ID A0A1Q4Z8D5_9ACTN Unreviewed; 1321 AA.
AC A0A1Q4Z8D5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=A6A29_07255 {ECO:0000313|EMBL:OKI43159.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI43159.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI43159.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI43159.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI43159.1}.
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DR EMBL; LWLE01000012; OKI43159.1; -; Genomic_DNA.
DR RefSeq; WP_073721218.1; NZ_LWLE01000012.1.
DR STRING; 1718998.A6A29_07255; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000186952; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19540; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 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; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186952}.
FT DOMAIN 972..1047
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1321 AA; 141338 MW; 723B335A8BDCF28B CRC64;
MIPLSFAQQR LWFIDQAEGP TAAYNIPLAI HLRGSIVPEA MRAALTDVVK RHESLRTVFV
DIDGVPHQQI LDAEAAHVPF RVMESGEEAA RDLLVREAAA PFDLSAGIPL RALLCQVGPR
ESVLSLVIHH IASDGWSTGP LVRDLGIAYA ARCAGAAPEW TELPVQYADY AIWQRDVLGT
EGDPESDLAR QSAYWSKRLA GTPHEATPVT DRPRPAVGSG RGAAVPVRID ADLRRRMAGL
ARETRATPFM VLHAALAVLL REFGTGDDVP IGTVTSGRTD DALHDLIGFF VNTLVLRTDV
SADPTFRELL ARVRETDLAA YAHADLPFER LVELLKPARS LALHPLFQVM LSVHQDADLE
FSVGPLAGRI VPVDVPVAKF DLALSLMERS DGTGAARGID GELRYATDLF DRTTAERMAA
ALLRILDGAT AGPDVPVGRI PVLGPEDRER VLDWGRGPAG PEPDSRGFLG LFEAQVRRTP
TAMAVVHGRT RLSYAELDAR ANSLARLLRR QGVDNGQFVA LALPRGTDAV TAMIGVLKAG
AAYVPIDPEH PADRIAFMLD DARPALLLTS RAVTGLPAVR MPVLRLDDEA TLSRLAQLPA
TPPEGAVQDP RYPAYVIYTS GSTGRPKGVV IPRSALADYV SWCANAYPGM SGVAVVPSPL
SFDLTVTGLC TPLTVGGCVC LASVTEPTDD ELAGVASFPA TFLKATPSHV AILDEAEAGF
SPSGELLLGG ESLSAEMLEN WRVRHPKATV LHVYGQTETT VNCTEYLIRP GQEIPSGVLP
VGRPQARQGV YVLNSALQPA PPGVVGEIHV TGAGLAHGYL NRPGLTAERF VADPFGAPGG
RMYRTGDLGR WNKDGDLEFV GRADQQVKIH GFRVELGEIE AVVAGHPDIG RAAVVMHDVR
GDRRLVAYAV PAEPGDAPDV SDIRTHLRGQ LPAYMVPSAV VVVPELPLTP NGKLDRAALP
QPDPTPSAQH IAPRTPGEAE LCALFAGVLG TGAVGVDQDF FALGGHSLLG IQLMRRIDER
FGVTLRIRDL FEAPTVAGLA RRVADGSRHD TFDVLLPLRA SGSRLPLFCF HPGGGVGWCY
SGLLGRIDPQ IPLYGLQARG LADTAARPGS VEAMARDYVD TLRGVQARGP YRLLGWSFGG
LVAHAVATLL QEAGEEVELL AMLDTFPSSR ITGESEPEGP DPASGPDPAS ADALGQLLTG
LRQARAKSPA SAAVQRQVDA LGAAIGGLDG ITEDELPRVV ETILHHQELR EEHVPRQFRG
DLLYFTANRG RPEDAPTARC WEPFVAGRVS DVPLDCRHGE MMSPTVLDSI APVIHRSLSD
R
//
