ID E1U3N2_9CYAN Unreviewed; 2389 AA.
AC E1U3N2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Non-ribosomal peptide synthetase module-related protein {ECO:0000313|EMBL:ACN96039.1};
OS Fischerella sp. MV11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=397321 {ECO:0000313|EMBL:ACN96039.1};
RN [1] {ECO:0000313|EMBL:ACN96039.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MV11 {ECO:0000313|EMBL:ACN96039.1};
RA Hess W.R., Scholz I.D.;
RT "High diversity of cyanobacterial nonribosomal peptide synthetase genes in
RT isolates from geothermal sites and hot springs of Costa Rica.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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DR EMBL; FJ211387; ACN96039.1; -; Genomic_DNA.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd12114; A_NRPS_TlmIV_like; 1.
DR CDD; cd19535; Cyc_NRPS; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 1.10.10.1830; Non-ribosomal peptide synthase, adenylation domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF10; PHENYLOXAZOLINE SYNTHASE MBTB; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF18563; TubC_N; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 3.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1238..1313
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2312..2387
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2389 AA; 270519 MW; F63098B2ABEB6A91 CRC64;
MATDILQKFK EQGIELWAEG DKLRFRATKG VLTPSLREEL VNHKEAILRS LFWTGISSIS
DISQITPASQ ERYQPFPLTE IQQAYLLGRS EIFSLSGVSA HAYQEFEAAN INIKQLNQSL
NRVIAHHDML RAIVLPSGEQ KILEQVPEYE IKFLDLRGKS LQEVDSCLEK IRSEMSHQVL
PTDKWPLFEI RATQINEEIT LIHLSTDLLI CDAYSNQLLI QEWFQVYHQP DIQLVGTEFS
FRDYVLALAS LQDSQLYQRS QAYWQKRLST LPLAPDLPLV KQVSSITKPR FVRREGKLDS
ETWRKLKHKA TQLHITGSGL LCAAFSEVLA VWNPNPHFTL NLTLFNRLPL HPEVEQILGD
FTTTILLEVN QSLNTFTTRA QRLQQQIWED LEYSQISGVQ VLRELAKQQG RSSSGILMPV
VFSSALFSEA TQPQETATIP WKEVYGITQT PQVLLDHQVR EDTGALIFNW DSVDEVFPPG
MLDDMFAAYY QLLELLACDD SAWQQPTRQL VPQTQLEQQA VENATAAPIS RELLHTLFAT
QVKAQRYSKA IVSHKRTMTY EELSDHAHQI GHQLRQLSVR PNQLVAVVME KGWEQIVAVL
GILNSGAAYL PIDPSLPTER QRYLLENGKV QVVLTQSWLS ESLEWPENIQ PICVDTQVID
NTVVPLEPIQ QPEDLAYVIY TSGSTGLPKG VMIDHRGAVN TIIDINKRFG IGSEDKILAL
SALNFDLSVY DIFGTLAAGG TIVIPEPART KDPAHWIELV DKAVVNVASQ KLVAYVVPNL
NNCPSLFAVK TGDAEKFITT WASLVQAGRQ QALQLPLEMN LQLYGTFWQS LEDFCTLSMC
CTLTKLGVFI QPREKHSLEE LVRTCGIDEK QKWLLGHWLK VLQQEGLLEE VATETFMNFQ
PLPSDFWNDL WQEIERSATW GNQAQTWQEY VKCSIDNHPA LLRGEIDLRE LLFPDGSWKT
AESLYALNPF TDYHNSIAQE ILRVVVGDWN QDRPLQILEV GAGTGGTTAA LLPVLLLCQA
VYTYTDISQF FTNQAQDKFK NYSFIEYGIL DVDKNPVHQG YEPHSFDVIV AANVIHNARN
VDKTLEYLRS LLTPNGILLL LEVTKNSRTQ MVTVGFIEQF THLEDERKKT KMPLLSVAEW
GKALDQAGFE EFVAFPESKS STEALEQHLI VAKAPAHVRS FQPSVLHTYL HNKLPEYMLP
SAYVLLETLP LSTNGKIDRK ALPEFNLVKS QQEKTFVLPR TSLEKQLVEI WADILNIKQI
GIHDNFFEIG GDSLLAIQVS SRVRQAFCVE LPLRRLLDSP TIAGLAKYIQ IARQEQQTEN
ETVVENLPSV VPQLNMRFEP FSLTDIQQAY WVGRMGAFEL GNVSTHIYLE LLSRGLDLER
LNLALQKLIE RHDMLRAIIL PDGQQQVLEK VPLYQIEILD LSRENEEAIA AGIDRVRQEM
SHKVRPANQW PLFEFRVTLL NAGHVRLHVS IDAIILDGYS ILTLFKEWSQ LYEHPELALP
PLEISFRNYI QAEQALRNTE LYRRSQDYWF NRLDTLPKAP ELPLAQKPHQ QQLFKRRVSE
LDKTLWQQLN QRAAKAGITA SGVLIAAFAE ILTVWSKSPD FTINLTLFNR LPLHPQVNNL
IGDFTSLNLL EVHNDTNESF STRATRIQKQ LWQDLEHRYV TGVEVLREMS RRQGGARVTM
PVVFTSALVL GSLGEDASVL NHFGDLGYSV SQTPQVWLDH QVINKNGALV LIWDAVEELF
PEGLLDEMYE SYCNFLKRLA TSDQEWIKPI RQLVPTTNLE LQAAVNATAA PVAEELLHTM
FLRQVQVRTH SPAVITSQQS FTYQELFTRA NSVGHRLRKL GVSPNQLVAV VMEKGWEQIV
AVLGILMSGA AYLPIDPELP TERRLYLLTQ GEAVCILTQS HLNQDLEWPN SIPRLCLDDS
DDLLAVDKSP LHSVQSPEDL AYVIYTSGST GLPKGVMIDH RGAVNTITDI NQRFGIGSDD
KILALSSLNF DLSVYDIFGT LAAGGTIVIP DASARKYPAH WLELMQREQV TVWNSIPTLM
QMLVEYAGGC QETLPISLRL VMLSGDWIPL NLPNLIKAAA NQTQIVSLGG ATEASIWSIC
YPIETVDRHW KSIPYGKPLQ NQRLYVLKES LEPCPVWAVG QLYIGGIGLA QGYWHDEQKT
NSSFIIHPHT GERLYQTGDL GRYLPDGNIE FLGRVDSQVK IRGHRIELGE VESTLAQHPA
IRSVAVVAVG DDEKSKDYLV AYVVPDREQT VTEEQLIVNL RTFLKQKLPE YMIPSAFLTL
ETLPLNPNGK VDRKALVKQT YFQPEPEVVY VAPQNEVERI IAKVFQELMQ VENVGLYDNF
FHLGANSLHL VRLHSKLQEI FHQDFAIATL FQSPTIYALA QHFNAYHAE
//