ID A0A0M8USI6_9ACTN Unreviewed; 1595 AA.
AC A0A0M8USI6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=ADL00_45650 {ECO:0000313|EMBL:KOV49503.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV49503.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV49503.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV49503.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV49503.1}.
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DR EMBL; LGDU01000424; KOV49503.1; -; Genomic_DNA.
DR RefSeq; WP_053764257.1; NZ_LGDU01000424.1.
DR PATRIC; fig|1519489.3.peg.10313; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000037758; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic 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:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR PIRSF; PIRSF001617; Alpha-AR; 6.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037758}.
FT DOMAIN 982..1059
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1107..1184
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1081..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1595 AA; 170312 MW; 3A4B836F62C35E52 CRC64;
MTSHDEAQLP TYPMSFEQES IWLQDQFHEV GAGQGDDGPS RPSRYLESLV HRLHGPVDTS
ALESALTALV AHQEGLRSAF RSVDGALVQQ VFPPMLLPVD ERRVRPDELE DALAAAITRP
VPLDRPPLLR ATLLRTGPED SVLALVGHHA VMDSWSSRLL EEQISEGYRA AVEGRPARLP
EIPLQLGPYA QRQREDDAVN SPVHLEHWRT VLADAPVEST FPGDRPRSAV PSHRGGEIRF
TVDGATGTAL RALARAERAT PFVVLLSAWT TLLNRFSGQD DVVVGTPFSR RNGTEVKSLV
GCLTDVMPVR QRFGDGCTFR EVVASMKAGV WSAIRHRHIP YGHLVREFSP ERVLGRFPLF
QVMFTLDDGL GEGLSLPGVV SERDHGHSGR SKVDLLLNLV TDGDGYRGYL EYAHDLYDTA
TAQRIADRFA TLLRDAIHRP DAETADLRLV TEEEEARTRA WAQGPLPSVT PPLAPSVVRP
HALVAPNRPA VVHADVTLSY AELDARADRL AASLTARGHT GARIGVCMDR PADHTVTVLG
VLRAGAACLP LDPGQPAERT AFVLRDADVR VVLSDPAHAA ALRAEHPGVT VLTHDALSPA
AAPGTALPEV SGDSLAYVLY TSGSTGRPKG VAMTHRGLAN LIAWQRRDSV CRTDARTLHF
APLTFDVAFQ EIFATWAAGG TLVVADAAAR KDPLCLLALL RDQRVERLVL PFVALQQLAE
HAVAEGQVLE HLREVATSGE QLYVTPALRA FFGWLTRADL QNQYGPTETH VVTALRLTGD
PAGWPDRPGI GRPIDGARVD VRDRALNPLP VGVTGEICVS GVPVAQGYLG HAADADDGFT
TGPDGERLYR TGDMGQWLPD GELAFLGRED DQVKIRGYRV ELQEVEAALK QVPGVADAVV
VAVPGETSAS TWLAAHYIAA TGAKVSPPAV REALRDRLPA HLVPAAIESV TAFPLTASGK
ADRAALARAL PAPAPLDAPR PVAGTATLER MADLWARLLR RDAGTVGPDD DFFHLGGDSL
LGAQLMLQLR EEFGVRLGLD AMYNAPTITG LAALVDAGTV TRRPGAVSAP TLPADIVPAA
SREAGGGEPA PEPTRTPPAP ASARRPAEGP ETLQRMADLW ARLLRRDAGT VGPDDDFFRL
GGDSLLGAQL MLQLREEFGV RLDVESLYEE PTIAGLAALV DTGAGTRRPD ADAEAAMHRP
DAETAPTAQT DGVPTQVTPE PAPLRHVLLT GATGFLGAFL LRELIDRTDA RVHCLVRARD
DAHALRRLEE SARGHGVWTP EVAARTVALA GDLGKPALGL DPAHHDELAR TVDAVYHCGA
AVNLVLPYAE LEAANVTGTV GVLRLAALHR TVPVHHVSTV GVYSGAHLAG SPVTADEPLP
GVDGLHLGYA QAKWAAECLT AQARERGLPV SVYRPTRIAG DTESGVCRPD DFLWLLLKGC
VEAGGYPADL GVGFDLVPVD YVSAAIVALS LDAEPPRAAH LAHGAELSLR EAVDRLAGLG
YRLQPLPTAE WTRRIEADPH NAAFPLIGLM APETVGSQAA ALTFDGSAAQ TTAAAHGVVL
RPVDRAAFAR TVDYFARTGF LPAPSGTPRS PRQTS
//
