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Database: UniProt
Entry: A0A0N0A4N8_9ACTN
LinkDB: A0A0N0A4N8_9ACTN
Original site: A0A0N0A4N8_9ACTN 
ID   A0A0N0A4N8_9ACTN        Unreviewed;      1025 AA.
AC   A0A0N0A4N8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE   Flags: Fragment;
GN   ORFNames=ADL04_38690 {ECO:0000313|EMBL:KOV89196.1};
OS   Streptomyces sp. NRRL B-3648.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV89196.1, ECO:0000313|Proteomes:UP000037702};
RN   [1] {ECO:0000313|EMBL:KOV89196.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV89196.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOV89196.1}.
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DR   EMBL; LGDZ01000255; KOV89196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0A4N8; -.
DR   PATRIC; fig|1519493.3.peg.8228; -.
DR   Proteomes; UP000037702; 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; cd08956; KR_3_FAS_SDR_x; 1.
DR   Gene3D; 3.30.70.3290; -; 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   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
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; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00826; PKS_DH; 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:UP000037702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          868..943
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KOV89196.1"
SQ   SEQUENCE   1025 AA;  105996 MW;  C2A6F3348CE33B2C CRC64;
     PVVSNVTGRL AEPGQLTDPA YWVGHVRRPV RFADGIAASG GQVFLELGPG GALTGAITES
     AGEDAVSVPA LRDERGEAQT LLAAVAHLFV RGTKVNWAAA LPEGAAEARV DLPTYAFDHR
     HYWLRMAPAT DAVALGQSTA NHPLLGAVVP LPQSDGLVFT SRLSLRTHPW LADHAVGGVV
     VVPGAGLVEL AVRAGDEVGC GVVEELVIEA PLVVPEQGGV RVQVTVEAPD AEGRRAVAVH
     SAREDAVGET GADAWTRHAT GSLTGAIPAA GRTFDFTAWP PPGAQAEDLT GVEERLLRYG
     YEYGPVFHGL RAVWRRGEEL FAEVALPDGQ RDAAARFGIH PALLEAALHP ALLDASAADD
     TQLWQPLEWN RLALHAEGAT VLRVRMARAG DALAVEAADE AGGTVVTAEA VTLRPLSAEQ
     LSTAAGTGAD DGLFRVVWSE LPPVAGAGEV PEATLVEARA GTGDTPLALA SRVLEAVQAW
     LADEGTEDGR LVVVTRGAVP AGGDAAVTDP AGAAVWGLVR AAQAENPDRI VLVDTETGEA
     DLGPVLACGE PQVAVRGTAL YVPRLARLAP AGGSDAPALD PEGTVLITGG TGTLGAEVAR
     HLVERHGVRH LVLAGRRGKA AEGADRLVAE LGERGADVSV VACDVTDRDA LAALLAAVPQ
     AHPLTAVVHA ARVFDAGVIG EMDRDRLARV FAPKVTAVEH LDELTRELAP GLAAFVLLSS
     ASSVFLGAGT GGYAAANAYL DAVAHRRRAA GLPAVSLAWG PWEPTGGQDT ATGDAVRNRT
     GRRGGVVPLT PAQGMELLDA ALAADEALVL PVKLDLRALR ADAALGAGVA PLLRGLVRTG
     RKAARAGAGD SGGLARKLAA LSPAEQETLL LELVQGQVAT VLGHTGADQV RAETAFKDAG
     FDSLTSVELR NRLREATGLP LPATAVFDYP TPLALAGYLH DRLAPGDQTA PATHPLLAEL
     SKLEGLLADT APDDTTRAQV ATRLQGLLTT WSTTNVTEPD AEEDVDFESA SDDELFELID
     TEFGH
//
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