ID A0A0L8MBT5_9ACTN Unreviewed; 1535 AA.
AC A0A0L8MBT5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE Flags: Fragment;
GN ORFNames=ADK74_10150 {ECO:0000313|EMBL:KOG47853.1};
OS Streptomyces decoyicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG47853.1, ECO:0000313|Proteomes:UP000037606};
RN [1] {ECO:0000313|Proteomes:UP000037606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Winegar R.A.;
RL Submitted (JUL-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:KOG47853.1}.
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DR EMBL; LGUU01000093; KOG47853.1; -; Genomic_DNA.
DR PATRIC; fig|249567.6.peg.2190; -.
DR Proteomes; UP000037606; 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 CDD; cd17652; A_NRPS_CmdD_like; 1.
DR CDD; cd19540; LCL_NRPS-like; 2.
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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; 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; 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; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
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}.
FT DOMAIN 1010..1085
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 627..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOG47853.1"
FT NON_TER 1535
FT /evidence="ECO:0000313|EMBL:KOG47853.1"
SQ SEQUENCE 1535 AA; 165975 MW; CD2F43FF86C61DA3 CRC64;
ELAVRDLFEA PTVAGLATRL HHATGARTAL EPRLRPDHIP LSHAQRRLWF LHQLEGPSAT
YNVPMVLRLT GALDTTALHE AICDLTDRHE SLRTVFPETD GTPRQQVLHG DAARPTVEVV
TTDAEDLAEH IATAARHAFR LTDELPLRVW VFTTGALEHT LLILAHHIAG DGWSMGPLAQ
DLATAYAARC DGNVPQWAPL PVQYADYTLW QREVLGDESD PDSVISRQID YWRSTLAGLP
EQLELPTDRP RPAVATHQGD SVPFTWGTEL HHGITRLARE HQVSVFMVVQ AGIAALLTRL
GAGTDIPMGS AIAGRNDDAL DDLVGFFVNT LVLRTDTSGD PTFSEVLGRV RETDLAAYAH
QDVPFERLVE IVNPTRSLAH HPLFQVMLVL QNAAEGEFAM RGLVATEDDD VHAGIAKVDL
TFSLGEQFGA GGEAAGMRGV VEFATDLFDR RTAETIAARL ERLLRNAVED ASRPLGELEV
LSVEERELLL HGWNDTARDV SDATLPGLFE AQVARTPDAP ALEHHGARLT YTELNTRANQ
LAHHLISKNI GPEQIVALAL PRSADLIVCI LAVLKTGAAY LPVDPDYPTA RITYMLDDAR
PALVITDSNT AGLPDTGLPT LTLHTDTGTD TGTGTGQLTI NPNDTHRSTP LLPTHPAYLI
YTSGSTGHPK GVAVTHDAVN GFAADGLGRW QLDGSSRVLQ LASPSFDPSV LEMWMAFRSG
GCLVVAPTGP LAGEELVGVV DGLRISHAVI SPAALASMPV HPLPTLRTLI IGGDAFTGEV
AARWSSGRRM FNAYGPTEAT VWVTSSSPLS GAVAPSIGRP GWNTRVYVLD SALRPVPVGV
PGELYVAGTR LARGYLRRPG LTAARFVADP FGSPGGRMYR TGDLVKWRAD GELEFVGRVD
NQVKIRGFRI ELGEIQNVLA THPGVGRIAV VVREDRPADK RIVAYVVPME GADGRVDLAG
LRDRAAGALP EYMVPSAFVQ LDTLPLTPNE KLDHKALPAP EYTGTEGGRG PRNAQEEILC
GVFAEVLGVP RAGIDDNFFA LGGHSLLAMR LVSRIRSAFG VELAVRDLFE APTVAGIAGR
LGTAAGGRTA LVPMERPERV PLSYAQRRLW FLHQLEGPSP TYNVPMRLRL SGELDTAALR
EAMSDLVERH ESLRTVFPEI DGTPYQQVLE GSAARPPVEC VRVEPAQLDE VIRQAAGHAF
DLTAELPLRA WLFRTGPDEH VLLLLAHHIA SDGWSIAPLA QDLAVAYAAR SKGAAPQWAP
LPVQYADYTL WQREVLGDES DPQSLISAQV DYWQQHLAGL PDLLELPTDR PRPAEAGYQG
DSLDFFWDVE LHEGVARLAR EHQASVFMVV QAALATLLTR LGAGTDIPLG SPTAGRADEA
LDDLVGFFIN TLVLRTDTSG NPSFADLLGR VRETDLAAYA HQDVPFERLV EIVNPTRSLA
YHPLFQVMLS FEAASADVPL DGVDSRLESS GSDTSKFDLE FGLEEKVTAD GLPAGMAGTV
DFATDLFDRQ TAEAMAVRLE RLLRAAVADA SQPIA
//
