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Database: UniProt
Entry: A0A093XLJ2_9PEZI
LinkDB: A0A093XLJ2_9PEZI
Original site: A0A093XLJ2_9PEZI 
ID   A0A093XLJ2_9PEZI        Unreviewed;      2191 AA.
AC   A0A093XLJ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V490_08126 {ECO:0000313|EMBL:KFX87624.1};
OS   Pseudogymnoascus sp. VKM F-3557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX87624.1, ECO:0000313|Proteomes:UP000029320};
RN   [1] {ECO:0000313|EMBL:KFX87624.1, ECO:0000313|Proteomes:UP000029320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX87624.1,
RC   ECO:0000313|Proteomes:UP000029320};
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:KFX87624.1}.
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DR   EMBL; JPJS01002446; KFX87624.1; -; Genomic_DNA.
DR   STRING; 1437433.A0A093XLJ2; -.
DR   HOGENOM; CLU_000022_6_2_1; -.
DR   Proteomes; UP000029320; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF40; NORSOLORINIC ACID SYNTHASE STCA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-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; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          283..721
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1554..1629
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1663..1741
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          264..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1632..1662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1752..1775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2191 AA;  240094 MW;  54789F9145D1DCE8 CRC64;
     MAITCIYQLG SFISQAGTCE FAEKAGALGL CTGALAAAAV SCSGNILDLV PLSVDAVTAA
     FRTGMLVADM AARVSPGKVG DSWSIIVSGS TSTEALNKFC EQTPLPLTSR PYVSVYTQNG
     TTVSGKPEVL EKLLSCESFQ GLRNTRIPIY GPYHAPHLYS QHDITAIVEG LASVKYAMYQ
     ERIPVLSSTG AKVERRNFAG LLRAAVEQIL LQPIRWSNII EDVQTCIHAV NPQAFTVVPF
     GTCADQIIYS TIKETPLGSL INAVRTSRKP SDSPSTPYPN PKKPKLAIIG MSGRYPGAKD
     NDAFWNVLHQ GLDMHKTVPE MHWDAKTHFD PTGTKKNTSA TEFGCWLDDP DLFDARFFNI
     SPREAPQIDP AQRLALMTSF EAIEQAGIVP DATPSTRRDR VGVLYGVTSN DWMETNSAQN
     IDTYFIPGGN RAFIPGRINY FFKFSGPSYA VDTACSSSLA AIHLACNSLW RGDIDTAIAG
     GTNVLTNPDF TAGLDRGHFL SRTGNCKTFD DSADGYCRGE GVGTVIIKRL DDALADNDPI
     LGVILGAYTN HSAESESITR PHVGAQRAIF NKILNQAGVD PYTVGYVEMH GTGTQAGDAG
     EMLSVLDTFA PPLSEVKRGR NADEALYIGS AKANIGHGEA ASGVSSLIKV LLMMKKNIIV
     PHCGIKTRIN RKFPTDLQER NVNIAFKPTA WDMSTGPNKP RRAFVNNFSA AGGNSALLIE
     DAPERPEISR DATDLRSHHL IAVSAKSGVS IQGNLSTMLR FLKENPDVSL AELSYTTTAR
     RIHNQHRVLL CGSNVKSLCN QIETSLQNKA GVTRAKNTPK VVFAFTGQGA QYPGMGRQLF
     ESFSVFRTEM NRLDHITQSL GFPSVLPLIQ SEEQDVDIFE PLVVQLASVC MQIATSKLWA
     AWNITPTTVV GHSLGEYAAL NVAGVLSDAD AIYLVGTRAT LLQQKCTRNT HAMLVVKASV
     DEIAQTLPNG SYEISCINSP RETVLAGKIE GITRLKDLLA EAGTKSIFMK VPYAFHSSQI
     EPLLSDFTIA ASCVSYLEPN IPVLCPLDGN VVEEHGNFNA EYLARHARES VNMRKALAAG
     HKQRLISDQT VVLEVGPHPA VSGMVRAEFS QQVTTLATLQ RGRDMWPVLG ASLQWLYVSG
     ASINWTEYHR DFKGSHKVLS LPSYSWDLKP FWMQYVNDWS LRKGDPPMVI NSALSLESTT
     IHRIVKETGD SQKTYIVVEA DITREDLSPL VQGHEVDGIP LCTPSVYADI ALSLGSYLLK
     RYQPAQKESL VDVSDMTVSK ALILQPNVTQ QLLQAHSDID WSNNCASTKF MSFDSKQKLQ
     EHARCVLRFK SHELQGILQA DAANVKKKMQ ALRDGIALET SARFNRPMVY RAIRPLARFH
     DDYRAIDEVV LNSTTLEASS QLSFGSVKRA GNFHTHPAII DSLTQSCGFT MNCNDSSDLD
     TEVFMNHGWG SLQIFEPMDF EKKYTTYTRM SQGPDKLWHG DVVIFNDDKV VAFFSQIAIQ
     GVPRRVLKVI LSLESGRKTQ KQQLAQTTSQ PAFEAKPTAS NLHTSSPNNQ GPQAAKLNMA
     LTIIAEESGL AVSDLSDTTV FSEVGIDSLL GLTISTRFRE ELDLDLEFNA MFYDYPTVGD
     LKLFFGDAEP SGTPISSSST SFDDTASPTS TAGATTPSNG EGASCELDFQ SVLAIISEES
     GIAMEELAED TNFADSGVDS LLSLVIVSRL RDELEFDIQH ESLLLECPTV GDLRRLLLGD
     VLSGNPVKFD LPIEPEVPEG TKTQGGASTT VDESPVRTEK EILALDTRKQ AVDELVQKYT
     ASFAVSGPSQ KSITASENET VVLVTGASGS LGSHLVYHFA QLPDVKRVVC LNRENKVDPY
     LRQRKAMRDK GIRFPEALEN KLLVLQTDIT KPMLGLPSDV YKSLTTSVTH LIHNAWPMSA
     KRDLAGFEPQ FQSMRNLIDF GCHVISCRSS SFKFSFQMVS SIGVVGHYGL GTGETRTMVP
     EDRMSIDAVL PNGYGEAKWG CERMLDETLH KHASHFRSMV VRLGQIAGSK TSGYWNPMEH
     FGFLLKSSQT LNALPDVDGD VFWTPVNDIA EILSDLILSN RTPHHIYHIE NPVGQTWKEI
     NAILSNALNI PNLIPFTEWL ERVRAAPHRK NPAATLLEFL ESNYLRMSCG GLILDTHHTL
     QHSKTLLAIG PVSEEVVRKY IHIWKEIGFL D
//
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