ID V6L2E7_9ACTN Unreviewed; 2240 AA.
AC V6L2E7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=N566_06530 {ECO:0000313|EMBL:EST38605.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST38605.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST38605.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST38605.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST38605.1}.
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DR EMBL; AWQV01000195; EST38605.1; -; Genomic_DNA.
DR STRING; 1380770.N566_06530; -.
DR HOGENOM; CLU_000022_53_3_11; -.
DR OrthoDB; 3488622at2; -.
DR Proteomes; UP000017915; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 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; IPR036736; ACP-like_sf.
DR InterPro; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; 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:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; 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:UP000017915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 341..418
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 457..890
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1584..1663
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1718..2141
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 311..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2240
FT /evidence="ECO:0000313|EMBL:EST38605.1"
SQ SEQUENCE 2240 AA; 234919 MW; 3B02B1666B557009 CRC64;
MSETLRPFDA EAALRTLGGR RFATRVTAGD AAVRDHLVHD TPVLPGVFHL DLVLRLVRHL
GVDPGDVELR RCVFIRPLIA VGDLDRQLRV TVAERDARGG LPVTVRSRPV VSGEVAAEEW
QTNFQAEIHP TGPWAPAPVP PGRLETASGA GSLDADDLYG LARQLDIEHG PFMKVQGRVG
AGADFSVADV HLDPSAAEQL GHFFVHPVFM DFSVLVPFLQ FPKEVRRGIV QPFIPIYVDS
FRARRSLQAR SLVHSPQLAN LRVDESTQAV VADIDICTPD GEVAVRLGGY RAKRVRSTED
IRKHAEEGRR LARTAGAPTQ SAVSAAGAPV TAGTAPASAA TPSGGGVGLI ARLVTEQLGH
PITPADNDQG FYELGLTSVD LLTIAGKLET TLNTDLYPTL LFEHPTISQL AAHLEAEGHN
TPHATTPDTT PGTEPPAPPP TPSTNEEGVV GGPAVSVTPM AIVGVAGRYP GARDLEEFWE
VLRNGRDCLG EIPADRWEVE DWYAPEPGTP GRSYLRRGGF IEDVDRFDTL FFNIPPQQAK
LMDPHERQFL EVAWSALEDG GFTPESLTAA ARGTVGVFAG SMWADYHLHG LDSVRSGTAD
VALSWLGGIP NRVSHAFDFR GPSVLVDTAC SSSLTALHQA CESIRSGECG AALVGGVSLS
LHPYKYVRSA ANGLLSKDGT SRPFGEGASG YVPADGVGAV VVRPLADAEA DGDRILAVVR
GSAVNHTGRT AGYTITSPDA QTRVVEEALT RAGVPASTVT LLEAHGAATS MGDQMEINAL
TKTFRQDTAA CGFCAIGSVK ANIGHTEAAA GLASLTKILL CLRHRTLVPA PHSDRPNAAI
DFASSPFRLL RAEEAWPTVS DPASGRPLPR RAAVSAFGFG GANAHVVLEE YVPAPARPAA
DPAPPPHVVA LSARTEAELT QRASDLAGAL RATPSARVAD VAHTLAVGRR HLRERLALVV
TSTADVTDAL DSFVSGRALA VPHFRAAVRG AAARGVPPTA ADAPESTAQA WAEGALGALT
GVPGGRRVAL PSYPFAGGRH WVAPSLRADS VSLPPAPGPV GSNGREPAFG TGVVPLTDLQ
HVMLYEPAWA PRAAPAPSVD LACGPVLVLD TSQDRVQAIR AHNAAVLVTP GSGFARLSAE
HFTVSPDSLE DHKELRAALE GDGLAPSAIV HLWHLDGSDP AGPAHKPTGL LSVYALCQAW
AVGRRTALPV VHAYHSRGES PPDASVGGLA RGLRLEQPKL PLSTVRFAAP SADAAAAAEA
VLGETGSPGD LEVRYTSAGV REVRGFAPVA PTPSGTPLAR AGGTYLLSGG TGGIARHVAR
HMARAAQPNI VLFGRSSEGE GQRAFVAELA RLGARAAYLQ ADVTRLDDVE RLVAEAENRF
GPVTGVIHTA GVVEDGLLIN KKPDSVRRVL APKFDGARNL DLATADRALD YLVLFSSTSA
VLGSIGTTDY TAANAYMDAF TDWRQDLVAR GERSGRSVAV NWPLWSEGGM RINPAVEAQV
LETTGLVPLE TAHGLAALEA GLAHDGPQLA VFEGDRTKVE RMLAVIWPQR VRADGYAPHR
PVKTQHDGAG GEADGAESGV ADVEMASELE AMIAETVTGL LPQTAGLSEE LMSWTFMELG
LSSVDVVGLS RRLGEQLCID LSPTVFFRCT HVPELSAHLC REHAAAVHAW YASFRETMTA
RGDRPEEAAA QAGSVTGAPE SGTPSSDVPA IARRATAGRD VAVIGLGGRF PGAGNPRELW
EALISGRDPV REVPRERWDH SRYLDPDGAA GSTECPAGGF LDDISRFDAA FFGIPHAEAE
AMDPQLRLLL EVLYETAEDA AVLPRLRGSD TGVFVGECFR DYEGEMIALS RKPGPYDATG
IATTMAANRP SYYFDLSGPS LTVDTACSSS LHALQLAVES LRRGECSMAF AAGANLILSP
RHYLSLSGTG ALSPSGRCHA FDEDADGYVP AEAVSAVLLK PLEAALADGD PVRAVIKGVA
VGHNGHAGAV TAPSPQRQTE LIRRAWRDAG VAVQSMGHLE AHGTGTRLGD PIEIDGLRGA
LAGRSSDAPP VLVGSAKAHL GHAEGAAGIV GVVKAVLSLE NGQVPAMPHF QRANPYLDLD
GSGLIVPEAP APWPAHPGTP RRAGVSSFGF GGSGAHVALE EAPQRPRALE TGRSLVLPFS
APSAARLPEV LRRQRAALAQ VHDLAAVAAT MQHGREALPA RVAVVARSVG ELTAELDTLL
GEEVETGTVR SAPGADPAAA
//
