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Database: UniProt
Entry: A0A094EN24_9PEZI
LinkDB: A0A094EN24_9PEZI
Original site: A0A094EN24_9PEZI 
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
//
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