ID A0A2T1LQM2_9CHRO Unreviewed; 2017 AA.
AC A0A2T1LQM2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:PSF28879.1};
DE Flags: Fragment;
GN ORFNames=C7H19_24545 {ECO:0000313|EMBL:PSF28879.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF28879.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF28879.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF28879.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF28879.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF28879.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) 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:PSF28879.1}.
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DR EMBL; PXOH01000070; PSF28879.1; -; Genomic_DNA.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000239001; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd17651; A_NRPS_VisG_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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; 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239001}.
FT DOMAIN 1011..1086
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT COILED 1..28
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 2017
FT /evidence="ECO:0000313|EMBL:PSF28879.1"
SQ SEQUENCE 2017 AA; 229426 MW; C073D5D5DFF0DA75 CRC64;
MSDLSKRLEN LSSEKRELLL KKMRSQNLNP QKEEKITIVS IARDKPIPVS FAQARLWFHE
QLEGANATYN MPAALHLQGI LNIVALKKSL QEIINRHEIL RTQFSENAQT VNQIILNNLK
FNLLEIDLYS VVKSEQMEKV YQLATEEAQK PFDLTKVPLI RATLIKLEAQ SNVLLLTMHH
IISDGWSIEI FIKELGILYQ AFCENKPSPL SNLTIQYADF SVWQRQWLQG NILNQQLQYW
KQQLNHAPSL LNLPTDKPRP VFQSFCGQTQ TFTLTNLFKK KLETLSQQYR TTLFTTLLTA
FAVLLSRYSA QKDIIIGTPI ANRNRTEIEP LIGFFVNSLP IRIKLENNPT FTDLLQQVRS
SCLDGFAHQD IPFEKLVEEL QPERNPSYHP LFQVMFDLQK EPLSQIKTEN LTLSLLKIES
NTAKFDLTLS FEETESELIG EFEYNSDLFE SSTIQRMIGH FQTLIQNIIT QTERPIRELN
ILTQAEQEKI LNEWNKTEVN YSSECIHQLF EKQVEKTPNA IALIYQKQQL TYSQLNSKAN
QLAHYLISLG VRPETRVGIS VERSIEMIIA ILAILKSGSV YVPIDPDYPT SRLDYIINDA
QINILLTQEH LLQQFIEKVP NIHSLSLDVT SFPTTNPVTQ VNPNNLAYII YTSGSTGQPK
GVMIPHQAVV SFTNSAISTY NFTAFDKILQ FATISFDAAV EEIYGALSSG ATLVLRSATM
LDSFETFLKE SQIEEITVWD LPTAYWQQLT NFIANTGQII PETLRLVIIG GEAASVNSIN
LWREKIGTSP RLFNTYGPTE TTVVATKYEI TSSIDINTVP IGKPLNNVQT YILDQYLQPV
PIGVLGELHI GGKQLALGYL NRPELTTEKF ISNPFSNDPL VKLYKTGDLA RYLSDGNIEY
VGRIDNQIKL RGFRIELGEI EAILTQHPQI SESLVIVSQT TPLKQKLIAY LVTKDSEIES
ASIRAWCNEK LPAYMIPAVY VILDAFPLTP NGKINRNALP IPNQSIERKK PPTTPTEQLL
ALIWSDILNI ENIEREDNFF ELGGHSLLAT QVISRIRQNL KVEIPVKSLF TYPTIEQLAQ
HITQIQQSEQ LPPIKARERN TTNLPLSFAQ ARLWFLDQLE EHSSTYNMPI VLQITGQLNT
EALQKSWTEI VTRHEVLRTN FVTHDGIPVQ IIHPEVDTEI NYIDFSKNTT NQKITDLIST
EIEKPFNLSS DRLGRVSLIN LGQDKYLLLV TLHHIISDGW SMSILVQELS TLYQAFSQNK
TSPLSELPIQ YADFAQWQRE ILTDEYLDKQ LQYWQQQLEQ STTTLNLPTD YPRSTLVTNR
GASFPLQINQ EITSKLKMIT HQQGVTLFML LLSVFSVILS RYSGQTDLII GSPIANRNRA
EIEPLIGFFV NTLPLRINLE NNPTFSDLLK QVRDICLDGY AHQDIPFEKL VEELKIERNM
TQNPLFQVMF VLQNTPEDKL KLGELDLTVL DSESQTAKFD LTLSMEETEK GLIGIWEYKT
DLFKTETIER LSQHFQNLLE SLINNPQQLI SETSYLSESE QQQILVEWNQ TQIDYPQKND
CIYQLFEAQV EKTPDAVALV YQNQQLTYSQ LNFKANQLAH YLISLGVRPE TRVGISVERS
IEMIIGLLAI LKAGGAYVPL DPHYPTARLN YIIDDAQITI LLTQEHLLSK ISKPNIRAIC
LEQDWSNTNL TNPDTLVKSE NLAYLIYTSG STGQPKGVAL THQSLVNLIL WQKQSSRKAN
AKTLQFAPIS FDVSFQEIAC TLCAGGTLVL INEDQRRDFF ALWQLIDIEQ IERIFLPFVA
LQQLAQVAQE KNTLPNSLKE IITAGEQLQM SSSINNLLQR LPDCTLENQY GPSESHVVTA
FKLSQNAQNL VLPPIGQPIA NNQIYILDTH LHPVPIGVAG ELHIGGVSLA RGYHNRPELT
QEKFITHPFS LDKTARLYKT GDLARYLSDG NIEYLGRIDH QVKIRGFRIE LGEIEAILTQ
HPQIKENVVK VLENQTGKQL VAYVVSRSST LKKEEIR
//
