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Database: UniProt
Entry: A0A2X0IJ23_9ACTN
LinkDB: A0A2X0IJ23_9ACTN
Original site: A0A2X0IJ23_9ACTN 
ID   A0A2X0IJ23_9ACTN        Unreviewed;      1091 AA.
AC   A0A2X0IJ23;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=DN069_13375 {ECO:0000313|EMBL:RAG85114.1};
OS   Streptacidiphilus pinicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=2219663 {ECO:0000313|EMBL:RAG85114.1, ECO:0000313|Proteomes:UP000248889};
RN   [1] {ECO:0000313|EMBL:RAG85114.1, ECO:0000313|Proteomes:UP000248889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS16-CNU450 {ECO:0000313|EMBL:RAG85114.1,
RC   ECO:0000313|Proteomes:UP000248889};
RA   Roh S.G., Park S., Kim M.-K., Yun B.-R., Park J., Kim M.J., Kim Y.S.,
RA   Kim S.B.;
RT   "Streptacidiphilus pinicola sp. nov., isolated from pine grove soil.";
RL   Submitted (JUN-2018) 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:RAG85114.1}.
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DR   EMBL; QKYN01000051; RAG85114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0IJ23; -.
DR   Proteomes; UP000248889; 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   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; 3.30.559.30; 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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
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; 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   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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:UP000248889}.
FT   DOMAIN          1012..1088
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1091 AA;  117074 MW;  E0EC8B31500F35D8 CRC64;
     MAKAEAAGAR LELSDLLGER PLAEALESAQ AVIRQPLAAQ HESVGPDERV RPCTSREASM
     LISEQMGAGT GWHLLFSADI RGGLDHQRLH SALQALTDRH PALRTVFSPE QMTARVVRNH
     RVRLLTCDLD LPGDDAVGAV NAMVGQSSAR LLDPFVRPPV AFQLTRVSPE RHVLSMLIHH
     AVADGWSVGV LWKELFDRYA AGSDESVGEA AVVPAVVASY EDVIERRVPE LKGVPTVLEL
     GGDLERPEVF DYRGLRLPFR LRADEVEGCE RLASSLGVTR NAVLLAAWSL TLARQASVDD
     LLLGLTWAGR ISEAERGLVG LLTDVLPIRC AVDGDIATAE FVQRIAREMR SALSARKAPF
     EEIAKTLGAD YDATRNTLVQ FAFAAHDELV SEQMSLPDLD VTIHEGHCLG TVFDSVLYVR
     RWGDDAELCL EYATSVVAPG EAAHLVSGFR EVLRGFVSRS EHGTRIGELS AGHEGASQWD
     PRRQSARAQV QEEAGLAGLW QMFESMAASR PDEPAFAESA RGTLTYRQIA AAAVAQSEAL
     RAAGVAEGDH VVLALPYSAQ ELVAVLAVLR LGAAYIGLDH AAGAAHIAHV QQIARPVLAI
     APQPRAKELE HDGLSAPVLE PVDPWNPPVP AVVGAAAAPD PDRIAYVAFT SGSTGRPKAV
     RVPHRGVLRL VHDTDVVRPN ALRRFLRVAP ISFDASTLEL FAPLAAGGCI VAFPEPYPVP
     TVLARFIEQE RISGLWLTAG LFRLVAEHAP TAFRGVDQLL TGGDVVPSGQ VRRVLEACPG
     LRVTNGYGPT ENTTFTTVHH VDDTTAVPAR LPIGAPVAGT TVIVVDRALR AVPEGAAGEL
     LTGGAGLAVD YLGDAEETRR RFVELEDGQR YYRTGDVVRW GADGTLRFLG RVDRQVKIRG
     FRIELEAVEA ALRAAPGVLD AGAYATAEQA GESRILVGVA GGDSHLDLDA LRDFVAARLP
     AYAMPSLWAV TDALPVTRNG KVDVQALLAK ATNRAEEPRA AARPQDSAES GMTAEEIEDV
     IAGIWEDVLG STDFGYEDRF FDVGGDSLRV PQVRRALLSA FPGCAIQMVE MFNRPTIAQL
     AVLIEGRLAA S
//
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