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Database: UniProt
Entry: A0A1Q4V8X0_9ACTN
LinkDB: A0A1Q4V8X0_9ACTN
Original site: A0A1Q4V8X0_9ACTN 
ID   A0A1Q4V8X0_9ACTN        Unreviewed;      1472 AA.
AC   A0A1Q4V8X0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=AB852_15165 {ECO:0000313|EMBL:OKH94291.1};
OS   Streptomyces uncialis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH94291.1, ECO:0000313|Proteomes:UP000186455};
RN   [1] {ECO:0000313|EMBL:OKH94291.1, ECO:0000313|Proteomes:UP000186455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCA2648 {ECO:0000313|EMBL:OKH94291.1,
RC   ECO:0000313|Proteomes:UP000186455};
RA   Yan X., Huang T., Ge H., Shen B.;
RT   "Cloning and characterization of the uncialamcin biosynthetic gene
RT   cluster.";
RL   Submitted (JUN-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:OKH94291.1}.
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DR   EMBL; LFBV01000003; OKH94291.1; -; Genomic_DNA.
DR   STRING; 1048205.AB852_15165; -.
DR   Proteomes; UP000186455; 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   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 3.
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; 3.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186455}.
FT   DOMAIN          995..1070
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1472 AA;  158336 MW;  9349ACB334AE03EF CRC64;
     MWYACEFGDP TAYNSPVLLR FPRSLDAGLL RRALRHVVAR HESLRTTFAM ADDGRLMLRV
     AAEPDFGFAT ATASGEDALT ALTAEFAGRR LDLRSGPLLH VLCVETGTGG TDGADGMART
     EGADATSGTE GVGGTGGAGG TALLVNVHHA VFDGFSWSVL LNEWLTLYQD LAAGAEFTPL
     PDAPQFREVV TGRTGGPDPQ ASLEHWTKHL AGVPALLDLP LDRPRGPSAA TARAVRTVLT
     GAEAGRLRER AAAEGVTPLM ALLAAYAVLL HRHTGQTDLA VGVPVSLRDR AMDQEVIGHL
     VNTVVLRHRV TSGDTVRELL ARTRREVLSA MRHKDAAFED VVKAVGSGED GGRSPLFRTM
     VTLMPRERRV LGHLGLGVTE WRHVSGAPKY DLALIVEEGA EELGLTFEYD PALFDTATVE
     RIVGRFRVLL ADLLDRPGGT VGELRWVPER ELRELAAVWH GPADDRPAKG SVTDLFEERA
     ARSPDATAVE TVDGTVLSYR RLNTRANRLA RALRLRGARP GTRVGVLLER GPEAVVALLA
     VLKAGASFVP LDPAYPAERV ALMLADSRPR LLLTRGVTDI PCPDGTEVFD LAAEAGRLRE
     LDGTDLPERR RPDDEMYVVY TSGSTGRPKG VAIQDFTLTN VAYRQAELSG PRAASRMLQY
     MSLSFDVSFE EIFGALCAGA TLVLTDEETR TDLHRLAGYL RERRVARMFL PYVALQELAS
     VVVRGNIPLP ELAEVYTTGE QLVVTPALRK MFGRLTDAGL INAYGPSEAH LCTALRLPAD
     PSSWPERPSI GHTVGEVRMY VLDGDRRPVP FGVPGELYVG GRVLSPGYLN LPEQTAERYL
     PDPYDTTPGA RLYRTGDLVK CTPRDGFTHL GRVDEQIKIR GHRIEPAEVE AVLGDLPSVT
     ASAVVAVEHG PGDRRLVAFL RSDPSPGPDG EPEREPDEAA LRRLLGRTLP AYLVPSRFVR
     VVQLPTAPSG KTDRAALAVM AAALPPPRGA VTAERPLTET EQGVARVWGE LLGGAGSGPD
     DDFFGQGGHS LLAVRLRGRL QEEYGVEVPL SALLSQPTVA GMAARVERAL TGDSGPDDAG
     EPDLWADVRL PDSVDVSHGA RPMGPGGART VLLTGVTGFL GVHLLRSLLA AGCVVHCLVR
     AGSTEEATRR VLDSARLYRA DEGLDLSRVR AVPGDLSRER FGLADGVYRE LAGQVEAVYH
     AAAHINFAAP YASVRPTNVD GFVRVAEFCA DTVLKPLHHM STLAVFSPEG PGGYIDEDTV
     PEVAEGLGIG YAQSKWVAER LAMAARERGV PVTVYRIGRI GPDSVSGACR TDDFFWLQIK
     SFLQLGLAPE VPGPPVDLLP ADVVADAVVL LSGAEAAFNR TVHVFHPVGM GWDSVFAALE
     SLGRAPRMVS ADEWLAALEA GPAEDGDRSL ASLVPLFREG VMELADHSYG NDRTVRLLRD
     LGLELPVPEP SWITSMVRYF TETGQVPAPR VP
//
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