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Database: UniProt
Entry: A0A1A8ZQ51_9ACTN
LinkDB: A0A1A8ZQ51_9ACTN
Original site: A0A1A8ZQ51_9ACTN 
ID   A0A1A8ZQ51_9ACTN        Unreviewed;       977 AA.
AC   A0A1A8ZQ51;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Non-ribosomal peptide synthetase component F {ECO:0000313|EMBL:SBT46010.1};
GN   ORFNames=GA0070621_2496 {ECO:0000313|EMBL:SBT46010.1};
OS   Micromonospora narathiwatensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=299146 {ECO:0000313|EMBL:SBT46010.1, ECO:0000313|Proteomes:UP000198765};
RN   [1] {ECO:0000313|EMBL:SBT46010.1, ECO:0000313|Proteomes:UP000198765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45248 {ECO:0000313|EMBL:SBT46010.1,
RC   ECO:0000313|Proteomes:UP000198765};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT594324; SBT46010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8ZQ51; -.
DR   PATRIC; fig|299146.4.peg.2585; -.
DR   Proteomes; UP000198765; Chromosome i.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198765}.
FT   DOMAIN          530..849
FT                   /note="Condensation"
FT                   /evidence="ECO:0000259|Pfam:PF00668"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   977 AA;  105119 MW;  270BF2080C9C6518 CRC64;
     MPAVPEAPDR LNGPLCKTRS SESTPNGSDV RSGMGFVDVV VPAEWASETL VRAEFSGAGT
     GSAPLTWAQQ VMWRSVARYG SNHVFLNLRR TVPVSARAGV DLAAAVRAVG AWMGRHGSLR
     TRVRVVDGEP RQETAAAGVL PLLVRAGTGD GARAAREVAG RLGDVAFDHA AEWPLRVALI
     IVDDRVRQVV AVFSHSTVDA HAAEQVLREL RLILLRGGLY TPAGPQSLDV ARLQHGPDRG
     RSARAVAYWL REFRRLPAEP LPSAGPGLEP PLRRGVLVSP AAGAAARLIA ARHRVSVSAV
     LLAGVTALAA GRSGRRICGL FPMAHNRFRA GYANAVANLG QIGFCVVDLA GRPDFAGLLS
     RVWAASLDGL RHAYYDPATL RHAFGEQGVD HASAFLPHYY FNDVRLPVGG VDPVPAATRS
     ELRAALAHST FSWTAGLHQA SWHLLTHVVD EAAGVGFTLT VDTRHVALDT VEPFLRGLEE
     LLVEAAFAEV PWPWSPVDAR PGEAPVPVPV AGVEETAYAE FHGGRAGTGP LSWGQRAMWR
     TVEEFASPAA YRVLSLPRTL AVSARADVAV PRALGALGGL VARHESLRTR IRRRDGELHQ
     EAAASGRLSV LVHAVPRPAD DPDGRTAAAE LAERLGGSPF DHVTEWPLRV ALVTVDDRVR
     QVVAVFSHST VDFHAAETVL RDLRVLLLRG SLDTPPGLQS LDLAERERGV ERRRSERAVE
     YWLRQFDGLT ASLSDPVGPA PGPRYRRGSL VSPAVHQAAR LVAARHGVSS STALLAATAA
     VLSADPGQDT CGIVVMANNR FLPGYDRAVG TVNQIGLCRL DLADRPGFAE LLPRARRAAL
     DAYRHAYYDP AAFEQAFTDL GHDHRSVLAP FCYLNDIRLS HDVGTDAAGP DEAALRATVA
     RGAFRWREPL DQFAWRCRVQ ALDAPGAVEL VVTADTRYLP AERVEPFLRG VEALLVEAAF
     RDVPWPWSPF PGRDPAG
//
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