ID U5DC50_9CHRO Unreviewed; 1981 AA.
AC U5DC50;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ERN42088.1};
GN ORFNames=KR51_00012610 {ECO:0000313|EMBL:ERN42088.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN42088.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN42088.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN42088.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) 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:ERN42088.1}.
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DR EMBL; ASSJ01000034; ERN42088.1; -; Genomic_DNA.
DR RefSeq; WP_022605758.1; NZ_ASSJ01000034.1.
DR STRING; 582515.KR51_00012610; -.
DR PATRIC; fig|582515.4.peg.1410; -.
DR eggNOG; COG1020; Bacteria.
DR InParanoid; U5DC50; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000016960; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd12116; A_NRPS_Ta1_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 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; 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; 1.
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; 2.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000016960}.
FT DOMAIN 997..1074
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1890..1965
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1981 AA; 220176 MW; C9568C3A30C470F8 CRC64;
MTDFAKRISQ LSPEQLARLT KRVRKNPTKP AIPTQSREQP LPVSFAQQRL WWLHELDPDS
PVYNVPAAVR LAGPLQVEAL LQSFQALGDR HEPLRTVFVP NAASEPLQKI LPELEIDLPV
TDLQHLDGAV RDAEVERLAV AAAREPFDLA YGPLLRATLL RLAPEYHVLL FNIHHIIADG
WSLGVLIREL VQLYEAQVRS QPASLPSLAI QYADYAVWQR EQLQGEKLTG LLDFWQEQLR
DVPEVLDLPV DRPRPARQSG RGDRVAVRLD GELVQHLQTF SRQSQATTFM VGLAAYFAWL
YRYTGRQDLL VGTPVANRNR VQTEGFVGVL INTLALRVRL QPQWSFRQLL DEVRSVVTAA
SDRQDLPFEK LIEVLAPERS LSHAPLLQVM FGLQADPHQP FSAGDLEITP LASNLGATQF
DLFLDLFESS QGVQGTFVYN CDLFDATTVE RWARHWQGLL AAAIAEPDTP IDRLPLLNRD
ERQRIRDWNA TQTPLPNWHT MHGGFEAQVA RTPEAIALEF EDRRYTYAEL NARANRLAAY
LRARGVEPET RIGLLLDRTA ETLIALLAVL KAGGAYIPLD PAYPAERLQY ALTDAGADLA
IVRGNDDLAQ MALAAGVPVV IDLLAETDAI AQQSAENPAQ TPHPAQLAYL IYTSGSTGKP
KGVQIPHQAV ANFLNAHGRS PGITPQDTLL AVTSLSFDIA VLELLLPLTY GATLLFASHE
TTLDGAQLAQ LLQRATMMQA TPASWRLLLA SGWDGQPGLK ILCGGEALPP DLAAALTDRG
SELWNLYGPT ETTIWSAQQQ IQNDASVAIG RPIANTQTYV LDTQLQPAPV GVAGELFIGG
LGLARGYQGR AGLTAERFLP DPFATEPGAR MYRTGDLACY RTDGTLQHLG RIDYQVKVRG
FRIELGEIEA CLHDHPAIAQ GVVSAHGDTL VAYLQGETEL PATELQQWLR QQLPEYMIPA
WFTWLPDFPL TPNRKIDRKA LPVPSGEALT ANQPYVVPET QRQQTIAAQF AAVLDLPPER
VGLHANFFDL GGHSLLATQL ISRLRQAFGV EIPLKVLFEA TTVADLDRAI AALEQSQTAR
QALPAIVPLP ATERDPANLP LSFAQQRLWF LDRFEGGSAT YNIPGSFRIE GVADLDAMQQ
ALDALVARHE SLRTYFPLRD GSDSAVQCVL PHLHVPLEIV SAVDLDCIPE DWLIRQTQQP
FDLATGPLLR VKVIQLAPNE NILSVVMHHI ISDGWSSGIF IREIITLYQG YRTGESTELA
PLPVQYADYG VWQRQWLEGE VLERQLNYWQ QQLAGVPALL ELPTDYPRPA RRSFQGRVQN
IALPPELTAA VKTLAQQQEV TPFMVLLTAF QLLLARYSAQ QDIVVGSPIA NRNHPEVEGL
IGFFVNTLAL RTTIDPTATV ADLLQQVRHT ALDAYAHQDV PFERIIEAVA AERTLAHTPL
FQVMFILQNV PTASLELEGI TLTPLEVETV AAKFDVTLSL QEGDRGFSGR WEYDSELFTA
ETIARMATHF EMLLRSMVAD VRQPVATLPM LTSRERQQIL TDWNNTAVDY PLDNCIHQLF
EYQADRTPEA IAAIYGAESI NYFTLNARAN RLAHALQEFG VKPGILVGLC VERSLDALVS
VLGILKAGGA YVPLDPSYPP ERLEYMLANS QVPFLITQNA IADRLPEHQA KTVCLDTDWT
SKIQPHSTEN PTSEVTPDSV AYVIYTSGST GKPKGVQGLH QGTVNRLYWM WTTYPFEPNE
RCCQKTSLSF VDSVWEFFGG LLQGIPTVII PAETVKDPPH LIDTLSTHQI SRIVLVPSLL
RAILETGSEL KDKLPHLKYW VTSGETLETN LCKEFYDKIP NSFLINLYGS SEVSADVTHH
ETWHSKVDPS PIELASVEFP DSSVRGRLTE PQQPEEKALA EIWKDVLQLE WVGIDDNFFE
VGGNNYLSNL TIERLHYLFG IPLPRESLYR APTIRELVKL LKEHEPEPGK VATIARILQQ
L
//
