ID   A0A0F2SC97_9FIRM        Unreviewed;      1438 AA.
AC   A0A0F2SC97;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=VR66_13260 {ECO:0000313|EMBL:KJS48559.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS48559.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS48559.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS48559.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-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:KJS48559.1}.
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DR   EMBL; LADV01000157; KJS48559.1; -; Genomic_DNA.
DR   PATRIC; fig|1629714.3.peg.115; -.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd05235; SDR_e1; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; IPR020459; AMP-binding.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
FT   DOMAIN          961..1035
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1438 AA;  164041 MW;  0FABC104D8DD3BE9 CRC64;
     MRMYKLYPLT NAQKSIWVAD NLYPGTSQAV SSTTAVIREV IDFTLMNEAI NIVIKHNDAL
     RIRLVNQNGT PQQYFSDFVK KQFDVLDFSY DHGENDYKQW EKKMVETPFN LVNSELFYFA
     LIKLSEKKNI CFFKFHHTII DAWGTALVIR KMLKEYWQLK YNSLSESHDE EFSFVHHIND
     ELQYMATPRF EKHMEFWSGV FGTVPEFTSF TDNKGITSLV GKRKSYILSE LISSKLNSFC
     ELNKVSAFSV FYALLALYLS KRSNKKDIAI ETPILNRSGK TEKNTVGMFM HNIPVRIYVE
     PSLDFLAFVN EAFRELKKFM RHQRYPYSSI LKDFREKQQF SGTLVDVTLN YHNLKLDSVI
     EYEAIWNYPG AQSNSLSICV SDRADTGLPE LDYDYLLEAF SEEDIDQMHN NLCNLLTDAL
     ENPSKRLYEL QMLSQDELIK LLLGFNQTEL AYEAKSVSEL FEDQVIKSLD STAIVFGDQR
     LTYRELNEKA NQLARYIRGK GMSCNSIVGL LVDRSLEMVV GILGILKAGA AYLPIDPAYP
     RDRIAYMLNQ SNTRLILTDK NNPNSSTFKN CVFANISLSN IAVYNSDTAN LEKDINHNTD
     DLAYVLFTSG STGKPKGVMV HHRALCNLIN SVARNLNFES QTIVSLTTIS FDIFFSDTIL
     PLTKGLKVII ANPEEQTMAK YLFALISKHQ VKVLQATPSR MKLILSEEQG RECLNDLSHI
     LITGESFPAP LLPQLKSVTQ AEIYNLYGPT ETTVWSTMAN VTHSEKITIG KPIANTQIYI
     LDDHLSPVTM GSVGEIFIVG DGVSLGYLAN PELTKERFLA NPYIAGYTMY RTGDLGRWLK
     NGDLECLGRT DNQVKIRGLR IEMEEIEVCL LEHTSVKEAI VMVREDKAGK RHLCAYLTGE
     KRLSHESLRS HILKYLPNYM VPACFIWLDA IPLTPNGKIN RRDLPLPNEL ELEQLTHAYI
     APRNDVEWKL AMIWAEALEV ERVGIDDNLF ALGGDSLTIL EIMAGALSYE WKLIAQDFYE
     CPTIGLLSSK ITGCSQEDKE SEEEVYLSDR VWPTEVTIKP MDIGNVLLTG STGFLGIHLL
     WELLDQTKNI IYCLVRGNQA KVKLDKLLSF YFPSLSVTLK NRIIVVNGDI SFEQFGLDDN
     SYKDLSQKVQ TVIHCGALVK HYGNYREFEK NNVQGTREVI DFCLKFDKKF NHISTISISG
     DFVVDLSKGK TVFSEKDFYL GQDYKTNVYV RSKFAAENQV FQAETEGLRF AIFRIGVLTG
     RYWDGKFQHN IAQNAFYRKI KSLVALRVVP ESFFDQSIEF TPVDYCAKGI VNIIQVNQAR
     GLVFHMFNHQ EIKAIELLSY LRELNMSVQT LSNQEFDVYI RQLSQTKEGK ETLSGLVSDL
     SVNKRLNYSN VITVDSTFTI NYLVQTGFVW SEIDVEYLSK IVSYMREVGF INDSISLA
//