ID A0A0S9ND95_9BURK Unreviewed; 1288 AA.
AC A0A0S9ND95;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=ASF44_06720 {ECO:0000313|EMBL:KQP43253.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP43253.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP43253.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP43253.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP43253.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP43253.1,
RC ECO:0000313|Proteomes:UP000051759};
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 -!- 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:KQP43253.1}.
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DR EMBL; LMNA01000012; KQP43253.1; -; Genomic_DNA.
DR RefSeq; WP_056900070.1; NZ_LMNA01000012.1.
DR STRING; 1736318.ASF44_06720; -.
DR OrthoDB; 6297021at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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: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 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; IPR020802; PKS_thioesterase.
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 SMART; SM00824; PKS_TE; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT DOMAIN 976..1051
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1288 AA; 141388 MW; D7C5C1AF2A688A17 CRC64;
MDTTVIDADP SAEAERREGL ALSLSQREVW LDQRAWPGSA HLNIGGGAFL VGLLDLTVFR
RALARLVAEN EALRLAPLPD GRQHLLPPTE EPALEVVDLG DAEDPKEAMR RWWQQRMTEP
FVLDGRSPWR FALLRASDQL HGLTIQFHHL VMDGWGTSQV MRRWAEIHNA LLAGEPPPAS
SVPHYSAFIA ESNAYRGSEG FERDKRYWRE RIPELPTPLI ERRFSQARPD TLPPASLAFH
RVPRADYERL RRHATEQGQT VFNLVLAALV LYFARICERS DVIVGVPSLN RGGRRYTDTL
GMFVGVVPIR IQITPQMQVG ELIASVGASM RAALRHPRYP ISELGRELQM IRANRDGLFD
VLLSFERQDY AVSFGAAQLV ESRQLFSGVA RFPLGVTVCE FHPTQDVELA LEASAACFSS
GETELLGRRL WHLVEAIMDT PPDGTVDSIE LLPPEERWHV VSGQHKDVAW HQVVLPFVNL
FEYQAALRPE AVALVWDGGA MDYLALDRHA NRLARKLLEL GAGRDVVVAM ALERSPELVV
TLLAIAKAGA AFLPLDVDAP LARLGAILQE SGAALLVVQP RHAERLGGLH GNTLVLDPLG
DEVFDANATD LPPRRPAASD MAYVLFTSGS TGRPKGVTIE HGMLSRRLMW LSRAWAVDAR
DRSGQGTQAT FDPSLIELLL PLIHGASVAL PPPGRLLPEM LAEFALRHGV TFMAFVPSTL
VRFLDAAAGR SGLKLRVACC GGEVLPPELA SRFISVTGGR LFNVYGPTEA TIFATAWECE
AQRSHAALPI GRPIDDTRIY VLDAGLRPLP LGVAGEIFIG GAAVARGYLH RPELDLLAFV
ADPFHPGERM YRTGDRGWLG SDGHLHFVGR LDRQVKLRGY RIELGEIESA LLAIDGVVQA
AAALRELRDK PAIHAWVQAP GQSAERLHAL LRARLPDYML PASITLMPEL PSSSTGKIDY
KQLPDPVAQP GGASRAPLND TERALLALWK DVLKVPTLGV QDNFFDLGGD SLAAVNMMSG
LEKLLGRQVP LYLITEHPTV ESLSAALQQH SATPGLLLPL GGTGRVPLYL AASGHGDLLR
LQNLGPALGE ACSLYMLQPP PGEPVKTIAE LAAMYADRIQ AQSLAEGFDG GWVAGFSVAG
MAALETARLL RERGWPVRGL VLLDTTYPSS VLGGTRAWRA AGWMVRHFHI QDLTMNGRRL
DAMFNDPGLV SQVMALRGYK PVAYDGPTLL VRTSGLRTWD RWLFKPWRRL MGHHLQEVEI
AGMHGTMFDE RHVAELAAAL RARMEPRA
//
