UniProt: A0A446BNQ2

Database: UniProt
Entry: A0A446BNQ2_9PEZI

LinkDB:  A0A446BNQ2_9PEZI 
Original site:  A0A446BNQ2_9PEZI

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Ontology (5)   
   GO (5)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (42)   
   InterPro (23)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
All databases (48)   

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ID   A0A446BNQ2_9PEZI        Unreviewed;      2184 AA.
AC   A0A446BNQ2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Ddfcf033-124e-48c3-8647-9deef8689590 {ECO:0000313|EMBL:SPQ24118.1};
GN   ORFNames=TT172_LOCUS6537 {ECO:0000313|EMBL:SPQ24118.1};
OS   Thermothielavioides terrestris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX   NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ24118.1, ECO:0000313|Proteomes:UP000289323};
RN   [1] {ECO:0000313|EMBL:SPQ24118.1, ECO:0000313|Proteomes:UP000289323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Huttner S., Dainat J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OUUZ01000012; SPQ24118.1; -; Genomic_DNA.
DR   Proteomes; UP000289323; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; cd05195; enoyl_red; 1.
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; 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; 3.
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; IPR013149; ADH-like_C.
DR   InterPro; IPR011032; GroES-like_sf.
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; 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; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 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; 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; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..431
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2102..2179
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1480..1503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2184 AA;  239315 MW;  BD81D50FBEA4C5B2 CRC64;
     MGSHKRRLAA IIGIGSRLPG DISTLSDLYQ MLSRKRTGWS EVPADRFNAG AYHHPNPDRK
     GCFNSQGGYF ISGDVSEFDA GFFDITKKEV ESMDPAMRLL LECVYEALEN GGVPKESISG
     KKVGVFVGAN YSEHRTSNLR DLDHIPTFDA TGNQGAFLAG RVSYYFNLRG PAVAVDTACS
     SSLHALHLAV QSIHAGESDL AIVAASHLLT DPDIWVSMGK LHLFSDAGKT YAFDHRAKSG
     YARGEGAACL ILKPLASAEA DNDYIYAVIT HTGLSHNGRT VGIAAPSPEE QERLLRKVFA
     EARIDPREIG FFEAHGTGTK KGDPIEARAI YRAVSHLFDP EDPLHIGSVK PNVGHLECAS
     GLVSVIKAAL ILSYRFILPN ADFERANESI PLSQWNMKVA TAQRPWPPKR KYVCVNNFGF
     SGSNSMAVLS AAPKPKGYEV SEKSRESPLR LYVLSAADET ALRNTISRLS VWIERHAELY
     QSTLPKNLAY TLCQRRSHLP WRVAVVADMC GGVAAALNSR DTTMARAPSD PPRLAFVYTG
     QGAQWWAMGR ELLRTHPVFL DSILRADEAL WPIADFSIYT ELTRDREESR VGLAHISQPL
     CTAVQLALTD LLHSFGIRPI AVTGHSSGEI AAAYAAGALG FKAAISAAFY RGRMITELKA
     RHPTLRGSMM AVGAGASDLA PVLATVTDAC VVVACENSPS SCTLSGDEAA LDRVAVIMQQ
     RGIFYRKLFV DVAYHSPHIQ LIAESYLRRV GHIHPLIERG AAPVQFFSSL YGRRAAFKEL
     GARYWVDNLT QAVRFSTALQ GLCIEHKPDI LIEVGPHAAL QGPIKQILQA MGIAGKTTYL
     PTLIRDQDAT RTCLETAGQL FVRGHPLNFY EVNHHHEENE SPQLIPSPYT YPWTRQKYWY
     ESRVSRLHRL KPFARHDLLG TMADWSSDLE PTWRNVFTTA DLPWLRWCRV QSRMVFPAGG
     FVSMVIEAAT QMAALKGTHA AQFDIWNLKI AENLFVDDDR EYELVLTTRS SSWPNTDGSY
     DFHISSHECS RGWMSHCTGT LVAAPRRTPC AKAAVARAAQ ATSARARRRM LFRSAAMRAH
     KIYVSPGDWR GPHAVPFRAT LAGVYQRLAA AGMVYPFSFQ SFVAVEVDES EASGQLLVQD
     GAPEMPMSHE ARYELRPSVA EAMFQLPVFS YQLDAWGKTT VPYLPSFIRH MTVHSSLAKA
     FRAGESAAAR ATPEPEPGSF MVELWKATDT TDPAAICMSG LKFAALEPSR PEIPMPRELC
     YKASWSYLVD CIPDGTAELC HNPRCRIVLV VRDMLQAKDP LVVALSSLLE SKTGVAPKVR
     HLGEILVWSP FFFIVLSEVW TPVLASMGEE IFYRVKALLS QAPGLLWVTK GATRFPTCPK
     ASLASGLLRT VRSERSIVAA TLDLDPDSWL DAAAQAALIW EAFATSVLSE GPGPTEMEFA
     EADGTLTVPR IVPDKQANVE VQRNLGESAP YWQNFHQPGR PLSLAPQRGG SGSSGGNEEV
     YFEDAPKTPL GEDEVEIAVT ACTLSAEDVA AGNTGRVTRG CCGRVTRVGR SAIMYWPGDR
     VLALVEGRFS SRVRAKLGNF ICLPRWITRE QAASIPDAVI PAIYALEHLI DIHPKERVLI
     DMSGPIGLAA IQVTRARGAI PLVLIRNKEQ ARAAQRAGVP DHRILDARSA YLRKHVHAAT
     RGRGADAALV LAGPNTAVAV KCLADFGRLV EIRRGSHPRT RVELGSVNAA FASVDMYDLA
     TQQPESMQRT LMATIENMRF GLLDPLPAKK VVPVSKLARG LRLVRKGAVE PVVVRVDGRG
     RVKAVHRRPK SVFRSDATHI VVGGTGGLGR SVAKYMMENG ARHIVLVSRS GLHSGVVEAL
     KPETERYRAM LTVMKCDVAD MRQVTEFVED CRRHLPPICG VVHAAMVLRD TLLDNLTYDD
     YRRVIRPKVD GAWNMHMALE ARYVPLEYFV VFSSTAGIIG SRGQGAYAAA NAFLDALIQH
     RVRIGLPGAA LDLTAVTNAG YLAENEGRQE GVFRNFGHET ISEREVLALL SAAVRGVGGP
     QYLTGLKLRP ACDGDWPYYA AHDRRFDMLK AASLAQAKDE SEGFNAPMPT GQAFQEAGSE
     EEATSVAAQG LIEKLSDVLS ISPDDLDVAR DITAFGLDSL TAIEIRNWVS KEYRVTLEIM
     QLLSSGTIMD LAASIVKNGW KKKN
//

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