVNSPHSVT LSGELELIES MTKILQDKKC
QTRRLTGRIP YHTRHMHRCS EAYLEALRNL DIKTQVPPQG FCAWFSSVEG HGKQVYNTSL
AAEYWIQSLV CRVRFDKAVA QALTDQGSVD LVLEFGPLAS LETPVLDTIK SVAMHELPYT
GIFQRGLGSA EGVAHALAFI WAHLGFSAVD FESYLNDMMG QSQLRLVPLN GLPALSWNHD
RVFWNESRSS RMHRYHRGLR HNLLGVQSPE SVESEFRWTN TLDIASVSNM MSSITHKDAA
VPFPVAMSMA LSAAMIAAKG QAVSMIILED CKVYSLERFH ASTTHMDTLF TLRILKKRAS
FVSATAQYYT TASEDTNSLQ MCFGVELRII FDLDQNKSGR QSLDTRSAAG ARPLISPAKL
QAILTSAYER QGFNTKHSSL SKIDCITVYP ELCLQAFESQ LSFKSSVVER RGDVFIDIEV
LGIDNSQAPI LIEGIHVSPP SHTLVANLPP HLGGDMKIEQ DVADLTLKDE IVTVDYEGNE
QVLLSAFLVK LKQITELSSD NGSAVEELPL VQLGIDSLGA TEIRTWFLRE LSISFSVRDV
LGGASARGLV DQAFSRLSPD STTLPSIQST DSQSNSTDET QSNDGMLLAP ATEEQPARSG
FERTAQLSHA QSGYWFTQCA TNDKTSLNVS FYYHFAGDLN VGRLERAVDL VVQRHESLRT
CFFVDEADNG RPMQGVLMQS ACVLENKIIF GNADVGVHFQ ALKDHIYDLD SGDTMKIILL
KEGTRSSYLL VGYHHMVMDG FSFQQIFLPE LEKAYTGQTL PQPVPQFCDH AYQQRHALET
GETGATEVAY WKKVFTDLPP CLPLFPMSRV TFRLPQTTYR YNTERLVLDK TTTDQIRKVS
RENNSSAFHF HLTILSILLF RMLEIDDVCI GVADANRNDE DETRVLGLLL NFLPLRFLYL
PGNNFSGSLQ NVRDLVYDAL SHSRLPFSIL LEELQVSRSS TSTPLFQTFI NYRSRQAEKG
SFAGLLGRSH QVQLTKAGYD LSLDIGETPD GETEIVFLCQ AAIIPQDGAS VIMNTYRNLL
RQFAHQPEVR MSACSLYDKQ DVNRALEAGR GPLIESGWPD TLIHHVDEMA RKFSSAIATS
DGTTTWTYRE LRARYISIAT ILSRKGVVAH SHVAVFQEPG CDWVASMLAI MYIGAVYVPL
DQQNPLTRLA VILRCCDPAA VICDDSTIDS SPSLGCSSDK LINVSNIITD RQHLAQLPPV
EAHGNDRAVV LFSSGSTGTP KGIAISHSNL VCKIESFSHR FRLAGSELVT LQHTAYSFDV
SLDQIFVGLA NGGRVHIASK SIRGDSAELA ATIVRERVTF VETTPSEMQL IVQFGLAELA
GNKSWTLALC GGEKFPESLK MDFRELNLPH LRLFNVYGPT EATIAVTHFE ISYRSIRHET
DEAQPIPIGP VLPNYSISIV DNNLQPLPAG VPGEILIGGG GVALGYLDDA LSVKSFIPDP
FASPAFRAKG WDRVFRTGDR GRMHHEGNVS FEGRIDGNTM VKLRGLRVDL GDVESSILSA
AHGLVSNVAV SMRGDPAFLV GHVVMSTQQH QSAPPMDTES FLRDLLPKLQ LPAYMIPAVL
VPVDKIPITN HGKRDQQAIA ALPMRSSPSL HALGTKSDVD SSFLFTKTQA ALKEIWIQLL
SEDITASRPI STNSEFFEMG GNSLLLIRLR KNIQNTFDIN IWLPTLMEAT SLGAMAEVIE
KEVSK
//