ID A0A117IW63_9ACTN Unreviewed; 1285 AA.
AC A0A117IW63;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=ATE80_16945 {ECO:0000313|EMBL:KUH37658.1};
OS Streptomyces kanasensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH37658.1, ECO:0000313|Proteomes:UP000054011};
RN [1] {ECO:0000313|EMBL:KUH37658.1, ECO:0000313|Proteomes:UP000054011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX01 {ECO:0000313|EMBL:KUH37658.1,
RC ECO:0000313|Proteomes:UP000054011};
RA Zhang G., Han L., Feng J., Zhang X.;
RT "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT kanasensis ZX01.";
RL Submitted (NOV-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:KUH37658.1}.
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DR EMBL; LNSV01000041; KUH37658.1; -; Genomic_DNA.
DR RefSeq; WP_058943056.1; NZ_LNSV01000041.1.
DR STRING; 936756.ATE80_16945; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000054011; Unassembled WGS sequence.
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; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 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; 3.40.50.720; 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; 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; 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; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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:UP000054011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1124..1199
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 131616 MW; B83D8059763E208F CRC64;
MDVVQPALFA VMAALAALWR HHGVHPDAVV GHSQGEMAAA YVAGGLSLQD AARVVALRSK
AIAGMAGRGG MASVTASPER LLPLLAEWDG LISVAAVNGP SSATLSGDPD ALDGLLARCA
AEGVWARRIP VDYASHSPQV EPLRERLAEV LAPIAPRSAK VPFHSTVTGG AFDTRGLDAD
YWYRNLRRTV RFEETVRALL DGGHTTFVEI SPHPVLTFAV EQTAERAAEQ TVERAGGRRE
GGSGRAAVTV LGSARREREQ AQFTASLAAA HAHGVPVDWA VVFDPADARD VELPTYAFAS
TRYWAAPRPA AGDVGDAGLR STGHRLLTAG AERADGGGWL FTGRVSPGTH GWSADHAVHG
TVLLPGTAFV DMAVLAAGHV GCDVVEELTL EEPLPLPAEG AVDLQASVGA PDARGRRPVT
IHSRPADATG GDDWTRHATG FLAPAPAHVD ASPATAAWPP SGADPLDVDG LYDRLADRGF
GYGPAFRGLR AAWRRDGALL AEVDAPTAAD GGGAEGYGVH PALLDAAFHA QLTELADADG
GSGQAWLPFT WSGVRVSRPG ATHLRVSLTP LGEGTVRMSA VDAAGDPVVT VDSVVARPVA
ADRLTGARGP ADRLFRVDWQ AIPAPDPALG PAPGRWAVLA EDGTTLPHPG TGAGTPAGPG
RPAGTGGTGA DAGTGADTPA GSLAPPLPTY RSLPHLTAAL DVGGPVPDTV VALVPAAHGT
PTAEAARARA HHTLALLRGW LADERFAAAR LVLVTRGAVA TAPGAAVAPD LAPLWGLVRT
AQSEHPGRFT LVDLAGDASD DPARVLPGAL AADEPQVAVR DGVLHVPRAV RVRGARGGPL
PFDPDGTVLI TGGTGGLGAR VARHLAAERG ARHLLLAGRR GPDAEGVAEL TAELTGLGAR
VTVAACDVTD RSATAALLAS VDAAHPLTAV VHSAGTLDDG LLEALTPERL DRVLAPKVDA
ALHLHELTAS VPLAAFVLFS SVAGTIGGPG QGNYAAANTF LDSFAQWRRA QGLPALSLAW
GLWEETSGMT RHLGDAGVAR LGRSGLAPLT TDEGLRLFDA VHGTDDALLL PARLDPGALR
AQAREGSLPA VLRALVPAAH VPAGRSGPAL PARLAAAAPE ERYALVLAAV AAEVAVVLGH
EDAGAVDPER PFKDLGLDSL GAVRLRNRLG QVTGLALPST LVFGHPTVSA LTAHLRTLLD
EHAAGAREAA APGVHADLDR LAGLLPSVAA SDVPAVRTRL RSLLTALDGR GGGDGEDGGG
LRRERIDEAS ADDLFDLIDN DLGVG
//