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Database: UniProt
Entry: C9ZDJ5_STRSW
LinkDB: C9ZDJ5_STRSW
Original site: C9ZDJ5_STRSW 
ID   C9ZDJ5_STRSW            Unreviewed;       340 AA.
AC   C9ZDJ5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative ATP-dependent polynucleotide modifying protein {ECO:0000313|EMBL:CBG70354.1};
GN   OrderedLocusNames=SCAB_32541 {ECO:0000313|EMBL:CBG70354.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG70354.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG70354.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG70354.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
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DR   EMBL; FN554889; CBG70354.1; -; Genomic_DNA.
DR   RefSeq; WP_013001009.1; NC_013929.1.
DR   AlphaFoldDB; C9ZDJ5; -.
DR   STRING; 680198.SCAB_32541; -.
DR   GeneID; 24312770; -.
DR   KEGG; scb:SCAB_32541; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_1_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR   CDD; cd07970; OBF_DNA_ligase_LigC; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR044119; Adenylation_LigC-like.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR044117; OBF_LigC-like.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          113..241
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   340 AA;  37548 MW;  A6D3C596B4C84CD1 CRC64;
     MVLRPPVEPM LARAHARDQL PTPGTLPGDP VIQPKFDGYR ALVFTPFPGP GPVLIQSRRG
     SVIQFRFPDL ARAAAQLPDG LVLDGELVVW DGDQLSFEAL QRRAASSGRT AQRLAEELPA
     HFIAFDVLQI DGTELLREPY AARRAALEEL FTRHRLTAPW TLCPQTSEVK TAQEWLTSWT
     EVSGLEGIVI KGGAQRYLPG VRGWFKIRRR DTTEAIVGGI TGSPDRPRTA FLGRYDQGGT
     LRLVARTTPL HPEVARGLSE RLTAAGPAHP WAGARFTTSW GSRTPLDVIL VEPDTVTEID
     VDTARDRGAW RHPVGVLRIR YDMRPGDVAA FDEDTTQTDD
//
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