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Database: UniProt
Entry: Q0F563_9RHOB
LinkDB: Q0F563_9RHOB
Original site: Q0F563_9RHOB 
ID   Q0F563_9RHOB            Unreviewed;       232 AA.
AC   Q0F563;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   Flags: Fragment;
GN   ORFNames=OM2255_00147 {ECO:0000313|EMBL:EAU49247.1};
OS   Rhodobacterales bacterium HTCC2255.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU49247.1, ECO:0000313|Proteomes:UP000009381};
RN   [1] {ECO:0000313|EMBL:EAU49247.1, ECO:0000313|Proteomes:UP000009381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU49247.1,
RC   ECO:0000313|Proteomes:UP000009381};
RA   Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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};
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:EAU49247.1}.
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DR   EMBL; AATR01000029; EAU49247.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0F563; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_1192147_0_0_5; -.
DR   Proteomes; UP000009381; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAU49247.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009381}.
FT   DOMAIN          1..133
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EAU49247.1"
SQ   SEQUENCE   232 AA;  26556 MW;  6578E36E598F9481 CRC64;
     SPADSFIYDC IALGSDAQRR SLVELPLCER HKLFTEVMTP VTQHRLRLSP PLVIDSKDHC
     IRLRDEVCEQ SGQRIEGLML KRKASLYVPG RPKGQWVKFK RDPMLIDAVI MYAQRGHGKR
     SSFYSDYTFG CWATNDAGER VILPIGKAYS GFTDAELHEI DKWVRKNTIG RFGPVKEVAK
     ELVFEVAFDA VHYSKRHKSG VALRFPRIHR IRWDKPANEA DELETLVGMI AQ
//
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