ID A0A2W2FPY2_9ACTN Unreviewed; 1428 AA.
AC A0A2W2FPY2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PZG23917.1};
DE Flags: Fragment;
GN ORFNames=C1I98_36015 {ECO:0000313|EMBL:PZG23917.1};
OS Spongiactinospora gelatinilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Spongiactinospora.
OX NCBI_TaxID=2666298 {ECO:0000313|EMBL:PZG23917.1, ECO:0000313|Proteomes:UP000248544};
RN [1] {ECO:0000313|EMBL:PZG23917.1, ECO:0000313|Proteomes:UP000248544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7K107 {ECO:0000313|EMBL:PZG23917.1,
RC ECO:0000313|Proteomes:UP000248544};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Sphaerisporangium sp. 7K107.";
RL Submitted (JAN-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:PZG23917.1}.
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DR EMBL; POUA01000517; PZG23917.1; -; Genomic_DNA.
DR Proteomes; UP000248544; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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 InterPro; IPR016039; Thiolase-like.
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; PF00109; ketoacyl-synt; 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; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 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 SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1122..1197
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1216..1428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 1428
FT /evidence="ECO:0000313|EMBL:PZG23917.1"
SQ SEQUENCE 1428 AA; 149771 MW; A9C257EE5D94F357 CRC64;
MARSLTMRAA LENRSVVVAG DRDELLAGLD GLVPGAGPVS GRTGLLFSGQ GSQRLGMGRE
LYESFPVFAG VVDEVCAVVD QVLDRPLREV MWGTDAAALE QTAYAQCGLF ALQVGLYRLV
ESWGVVPDAV MGHSIGELAA AHVAGVFSLQ DGAALVAARG RLMQALPEGG AMLAVAATEA
DVTEAVAGLD LSIAAVNGPS AVVVSGAREV LEEFAAGVEW RSRWLRVSHA FHSGLMDPML
AGFAEAAAKV TYASPRIPLV SNVSGTWAGA EVCSPEYWVG HVRRTVRFEE GVAAMAADGV
TRFVEIGPDG VLTALNEERL FVPLLRKDRP EVEALWSGLG RAWASGLAVD WKTILTGRGH
RVDLPTYAFQ HERFWLESAH DAGDVTRVGQ SPADHPLLGA VVTLPGTGGV VLTGRLSVSD
QPWLADHTVL GQVILPGTAL VELALQAADQ TDCRTVEELT LHAPLVIPEQ GGIALRISVD
AADEQGRRPI EFHSLPECAE PGTPWTLHAT GLLAEASTMA AVEDLTAWPP PGAEPLSLDG
FYARLAADSM SYGPLFQGLR AVWRRGDELY AEVALPEEAE PARFGLHPAL LDAALHATDL
LGRSAPGPVL PFAWENVTLH ADGARSLRVR IAQSRTSPDA LALTLSDDAG TLAASVGSIV
IRPVTEEHLA AARTEPLFRV DWTRLDTRPQ AQPHIGAVLG VDGNEAPWGA PVHADVASLT
EAGVPQTVAL VCERDGGPLP ESVHTAVVRV LETVRQWLAD DRCRDSRLVI VTRGAVAARP
GEVVEDLAGA AVWGLLRSAQ AEHPGRFVLV DTDGPVLPAG DEPELAIRGV EVFVPRLTRV
RPTGELPRLS GPVLVTGGTG GLGALVARHL VTKHNVRELL LVGRRGLDAP GAAELCDDLT
ALGAEVEIAA CDIADRDAVA GLLAGREPGA VVHAAGVLDD GVIESMTPDR MATVLRPKVD
AAWHLHELLP DVSAFVLFSS LSGVLGAAGQ ANYAAGNAFL DALAQHRRGQ GQAALSLAWG
LWEQAGGMGG ALADVDRSRV GRGGVLALTA ADGLGLLDAA LGVDAPALVP VKLDFAALAA
AGESAPALLR GLVQVKRQRV AETTPDGLGA RLAGLTEAER ERVVVDLVRA QVASVLGHGS
AEAVEAERAF SDLGFDSLTA VELRNGLGSV TGLRLPATLV FDYPSPGALA EYLLDEVVGT
EEVAVPVQVA TVAVDDDPIV IVGMSCRYPG AADSPEQLWR LVADQVDAIS GFPTDRGWDT
DGVYDPEPGR PGRSYVRDGG FLYDAAEFDP GFFGISPREA LAMDPQQRLL LEVSWEALER
AGIDPQGLRG SRTGVFAGVM YHDYAESSSS GSVVSGRVSY TFGLEGPAVS VDTACSSSLV
ALHWAAQSLR QGECSLALVG GVTVMATPDS FVEFSRQRGL APDGRSKS
//
