ID D4M3L1_9FIRM Unreviewed; 579 AA.
AC D4M3L1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Amino acid adenylation domain {ECO:0000313|EMBL:CBL25823.1};
GN ORFNames=RTO_11570 {ECO:0000313|EMBL:CBL25823.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25823.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL25823.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25823.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL25823.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25823.1,
RC ECO:0000313|Proteomes:UP000008956};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929055; CBL25823.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M3L1; -.
DR KEGG; rto:RTO_11570; -.
DR PATRIC; fig|657313.3.peg.936; -.
DR HOGENOM; CLU_000022_2_12_9; -.
DR Proteomes; UP000008956; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF10; PHENYLOXAZOLINE SYNTHASE MBTB; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
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 PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 491..566
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 579 AA; 65772 MW; 4507851B8D5B64E6 CRC64;
MMNDREFSNR KETLHGEFYE NALKYPERIA LIYENEKVSY KMLRLYALRA ANYMWQRGVR
RNDKIVVILP RGIGQVAALL GILAIGAAYV PIAMKQPLGR RKKIIENVKP ALVLQDEAFL
EENPWTGCIE NNSKDTAYII YTSGSSGEPK GVEMSHVAAM NTIEEILHMW NIGAEDSVLN
ISAFDFDLSV FDIFGLLTVG GTIVLIDEDD FRDPEVWKNL IEIYGITIWN SAPALLDMFL
IMGENNHFGK LRLALVSGDW IPLYLPEKWY KVTSANSQFV ALGGATEGGI WSNYYCVSKV
DRLWNSIPYG QALPKQKYRI TDENFVECGV DIPGELQIGG GSLAKGYIND EELTMKKFIT
DVKGERWYRT GDRGRRWADG TIEFLGRMDT QVKIRGHRIE LGEIESVLKS ISRIKEAVVV
AQGDKYHKEL VAFYLGEYIA ESEIEDYLKI HLPEYSIPNS INRLENFPLN ANGKVDRRRL
AEYQKTDSVE IMSDKVLNIV LMIWEELLKN KVADLDENLF KIGADSLLAA RFVAAINARC
GIEVRMKEVF MNPSINALTK LVDKRKNTDI AEFVEEGEI
//
