ID B8NKE5_ASPFN Unreviewed; 1734 AA.
AC B8NKE5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Nonribosomal peptide synthase, putative {ECO:0000313|EMBL:EED48939.1};
GN ORFNames=AFLA_090200 {ECO:0000313|EMBL:EED48939.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED48939.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED48939.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- SIMILARITY: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ963480; EED48939.1; -; Genomic_DNA.
DR RefSeq; XP_002380840.1; XM_002380799.1.
DR STRING; 332952.B8NKE5; -.
DR EnsemblFungi; EED48939; EED48939; AFLA_090200.
DR VEuPathDB; FungiDB:AFLA_009234; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_2_1; -.
DR OMA; YTIWEVT; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
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; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 555..631
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1217..1290
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1734 AA; 192495 MW; BAAE6BAB63E75651 CRC64;
MLKQIIHNLT NSPSRPLVDS CLLSKHHQDQ IARWNSDAPA VPLDSCIHTL FRVQCMLQPD
AQAICAWDGT ITYRELDRLS SAVQGLLQPY NPAPNSVVPI LFKKSKWAVV AMLGVLKAGA
AFSMLDPSYP TKRLVDICHD VDAKVLVCSE ELSIDVSGNI LTIGDHNIAN ASYSAVHPVK
TASHDAAYVV YTSGSTGAPK GIIIEHGSFC TNVMASSRAQ NLDRSSRILQ FASYAFDVSI
HECLTPLLLG GCVCIPSESQ RVNSLKEAVR SLGVNWMELT PSVARLWQPE DIPTVSTLVL
GGEPMLPSDV SQWKDKVRLV CAYGPAECTI VSTVQSCVQD LGNIGVSPGG TCWIASQDNH
QRLMPVGCVG ELIIGGPIVG RGYLKRPCLT KNAFIINPEW ASLFRLDETY RLYKTGDLVR
YNYDGTIAYI GRKDTQVKLN GQRVELGEVE YQARQCFHDA VIAAEIAAPA GRKPTLILFI
APRQEYSIQM DSARSGLQNV LPRHMIPTAY IELVAMPISR TGKVDRRVLR EAIENVSEDD
FRAYYPTPHN NMINSPNTPV LDQLRYLFSA ALDIPEDKIG PNDSFFQLGG DSVSAIKLVG
DARDQGLKMT VEALFRQQTI CKLETCTHQT SGSIDTPISA FSLLDPSSKA TYIAQATEQC
FVSPEQIEDI YPCTPLQEAL MAYSSKRPGA FQATFRFRLP QQLDILRLKE AWITVIAANP
ILRTRIVHSE TGALQVVLRP DEPLQWDLIY DVNEIPGSFM SYGAPLINVA VVSDTGGKPD
RTFCLMMHHA IFDGWSYALI LSAVEGAYKH MNAVQRPFTP FIKHIMSCNY ESARDFWCSE
FKDTQAVPFP VPPFTSGHMV NSITTVQRQI HISEWLGGCY TPSTIIQLAF AMLIAWRTSS
MDVVFGLTVT GRNAPVPGVH ETTGPTIATF PLRTILHGRL NVADSLVLMQ NHITRLIPFE
QTGLQRIKSL SSETASACQF QSLLVIQPAT NRKSQRILSE CPSNEYEQVK FSTCPLTLVC
ELEADKLSIK AVFDNAVVVA DGMQRMLDQL EYLVDMITKS PTSKIESIIP RPSNIYPDAF
RQGQSWSAYI EKKAYDYFDG EVSVVVDTIV PKGGSNQHTV MFICEADQNC ESAELSDLFT
RPTDQVRWQL HQLICSLQES LPCSVVPSLC LPIHSMPLDA FGQPDRSRLC EEASSKSHCF
LRSLMVPANN QIDYNILPGE ARLRTAVAHV LGMEPKNISP KDDFFALGGD SISAMQVVSL
CRKHHLSLTA SDIFDGKSIE TIASSVKPLT LYTPPSTPGS DRSLGARFPL LSLKSDSDME
VLESAIMATY DFQSMDSIED VYPCSESHQG LLPTQMLQPF IYQSYTIWEV TTGSMASPVC
PIKLRNAWFN IARRHPALRT HLIESPLSVG IHQKIHIVHE DYVTDIPIIS CADEQVFAEL
RKPFLQTSAK IYYPHAFTIC QSISGRVFCK LEGGQAFLDA ASVLIILHEL SEAYDGQLSP
LPGPLYGPAV AWFQSLRNAD DRMDYWRRQL EASRPCIFPM LRDQDSPTET LVITEHLAST
ATLISFCTLH GLTVTNLMQV AWGLTLRYYT ESDDVCFGAL MSGRDSRIAD VDKMIGPFFN
VLVCQLRFGR EDSLLAILRR NQVETGNRLL NQHCSLIEIL RFSKYFGQPL FNTCISVEQP
LSMDSCNASL CFKELETLEP TEVCFQQSHC LTQLTALNSM ALSLPLRLDQ RMFG
//
