ID A0A0U3Q586_9ACTN Unreviewed; 1658 AA.
AC A0A0U3Q586;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=AS200_25180 {ECO:0000313|EMBL:ALV34972.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV34972.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV34972.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV34972.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP013743; ALV34972.1; -; Genomic_DNA.
DR RefSeq; WP_058924589.1; NZ_CP013743.1.
DR STRING; 1725411.AS200_25180; -.
DR KEGG; scx:AS200_25180; -.
DR Proteomes; UP000068029; Chromosome.
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 CDD; cd05930; A_NRPS; 2.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
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; 2.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
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:UP000068029}.
FT DOMAIN 506..581
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1561..1635
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 580..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1658 AA; 177435 MW; 41CE0F515BFBB5A5 CRC64;
MSPLLPARIA EQAARTPAAV AVVDGDRSLT YGELLAAADR VADVLRARGL GPEDRVGVLL
PRGADLVVAL LGVWRASAAY VPLDPAHPAE RTRWIVADAG LRIVLTDAPH AGVLAADTVP
ALLVGTEDEL PAAPRPAAVG RPAPDPANAA YVLYTSGSTG RPKGVVVTHE AIAGYVDWRI
TTHGLGPGDR VLQRTPVGFD AAGWEIFAPQ ACGATLVIAP PGAERDPVEI VRAVVDAEVS
VLQVVPSILR LLADEPEWSR CHSLRVLTSG GESLHAEDVA AVPATAQVYN TYGPTECTID
VAAHPCDRAV PFGPAPIGRP VTGVRLLVLD PGGEPCPVGV PGELYVGGPA QARGYQGRPD
LTAQRFVPDP YGPAGGRLYR TGDRVRWRED GNLEYLGRLD QQVKVSGVRI EPGEVETAIA
AHPRVTAVVV GAAAGPDGVA RLTAHFVGDV APATLRSFLR ERLPAPMIPS VLTPVDRFPL
LSNGKIDRAA LSSQEPLPAT RPAYLAPRTD AELAVAEVWQ ELLGVEKVGA EDDFFQLGGY
SLLLTRLAQR LTRATGADVG LQDLYTHTTV ADQALLVAPK ADGPGREEPP PITGAPRGGR
LPLSFGQRRM WFLDRLRPGS GEYTVPLFVR LHGRSDPGQV RHALGRLAER HEILRTRYVQ
EDGEPLQIVD PSAPVELRTS ESSHPVREVS AEVARGFDLA AGPVWRALLV RSADGRGNDL
LLLTLHHIAC DGWSAVVLER DIHALLAGDE PTPPPVQYAD YAVWQRQWHT DARTERGVAA
WRDTLTDLVP LELPTDHPRP PVRDATGALV TFDVPAETAE ALVRIGRRGG ATPFTVLLTG
LATLLARRTG QWDVAVGTPT AGRLRPETQD VVGFFLNSLI VRPRLRPEED FERSVRRVEE
ARRFALSHQD VPFDLLVDAY AGERDLSRTP LYQVAFDLHD EQLTGGMSGS DDLAAMREAW
RVAKTDLTVF ARRRPDGSYA FGFEYATALF DRDTVEALAE QFRQLLGRLA AHPELPLRDV
DLLSAAEHER FDAWNRTDAA FGPGTTLSLF ERQAAKTPDA SAVTYSGTTM SYRELDVRAN
QFAGLLKDLG VRRGDAVGVL VGRGLDLHPV LLGVWRAGAA YVPIDPLFPA ERIGHMLADA
RAKVLVSESG YRTLLPETFD GELVLVDLHR ERVEDRPGDP PGPRIAPEDT AYLIYTSGST
GRPKGVRVSH RGLANHLQWA VRDLASQGTT GAPVFSSTAF DLVVPNLYAP LLAGQPVHMA
PRDLPVAELG RVLAETGPFS FIKLTPGHLE LLAHQLGDAA AASLASVIVV AGEALPARQA
EHWRRLLGDG RLINEYGPTE GSVGSTVHPV VGEPAQRIVP LGRPLPGVTV HVLDEVLNRV
PVGSPGELCV GGAGVADGYA GDPARTAARF VPDPYGTPGA RLYRTGDLAR FGPTGDVMFL
GRMDGQIKVR GYRVETGEIE AVLREHPGVR DAVVITAAAG SDASEGPESG DVRLHAYYVP
ADAAVPSAEL TAHAVRRLPD YMVPAAFAPV ELIPLNRNGK VDRSALPRIQ VDDGALADGD
TPTGPAQIRI ATIFSALLGV DPGAHTNFFA AGGNSLAAVR LIARIQDEFD VDLAVRTVFS
GPTVAELAQA VEEAIQTEID HMSDAQLAAA QQEQLEQQ
//
