ID K9U3T1_CHRTP Unreviewed; 1526 AA.
AC K9U3T1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:AFY89106.1};
GN ORFNames=Chro_3661 {ECO:0000313|EMBL:AFY89106.1};
OS Chroococcidiopsis thermalis (strain PCC 7203).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Chroococcidiopsidaceae; Chroococcidiopsis.
OX NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY89106.1, ECO:0000313|Proteomes:UP000010384};
RN [1] {ECO:0000313|EMBL:AFY89106.1, ECO:0000313|Proteomes:UP000010384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY89106.1,
RC ECO:0000313|Proteomes:UP000010384};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Chroococcidiopsis thermalis PCC 7203.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003597; AFY89106.1; -; Genomic_DNA.
DR RefSeq; WP_015155650.1; NC_019695.1.
DR STRING; 251229.Chro_3661; -.
DR KEGG; cthe:Chro_3661; -.
DR PATRIC; fig|251229.3.peg.4271; -.
DR eggNOG; COG0500; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_40_2_3; -.
DR InParanoid; K9U3T1; -.
DR OrthoDB; 428071at2; -.
DR Proteomes; UP000010384; Chromosome.
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; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; 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; IPR029063; SAM-dependent_MTases_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; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010384};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1420..1495
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1498..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 173176 MW; 2AA8B703DF18E7CA CRC64;
MVQDRSISAQ NSKLSASKRE LLAKLLQGEI TTPNPQQAQE TIPQLVPDRE SRYQPFPLTE
MQQAYWLGRS DVFDLGNVSM HNYIELDAVD LDIERFNCAW KRLIDHHDML RAVVLPNGQQ
QILDRVPPYE IQVLDLRSRD EQTINSQIQT IRDRLSHQVL PLDRYPQFEI VATQLGDRHF
RLHMSLDGWC IDYWSSIKLF QDLSQLYNQP EKPLPCLEIS FRDYVLASRT LENIPIYQRS
LDYWRSRIPS LPPAPELPLA KHPSAIAKPE FIRLQSALDS QTWQQLLKRA ARANLTATGV
LLAAYAEVLT LWSKSPKFTI NIPSFNRLPF HPQVNELVGE CASFTLLEID NTRQESFQVR
AQRIQTQLWQ DLEHEYVSGV RVLREWTNAQ DKAARAGTMP IVFTHGPQVD DKNPTAIAFL
EEQTKLVYSI SQTPQVWIDN QYAVKSDGSL SINWDFVAEL FPEGMVEDMF DAYCRLLNRL
VSEEKIWQET SLQLVPPTQL AQRAAIDATN TPISTELLHT LFAAQVPQRP QQPAVITSSH
TLTYEELSHR AHCLAQQLRQ LGASPDRLVA VVMEKGWEQV VAVLGILIAG AAYVPIDPAL
PQERQWHLLA QGEVQLVVTR SELNEKLDYP VGIQQICIDS FNYQLPITNY PLPITHYPSP
ENLAYVIYTS GSTGEPKGVA IDHRGAVNTI VDINQRFSIN SQDRVLALSS LSFDLSVYDI
FGTLAAGGTI VIPDAAATKD PAHWVEMILR QQVTIWNSVP ALMQMLVQYV SDRSECSLDS
LRLVLLSGDW IPLNLPEQIR ARVQEVELVS LGGATEASIW SILYPIQQVD PSWKSIPYGY
PMANQQFYIL NDKLEPVPVW VPGQLYIGGV GLAQGYWRNE EKTANSFITH PVTGDRLYRT
GDLGRYLPDG NIEFLGREDS QVKIRGYRIE LGEIETALKQ HPDVKDGAIA AVGEKQGNKQ
LVAYLVPQEE TTTLFEIEQA DPSQMQSLWK SLVEVGCRQA QQTFDWVDVS TFSAYWQLLD
KLYISSVRLA LKKLDVFVRS HEKYSLDDLM QKCQIKPRYD KWLKRALKTL VEEGLLQQHG
EVFENTLPLS TEVLSTLAAG FQSEAAQKLG LSQAMTNSLL HTANHLPDIL TENLHSAQIY
ASEETAEIYQ KLFKYCNTIA STVIRAVVQF WQPEAQLRIL EVGAGIGSTT AYLLPVLPPE
RTTYFYTDIS NYFMQLAQQQ FGAYPFLKTS LLNIEEDPQK QGYEPHSFDV VVASSVLHVV
RNLEETLRYL RSLLAPNGLL LLIEETKFHR PFDLGMGLQQ GFDRFEDEEL RQNHPLLSRE
KWQQLLAAQG FENCVIFNQP NTVPEFLGFD VLLAQAPASI KRFKPNELNS FLQKKLPEYA
IPCAYNLLEA LPLTSNGKID RQALSTIRLV KLDREKTFVA PQTPLEETIA AIWTGCLSIE
QVGTQDNFFD LGGDSLVATQ VHHKLQTTLQ RDFPLVKIFE YPNISSLANY LSNEANETPV
LQQGSDRGEK RKEVAQQKRR RQDKKG
//
