ID A0A2T0RJN8_9ACTN Unreviewed; 3096 AA.
AC A0A2T0RJN8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:PRY21332.1};
GN ORFNames=CLV70_12041 {ECO:0000313|EMBL:PRY21332.1};
OS Pseudosporangium ferrugineum.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Pseudosporangium.
OX NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY21332.1, ECO:0000313|Proteomes:UP000239209};
RN [1] {ECO:0000313|EMBL:PRY21332.1, ECO:0000313|Proteomes:UP000239209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY21332.1,
RC ECO:0000313|Proteomes:UP000239209};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY21332.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PVZG01000020; PRY21332.1; -; Genomic_DNA.
DR OrthoDB; 5476359at2; -.
DR Proteomes; UP000239209; 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 CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; 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; IPR049552; PKS_DH_N.
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:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239209};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PRY21332.1}.
FT DOMAIN 32..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1353..1428
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1446..1870
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2996..3071
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3096 AA; 325148 MW; 6981208DDC3AE459 CRC64;
MSDDKLRHVL KQATVELRQA ARRVRELEER DREPIAVVGM ACRYPGDVGS PEDLWRVVAD
GADVISEAPD DRGWHLDALY DPEPGKAGRT YVRHGGFLHD SADFDAEFFG ISPREALGMD
PQQRQLLETS WEALERAGIR ASTLRGSRTG VFVGMCYTGY GFRDQDVAEE VSGYLITGDA
MSVASGRIAY TFGFEGPAIT VDTACSSSLV SLHLAARSLR AGECTLALAG GVAVLSTARG
FIEFSRQRGL AADGRCKSFA ASADGMAWGE GAGVLVLERL ADAERHGHRV LAVIRGSAIN
QDGASNGLSA PSRPAQERVI RDALDSAGLS PADVDAVEAH GTGTTLGDPI EAAALLAVYG
QARPADRPLW VGSVKSNIGH AQAAAGVAGV IKMVQALRHG LLPRSLHIEE PTPHVDWASG
AVSLLTEAQP WPETGRPRRA GVSAFGISGT NAHVIIEQAP EAVTPASGGD GTLPWMLSGR
SPAALRAQAE RLLAHLRSHP LSGADVAYSL AATRDQHEHR AVVLGEDREA ALAALIEDRP
AGGLVRGAAA PDRGRTVFVF PGQGSQWTGM AVELMAASPV FAERMAECEA AFGGLVDWSL
RDVLADPAML ERVEVVQPAL FAVMVSLASL WRSYGVTPDV VVGTSQGEIA AACVAGALSL
EDAAAVVILR SRAIAEDLAG RGGMTSVALD VDEVTTLLRR WQGRISVAAV NGPASVVVSG
EPAALDELYA ELEPAGVRVR RMPVDYASHS EQVESIRDRL LTDLSSITPR AADIPLRSTT
TGEPADTSTF DAGYWYRNLR QTVRFSETVD ALLRDGHTTF VELSPHPVLT TAVQETAEAA
GIEALATGTL RRDDGGLERF RHSAAELHAG GVDVTWPFEG RGVDLPTYAF QHRRYWLEAG
TAARPSLADG LRYRIGWDAL PVAAEAAPGG SWLILATPGD ERAAAISRAL GAEVASGIDG
AALRRHDNVV ALLPAPEVLA LAQALAGGGT RLWCVTSGAV SVNGENVRPE QARIWGLGRV
VALEHPELWG GLVDLPGTLD EQALSLLRAV LGDARGEDQV AIREGRVHVR RLRRAPLGAV
PPTRDWQPAG TVLVTSDGGP AARHVARWLS REGAEHVVLA GAGDGQDELR ADLAQHGTEL
SVVDCDLTDR AELSAMLESF APIRAVVHAA GLARLTPVAG LSGEEFAETI ATKAGVADLL
DDLLDHDLDA FVLFSSVVGV WGSADHAAYA AANAHLDALA RRRRARGLRA LSIAWGLWDF
GGDQAEHRLR GTGFLRPAVA CEALRQAVAH DETDVTVAEV DWDRFVPVFT SAGPRPLLSG
VPEARHLLEP ESTEAESPLR QRLSGLSAAE RHRELLTLVR EHVATVLGFP DAEAVGPKHQ
FKDLGVDSLT AVEVRNRLSA AAGFRLPSTL VFDYPTPQAL AGFLRSAVLG EDERPAGPAP
VAATADEPIA IVAMSCRFPG GVTSPEQLWQ LVDEGRDAVG PFPSDRGWDR SWYDPERGAG
KSYVWRGGFL DGFAGFDPAF FGINPREALI IDPQQRLLLE TSWELLERAG IDPASLRGSR
TGVFVGSNIQ DYAAHVLQGD DLTGGYAGVG NAASVMSGRV AYVFGLEGPA MTVDTACSSS
LSAIHLAVQA LRRGECPLAL TGGVTTMSSP LSYVEFSRQQ GLAADGVCRA FSGDADGTVL
SEGIGMVLLE RLSDAERHGH QVLAVIRGTA VNQDGASNGL SAPNGPSQQR VIQAALADAG
MTVADVDAVE AHGTGTKLGD PIEAQAILAT YGRDRGDAGP LWLGSLKSNI GHAQAAAGVA
GVMKMVLAMR HGVLPRTLHV AEPTPHVDWT AGDVRLLTEA RPWPETGHPR RFGVSSFGLS
GTNAHVIVEE PPAAATVAPQ APADEVVALA LSARSDPALA ALAAALDGPV ATSGPADVGY
SLATTRATLV HRAVVVGGDV RAGLAALASG ADAENVVRGV ARGDAEVVFV FPGQGSQWEG
MCRDLLETSP VFRAELTACS AAFEALLGWS VLDVIRGAPD APPLARIDVL QPALFSVMVS
LAAVWRSWGV TPAAVTGSSQ GEIAAAYVAG EIDLADAARV VGLRSRLLQE HLVGRGVLAS
VSLPADRVRD RLEAFGGALS LAGVNSPTSV TVGGDVAAVE RLVAELTAEG IRARVVPSSV
ATHCAQVDGI RDEVAAVLAP VTARRGTVPF FSSVTGERPA PGTLDGAYWL ANMREPVRFE
DAVRGLLGAG HRIFLEVSPH PTMAVPIQEI LDETVPDAAV LGSLRRNENG RRRMLTALAE
LHVRGVPADW AATFTEGSVR RVELPTYPFQ RSRFWPEYAG RTARPAEENP LGHALLTSTL
PLADGDGLVV LGRLEAGRPW TAGQALPAST LVELSVRAGD EVGCDVLAEL EIGAPLTVPA
DGARRLQLRI GAADAEDRRA FTLHSRADGE AWVAHARGVL AVGAAVPEFD LTEWPPPGAV
PDGARTWRRG GETFAEVRID EEDDRFLIHP ELLASALSAD RIPVRWQDVS LYAARAQALR
VRTVQLAGDA VSVQLSDRFG KPVATLGSVT YGAPRQASPD DSLYGLDLVR VPVPATGPEH
VTVDDLDHLG AVPPLVFLDL HAADARAATA RAAEAVRTWL ADERFADSRL AVVTRGAVPA
GDVTDLVHAP VWGLVRSAQS EHPDRFVLVD TDDSEAPLAA AAAAEPQVVI RDGVVLAPRL
VRIAPPASEP GPFGGEGTVL ITGGTGALAG LLARHLVTAR GVRHLLLVSR SGENAGGAGE
LAAELTAAGA EVRIAACDVA DRAALADLLA TVDRPLTAVV HTAGVLDDGL VTALTPEKID
AVLRPKADAA LALHELTRDL PLEAFVLYSS AASVLAGAGQ GNYAAANAFL DALAAHRRAN
GLPAVSLGWG YWSQASGMTG HLDRGGLTDR MARAGVLPIS AADGLALFDA AVGGTRPVVF
PLRLDHAVLR AGATPLPAVL RGLIRTNARR IVRDEPAAGT SPAERLAGLS RAEQDEALLE
VVRGVVAGAL GHASAGDVTP DMSFKELGFD SLTSVEMRNR LGAATGLRLR ATVAFDHPTP
IAMARFLREQ LFPEPDDLDA ADLSALIDLA LEGGRP
//
