ID A0A0Q8NRY0_9ACTN Unreviewed; 1315 AA.
AC A0A0Q8NRY0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=ASE03_05490 {ECO:0000313|EMBL:KRB63997.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB63997.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB63997.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB63997.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB63997.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB63997.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KRB63997.1}.
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DR EMBL; LMHX01000034; KRB63997.1; -; Genomic_DNA.
DR RefSeq; WP_057234216.1; NZ_LMHX01000034.1.
DR STRING; 1736486.ASE03_05490; -.
DR Proteomes; UP000051829; 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:0019752; P:carboxylic acid metabolic 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; cd12116; A_NRPS_Ta1_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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; IPR006162; Ppantetheine_attach_site.
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.
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:UP000051829}.
FT DOMAIN 964..1039
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1315 AA; 142189 MW; 7B056E3F3F006FB7 CRC64;
MTLGDIVDAY PLTRLQSGML YHSLLDRDTP TYHDISAIRL AGRFDRAALD EVFAGVIARS
DMLRSSIDLT NFSEPMQLVH SAVPTPLTVE DLRGLPAEDQ RRRAAEWTAT EKATAFDLAV
APLLKLHVLV FADDDFQLNL SFHHAILDGW SLSLVTSQLL TGYDARLAGR ATELEAGGAT
APATRFRDYL ALEQQALAGQ EARDFWARTL SDTEFTGLPR YPDQDLAAER TAQVYEVPLP
ADLTAGLRAV AARAKVPVKS VMFAAHARVL ALLSGSTRVV TGRVSNGRPE TADGDQVVGL
FLNTLPLVAE VAGVSWIELA QQIHRQESEA LAHRRYPMAQ LLQDLRRPEL FEVVVDHRSF
RSYDMTLEQI AITGGEFFEQ TNFPFTANFG TDPATGEVRL RFNYDRAEFS AGRITEIGGY
YAAALAALVA EPTAPAQAAG LLADEQLTRL VSGWNDTAAP RTPGQTLPEL LARRAAEHPD
AVALRAGDTV LTFAELHARS NRLAWRLREL GVGPDVLVGV HLARSADLIV SLLAVLKAGG
AYVPLDPGYP SERLEFMLAD AEVSVLLADP ELIGELDPAG ARVLAVDAAA TAGYPEHEPP
LAVTPDHLAY VIYTSGSTGR PKGVQIPHGA LLNLLQSFER DLEITDRDRL LAVTSLSFDI
AGLEVYLPLM VGAELILAPD IAVDGPRLRS FLETSGATVM QATPSSWRLL VEAGLRADPA
LRVISGGEAL PADLAAELTA RFPVVHNAYG PTETTIWSCL QRVLPGAPVT LGGPIANTRV
HVLDQTFGLV PEGVPGDLWI SGDGLARGYL GRADLTADRF LPDPFAGTPG ARMYRTGDVV
RRLPSGELEF LGRSDHQVKV RGFRIELGEI ESVLARHPGV GRVVVVARED QPGDKRLAAY
LTPVGDAPTT AELRAAVAAE LPDYMVPSAF VVLDAFPLTP NGKIDRNQLP APGREESAAG
AFVEPRTATE RALAEIWSDV LGVERIGVTD AFLELGGNSI SALRVIMRLP DITEVELPVA
ALFEGGTIER IARIIDGEQE VVNSVVVALR STGSKPPIFF VHPLGGSVFS YAELVEALDP
EQPFYAVQAP EYAGPDVPRP DTMEGIAALY LSELRAIQPE GPYHLGGWCM GGMISYEMAR
QLQAGGEEVA MLTIVSASID DPVPPRYVTS ESAAILGAFG HKLPTTEAVL EAMDEDARLR
YVIQLTHGTD DERADAATVD DLRRLVRLYQ RHARALITYR DTPREPFRGD ALLIRAETEL
FTGWDFGWKE RVDGRLLIDE SPGNHFSMLE QPNVPKVAAR IEAAAAGQPS GVVAE
//
