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Database: UniProt
Entry: A0A1E7JRE5_9ACTN
LinkDB: A0A1E7JRE5_9ACTN
Original site: A0A1E7JRE5_9ACTN 
ID   A0A1E7JRE5_9ACTN        Unreviewed;       969 AA.
AC   A0A1E7JRE5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE   Flags: Fragment;
GN   ORFNames=AN216_25440 {ECO:0000313|EMBL:OEU90847.1};
OS   Streptomyces oceani.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU90847.1, ECO:0000313|Proteomes:UP000176101};
RN   [1] {ECO:0000313|EMBL:OEU90847.1, ECO:0000313|Proteomes:UP000176101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU90847.1,
RC   ECO:0000313|Proteomes:UP000176101};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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:OEU90847.1}.
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DR   EMBL; LJGU01000160; OEU90847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7JRE5; -.
DR   STRING; 1075402.AN216_25440; -.
DR   PATRIC; fig|1075402.3.peg.5563; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000176101; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd08952; KR_1_SDR_x; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 6.10.140.1830; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041618; PKS_DE.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF18369; PKS_DE; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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:UP000176101};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          810..885
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          932..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OEU90847.1"
SQ   SEQUENCE   969 AA;  100906 MW;  07AD5DB0A75D1F6D CRC64;
     EASEAEVASL LVGRADEVGV AAVNGPSSVV VSGVEAAVTE IGERFRARGA RTRRLSVSHA
     FHSPLMEPML AEFRRVAEGV AYGRPSLSVV SNVTGELATV EELTDPEYWV RHVREAVRFA
     DGVAALTAQG VTRFVEIGPD GTLTAMARGC VEGEASGGEL SFVPLLRKDR PEVESVLAGV
     AGVFVRGQQV DWSAVLPEVP TVPGTDRVDL PTYPFQRERY WLSQRRPDPV TVGHSAELDA
     PFWEAVERDD LDSLSGELDI DQDAPWREAL PALASWRQRR RAESEADAWR YRVSWEPYGG
     LSGTERVSGR WLVVVPESSG TTESSGTAVP EELLAALGTE PRVVPVPAGA ERADLAERLR
     AATASDTEPI DGVVSLLACV EGAGEVGAGG VPVGVVGTLG LVQAMGDVGV GGRLWVLTCG
     AVSVGRVEGG PVVGLAGVWG LGRVVGLEWP ELWGGVVDVP GVWDGRVVSR VVGVLGQSVG
     AGAGAGAGAG PGAGVEDQVA VRGSGVWVRR VVRAGVAEVG VGGSWVPGSE AGAVLVTGGT
     GALGARVARW AVERGARKLV LTSRRGSEAP GAAELERELT ELGAETSVLA CDVTDPEAVA
     RLLDQHPVDA VFHAAGVLDD ASVGELAEST LAASWSGKVA GAVHLDALTR DRELSAFVVF
     SSIAGVWGSG GQGAYAASNA ALDALVESRR AAGLAGTSVA WGPWAEAGMA ADGAAEEQLR
     RRGLSPLPPR EALRALGRVL SAGEGAVVVA DVDWSRFAAA FTSRRAAPLF AELPEAAPAS
     ASAPVARTDH DAASELARRL ADASEAERDE AVLTVVRSCA ARALGYAGPK AVESQRAFKD
     LGFDSLTAVE LRDQLSGETG VTLPATLVFD HPTPKDLARH VSDQLFSDTV EDSASVIADL
     ERIAGAISRF SPDYDARAVI EARLRRMLSE LGESAQGDPQ DQKAAVSQQL DTASDDEIFD
     FINQELGRS
//
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