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Database: UniProt
Entry: L8EXQ4_STRR1
LinkDB: L8EXQ4_STRR1
Original site: L8EXQ4_STRR1 
ID   L8EXQ4_STRR1            Unreviewed;      2389 AA.
AC   L8EXQ4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:QST82183.1};
GN   ORFNames=SRIM_020315 {ECO:0000313|EMBL:QST82183.1};
OS   Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS   4667 / NRRL 2234).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1265868 {ECO:0000313|EMBL:QST82183.1, ECO:0000313|Proteomes:UP000011074};
RN   [1] {ECO:0000313|EMBL:QST82183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82183.1};
RA   Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Tze-Tze L., Chu J.,
RA   Guo M., Kirby R., Hoskisson P.A., Herron P.R., Hunter I.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QST82183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82183.1};
RA   Algora L., Schniete J.K., MacFadyen A., Hoskisson P.A., Hunter I.S.,
RA   Herron P.R.;
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QST82183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST82183.1};
RA   Algora-Gallardo L., Schniete J.K., Mark D.R., Hunter I.S., Herron P.R.;
RT   "Bilateral symmetry of linear streptomycete chromosomes.";
RL   bioRxiv 0:0-0(2021).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP048261; QST82183.1; -; Genomic_DNA.
DR   RefSeq; WP_003979972.1; NZ_CP048261.1.
DR   GeneID; 66856350; -.
DR   Proteomes; UP000011074; Chromosome.
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; cd05930; A_NRPS; 1.
DR   CDD; cd17652; A_NRPS_CmdD_like; 1.
DR   CDD; cd19543; DCL_NRPS; 1.
DR   CDD; cd19540; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 4.
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; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; 2.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
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}.
FT   DOMAIN          968..1043
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2030..2104
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2389 AA;  253553 MW;  5D5C66D76D1B80DC CRC64;
     MKRSGISDVL PLAPLQKGLL FLSEYDPRSA DAYSLQLSVE LDGPLETGAL RAACAALLGR
     HPNLRACFRR RATGDPVQLV PHEVELPWRE LDLPGADAGQ LRAAADEERG RRFDLARPPL
     MRFVLVRQAE TRHTFIWTLH HSLADGWSLP MLIQDLFTLY AHGGRADGAG LPQAAPYRNY
     LAWLGAQDED AAHAAWRDAL AGLDEPTRLA PVDGRAPVLP DSLTMDVPER LAAGLAARAR
     ALGVTLNTVF QAAWSLVLGA LTGREDVVFG TVTAGRPAEL PGVEAMVGLF ANTIPVRVTA
     RPGQSVAALL ADVQERQSGL MPYEHIGLAD IQRQAGIGEL FDTVMLFQSY PMDEDQLAAS
     LPGLRVADAA IRSVTHYPLA LAVLPGPGTR LGLRFDYAPD LYGPADAERF GRRLLRVLEA
     IAADPEQPLA RISVLEPVEA RLLQEAGDAV ATAAPARPVA EAVEERVREL PDDTAVVCGD
     DTLTYRELNA RANRLAHALV AHGAGPGRTV AIALPRSTGL VVAALAVLKS GAAYLPVDPD
     HPAERNTVVL EDTRPVLALT TTATDGKLPD AGQTRWIMDL PDTAELVAGF PDTDLTDADR
     ARPITADDAA YVLFTSGSTG RPKGVVVTRG GFANVIEDIR HRYALERGET LLSVTTFGFD
     IANTELFGPL VSGARLALAD RETVRDPAAL GRAVTATGAT VLQATPSLWQ ALATVAPDVL
     GGVRGFVGGE ALSEPLGETL RKATASITNL YGPTETTIWS TGAPPLDGVR AGAPAIGFPF
     ANTRLHILDD WLRPVAPGVI GELYIAGAGL ARGYLGRPGL TAERFVADPA DPAGGRMYRT
     GDLVRLGADG QVEYVGRADH QVKIRGFRIE LGEIENALSG HPEIGQAVVA VREARPGEPL
     LAGYLVPADG AAVPEPGALR AYLAERVPEY MVPAAFVTLD ALPLTPNGKV DRKVLPDPEL
     RSRATGRAVR SPQEDLLCQV FAEVLGLPRF GPEEDFFAHG GHSLLAARVV SRIRTVLGAE
     VPVRALFEAP TPAGLAERLP RAGAGAARPA LRPGDRPEDV PLSYAQLRLW FLNRLDGAHG
     TYNISLALRL TGDLDRDALG GALSDLVGRH ESLRTVFPDR DGTPRQHVLP LDEAGFGLRE
     HVTDEERLDG LLASEAARGF DLAREIPLRA DLFRLSATEH VLLLVLHHIA GDGWSLTPLA
     DDLARAYAAR RGGTAPEWAE LPVQYADYAL WQREVLGEED DADSLAARQL AYWKTALAGL
     PEEIELPADF ARPAVAGHEG AEHTAFIGPD LHRALAGLAR AHGVSLFMVV QAALAALLTR
     MGAGEDIPLG SPIAGRTDEA LDDLVGFFTN TLVLRTDTSD DPAFTELLRR VRETDLAAYE
     NQELPFERLV EVCNPVRSLA RQPLFQVMLA FQNTAEAKAA LPGLTAAVHP VGSATAKFDL
     AFQLTERAAG DAAADGEPGG IDLVVEYSTQ LFRPETVRQL AERFTRVLAS VAAAPKAPLS
     SIDVLGDAER RRIVGEWNSA TTEVPERTVA QLFEEHAARQ PDHEAVVFGE VSLTYGELNA
     RANRLARVLA GRGAGPGTLV GLLLPRSVEM IVSILAVLKS GAAYLPLDPD YPADRIAYMV
     GDAAPVCVLA VPGTGGALRD GGTEVIELDG GVGGDARPAT DLTDADRTRP LTCRDAAYVI
     YTSGSTGRPK GVVIEHAGVA ALAADHVRRF GLGARSRVLQ FASPSFDAAT AELTMALLSG
     GTLVLATPES RGPGEPLADL ISRHGVNLAV LPPVVLAAFP EDITLPGELT LITAGEALPP
     EVAARWADGR TLHNCYGPTE STVCATSSDP LTGEGKPPIG RPLANTRAYV LDGRLNPVAP
     GVTGELYLAG AQLARGYLGR PGLTAGRFVA DPFGPAGARM YRTGDLARWT ADGTLEYAGR
     VDHQVKLRGF RIELGEIESA LAAHPGVAQA VAAVREDRPG DRRLAAYVVP EGAPVPAAAL
     REHLSGLLPD YMVPGAFVTL DALPLTPNGK VDRKGLPALD APEAAAHGRT PRTERETLLC
     QVFAEVLNLP EVGAEADFFE LGGDSIRSVQ VVGRARKAGL DLALPDVFRH KTVEALAAAL
     ERAERAAGTT FLDRVRQRLD DPSADAPLDP YGPVLPLRTT GDLPPLFCVH GGMGFALPYL
     GLAGHIGERH PVYGLQASGL TGTGPLPGSI AEVAAEYVER LREIQPAGPY HLLGWSYGGI
     VAHEMAAQLE AAGEEVALLA NLDSYPAEPG EPAPTDAELL TAVLEYCGLE TAANDDGGPT
     PETVRDALRR ADSPLGDLDI PRLVDVMRNH VRLVQEHTPG RVRTPVHLFV AELGLPPEER
     AARPGRWAAH TDGGTAVHPV PCGHEFMMHS GPQAAIGQAV ADELALLHP
//
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