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Database: UniProt
Entry: A0A1I4SGS1_9ACTN
LinkDB: A0A1I4SGS1_9ACTN
Original site: A0A1I4SGS1_9ACTN 
ID   A0A1I4SGS1_9ACTN        Unreviewed;      1033 AA.
AC   A0A1I4SGS1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Amino acid adenylation domain-containing protein/thioester reductase domain-containing protein {ECO:0000313|EMBL:SFM63493.1};
GN   ORFNames=SAMN04487980_1003314 {ECO:0000313|EMBL:SFM63493.1};
OS   Streptomyces sp. cf124.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFM63493.1, ECO:0000313|Proteomes:UP000198530};
RN   [1] {ECO:0000313|EMBL:SFM63493.1, ECO:0000313|Proteomes:UP000198530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF124 {ECO:0000313|EMBL:SFM63493.1,
RC   ECO:0000313|Proteomes:UP000198530};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOUV01000003; SFM63493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4SGS1; -.
DR   Proteomes; UP000198530; Unassembled WGS sequence.
DR   CDD; cd05930; A_NRPS; 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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
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   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450}.
FT   DOMAIN          553..628
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          514..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1033 AA;  109670 MW;  C3BD174BE1EE7734 CRC64;
     MSETNWQVAG AEVDHGPYRP VATLIEEQAD RTPGRIALVH RGETETALTY AEFDALANGL
     AAELASAGVR EGDLVPLMIG NSVELPLCMV ALMKLGAVFV PCDPAWPEER LRTVLQVLAP
     PLALTSGSLV RTDGRSRVVS HRAIVPSTER PGRRPAPDSP VYGVFTSGTT GVPKCAVNLH
     GGLTNRFRFM SRYFAATGDE VVLQNSRHTF DSAIWQLLWP LTTGGRTIVP EQGEFLDLER
     TVDTIARYGV TVTDFVPAIL GMLVALLEAE PAHVARVASL RHLVVGGEEI IPHAVHRLRE
     LVPGLGITNG YGPSEASIGM VFHRVDGTEG DHIPLGRPID NCYALVDAAD ADGIGEILIG
     GACLGAGYVG EPELTAEAFV PNTSPGVPGE RLYRTGDLGR FDDAGLLRFV GRRDRQAQVD
     GVRVELREIE TTAESCPGVI QAKALTLRRS GRTRLVVAAA AEGGTTPAAL RRHLASLLPR
     VQVPRHCFVL QALPLTDNGK VDLRALRTIV EEKLGPGTGS GTGTGTATGA GIGDDAGITR
     AEGIAGLTRG EHAGGLTRAE RLAEVMGAVL DRPGFGVRDD FLDHGGDSLT ALTAVLRIRE
     TLGVRVGISD LHAHRTPAAL ATAVPGDGDA VMPAEDVAAL MERDAELPDD LAALARTAAG
     ARPAPPPRTV LVTGATGFVG ARAVHRLLTA TGARVVCVVR ARDDAHARHR LREALTAQGL
     WDESLAGRLD ARRGDLARDR FGWTRETWEA YAARCDAVLH IGALVNFLLD YRAHRPANVD
     GTTEVLRFAL SGRTKALHHV STLGVLDREA SGARECARDR LGEDFDPARA ATPTSGYSRS
     KWVAERLVLA ARRLGAPVTL YRLGEIMPAA DNGVPNPKAL THLLLSAFHR LGLRPDVPMR
     SDYTPVDEAA ARLVAGLAEP AEGAVHHVFR DGGADFASLA LTEVERAVPV PEFMAALRAA
     AAEDAGSAAA VLDAVLTLLP ASGPDGAPDF RRLLTDNPRL FTRASCTALD ARHGLRERPL
     EAAVAAYRTT LTQ
//
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