ID A0A372FQW3_9ACTN Unreviewed; 1476 AA.
AC A0A372FQW3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:RFS40480.1};
DE Flags: Fragment;
GN ORFNames=D0Q02_30560 {ECO:0000313|EMBL:RFS40480.1};
OS Micromonospora craniellae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS40480.1, ECO:0000313|Proteomes:UP000262621};
RN [1] {ECO:0000313|EMBL:RFS40480.1, ECO:0000313|Proteomes:UP000262621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63014 {ECO:0000313|EMBL:RFS40480.1,
RC ECO:0000313|Proteomes:UP000262621};
RA Li L., Lin H.W.;
RT "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT South China Sea.";
RL Submitted (AUG-2018) 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:RFS40480.1}.
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DR EMBL; QVFU01000110; RFS40480.1; -; Genomic_DNA.
DR OrthoDB; 5476914at2; -.
DR Proteomes; UP000262621; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 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; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
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 NCBIfam; TIGR01720; NRPS-para261; 1.
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; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000262621}.
FT DOMAIN 100..174
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFS40480.1"
FT NON_TER 1476
FT /evidence="ECO:0000313|EMBL:RFS40480.1"
SQ SEQUENCE 1476 AA; 157414 MW; 67D82C74FE84E23A CRC64;
RGFRIELDEI RNVLEGHEAV SAAAVVALDH PAGGKFLAAY TIASASADEL RAFVEARLPE
YMVPASFTRL DALPVTANGK LDRRALPFPE LGAGRAEGRA PQTPTEQILA GVFEDVLQLS
SVSADDDFFR LGGDSILSIQ AVSRARRAGV IVTAADVFTA RTVAALARLA KQDADAVRLP
ERTNSGLWPI AAAEVDLPGF GAFTQSYTFV TPPGLTEPAL HRILGRVIER HPALSGRLVC
GDRWRFETRA AGPIAAQISV EQEWTDSAVA ELSESLDLEA GVLWRARWYT DGRLLWVIHH
MVVDGVSWRI LGDDLRHAWE LETGRTTEPL SPAGTSLPAW SHALTARAAD TDITDQLAYW
SDVVATDDPL IGSRPLDPAR DTEATAGTVE VLVPVQAVLT DLPSLLSAEV DDVLLGALTI
AIGAWRDRRR VLVGLEGHGR QESLIPGADL SRTVGWLTTW YPVALSSDDI DPAAALHDPQ
AAADVVLRVK EQLRRVPGRG IGYGLLRHLN PTTAAQLAAG AVPQIGFNYL GQFRDDEPAQ
ALAWSGSLDG YAPGELPLAA AVDINVAAVP GEDGLVLDGT VSFAEGISDV RELVDLWSTA
LATLTRYAGS ASHTRRSPSD LTAPALTQAD VDTWEARYGE LTDVQPLTAL QRGIAFETLL
GTDDGAVDVY VTQTVLHLDG DVDPERLRVA LARVLERFPN LRAAITPTGA GELVAVIPAA
VVAPLTTIGT DVPLDAVLDQ DRAAPFELQS APLTRATLRT AAPGRHTLIW TMHHVLADGW
SSPRLVEALL KAYRDPAALA EPDRVYPAFL SWLAARNERA SLDRWSRVLA EVDEPTLVAP
GASITSAVFP DEIELEIGAE RHAALQAAAH AAGATLSTLM QAAWGVLLSS ITGQQTVVFG
AAVSGRPAEV DGIEDAVGLF INTVPAPVTL TGNPTLAEVI ARVQAQNTDL LDHHHVPLAE
VQREAGFSPL FDTLLVYESY PVDDDQLAEV QQDVGIALRE VDGRDATAHP LALSVTPGPD
SAVLELSYRP DVFDRATVER FIAVFERILT AMAETPGVRV AELAFGGVAE VVGAPLEVRP
LTLDGLIRSQ VEATPGGIAV VADDGVQLTY GEFDARVEAT ARALQDRGVK VGDRVAVRLP
RSIDLVVTLA AVVRVGAAFV PIDTAYPSAR VQTILEDAAP ALLVSEPLEG VDGPVVLSRS
LSSLDVAYVI FTSGTTGRPK GVAVSHQAIV NLIAWRQEMF PVGVSDRVLQ KTMVGFDVAV
PEFFWPLAVG AAVRLVKPGG EREPDYLAGI LDGEPVGFVE LVPTVLQAML DVGFQPTRVR
HLSVGGEALP AELGRRLKAV SGVNVWNTYG PTEVAVDSTG VSLSDVDLDG VPVVPIGGPV
ANVRAVVLDS WLRPTPPGVV GELYLGGVQL ADGYVGRPGL TAERFIADGH GERLYRTGDL
VRWNGRGQLD FLGRVDDQVK IRGFRIELDE IRNVLE
//