ID A0A101SJK6_9ACTN Unreviewed; 1862 AA.
AC A0A101SJK6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE Flags: Fragment;
GN ORFNames=AQJ66_35885 {ECO:0000313|EMBL:KUN75384.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN75384.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN75384.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN75384.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:KUN75384.1}.
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DR EMBL; LMWX01000093; KUN75384.1; -; Genomic_DNA.
DR STRING; 285568.AQJ66_35885; -.
DR Proteomes; UP000053024; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.50.11460; -; 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; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1700..1775
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUN75384.1"
SQ SEQUENCE 1862 AA; 194681 MW; E53DB5D3B37BA6F6 CRC64;
EVPQTETDTD SAETDVPSAS VDDRTVLLPL SAADPRALRE QAERLVSLLS SDSELSPRDV
GLSLATTRSA LEHRAVVLAA DREQALRGLQ ALVRQEPVHH VVTGTAKAGA DRTAFLFAGQ
GSQRLGMGRE VYDTYPVFAE AFDAVDAELP FSLREVVFGE DEGALNRTEF AQPALFALEV
ALFRLLESWG VRPDVLLGHS IGELAAAHVA GVWSLADACR LVAARGRLMQ ALPEGGAMVA
LQASEDEVLR LLAGRETEAG IAAVNGAEAT VVSGTARAVE EIAAHFRAED RRVTALRVSH
AFHSPLMEPM LADFRKVAES LAYDRPRLAI VSTLTGDLAD PDALMSSEYW VRHVRHAVRF
ADGVRRVRAE GVGNWLELGP DATLTALVRA ETGTGRAAEE PLYAPVLRKD RDEVAALLTA
VAALHTRGTA LRWPAVFAGT GARRTTLPTY PFQRQRFWPG APSAAPGDAA GLGLTASGHP
LLGAEVTLAE GPGTLLTGRL SLAAHPWLRD HAVAGAVLFP GTGFLELALQ AGRQVGCGRV
AELTLEAPLV LPDSGGVRIQ VAVGGPDGAE RRTVSVHSRS DAPGAAPDPW VRHATGFLDE
GDDASEPEGH DTEGRVCRPP ADADRVPLDG FYERLADDGY VYGPAFQGLR AVWRQGDDVY
AEVRLPADRQ DDAGRQGLHP ALLDAALHAW LAARPPAAHG SGAVRLPFSW SGVTLSAVGA
SAVWVRLTPV DEDTLALSLA DAEGHPVARV DALTLREVDP AAQATAESAR AETGNALFAL
DWSALPAPAG ALPAQAQRWA VVGPPIDGLT DAPAGHYPDL ATLAAAVAEG TPVPDSVLVA
CGGAARPAGP GPDTPDAVDT AKGVDTVGTA DAVDAARPSH FTTASADTVD VAHPSHLRTA
TADTADPSHL PTNSADTVEA TRAALHDALA LIQSWLADDR FTAARLVLVT RGAAPVGGDR
APTDPVAAAL WGLVRSAQSE HPGRLVLLDL APEDTGRAGD TPLTGLLAPS AGQSGDSGRA
HPAGPADPAH ALATGEPQLA LRGGTAHVPR LAPAHTGSPL LPPPGEAAWR LDVTAPGTLD
NLALVACPEV TGPLAPGEVR VAMRATGVNF RDVLVCLGML DREVPGREGA GVVLETGPGV
TGLAPGDRVL GLFSGAYGPV AVTDHRLLAR VPEDWSFTEA AAAPIVFLSA HHGLVHLADL
CPGESVLVHA GTGGVGMAAV QLARHLGAEV FATAAPAKWP TLRAMGLDDD HIASSRDTDF
EQKFLRVTAG RGMDVVLNSL ARELVDASLR LLPRGGRFIE MGKTDLRDPR VVAAEHPGVV
YEAFDLRDVD PEHTAEMLTA VLDLFAQRAL RPLPVTTWDV RRAPEAFRYL SQARHTGKIV
LTVPGVPLDL TRSAVAGPAA AERTHGDGTV LVTGGTGTLG ALLARHLVTR HGVRRLLLTS
RRGPDAPGAH DLAAELTGLG AEITVAACDA ADRQALAELL ATIPGDRPLT AVVHAAGVLD
DGILDGLTPD RVDRVLRPKA QAAWNLHELT RDRDLSAFVL FSSVAATFGS QGQANYAAAN
AFLDGLAHHR RAQGLPALSL AWGLWDTDTG MAGTLGEADV RRVGRLGLAP LPAEQGLALF
DAALAADRAL LLPTRLDLAG LERRGAEPPA LLRNLARIPV RRAAAPAAAT AGGQDGADGE
RGTVPFTEQL RLLPAAERER AALDLVRTHT AAVLGHADPE SVDSDRPFKS LGFDSLTAVE
MRNRLGTATG LTLRATLIFS YPTPAVLARH LLEQCAPQEA RPADVLLAEL DRLESAMAGL
DRTTDGTPDG GAADDEVTTR LRDLLLRWTG GSSHGTTTAG TGLESATDDE MFDLIDKELG
IS
//
