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Database: UniProt/TrEMBL
Entry: D5UKM3_CELFN
LinkDB: D5UKM3_CELFN
Original site: D5UKM3_CELFN 
ID   D5UKM3_CELFN            Unreviewed;       522 AA.
AC   D5UKM3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   25-OCT-2017, entry version 47.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=Cfla_0933 {ECO:0000313|EMBL:ADG73841.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / NCIB 8073 / NRS
OS   134).
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG73841.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG73841.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / NCIB 8073 / NRS 134
RC   {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain
RT   (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP001964; ADG73841.1; -; Genomic_DNA.
DR   RefSeq; WP_013116175.1; NC_014151.1.
DR   STRING; 446466.Cfla_0933; -.
DR   EnsemblBacteria; ADG73841; ADG73841; Cfla_0933.
DR   KEGG; cfl:Cfla_0933; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000000849; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3260.10; -; 2.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000849};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:ADG73841.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000849}.
FT   DOMAIN      314    427       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    229    229       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     227    227       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     234    234       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     249    249       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     278    278       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     316    316       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     387    387       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     393    393       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   522 AA;  55151 MW;  EB2196E8F8172D6C CRC64;
     MLLDDVADAS AQVAATRSRL AKRAVLVDVL RRVAADGPDD VAIVSRYLGG ELRQRRTGLG
     WRSLASMPGA AEVPSLSVHD VDAAFAGMAV LAGPGSATAR TEAARALFAA ATEREQHLLR
     GLVSGELRQG ALDALLLDAV AEAAGVPADV VRRAAMLAGE TEAVAVAALG AASPDDARTA
     LDAFALTVGR PVRPMLAQSA PDVPTAVAQL GERAGTAESP AAQVVVDTKL DGIRIQVHRD
     GDDVRVWTRS LDDITARVPE IVAAVRGLPA RALVLDGEAL ALDADGRPRP FQETASRSAT
     RDAELAGSAT LTPFFFDVLH VDGRDLLDAP LRERLAVLDQ VAAPHVVARV VTADPAVATE
     HFRAVVAAGQ EGVVVKAADA PYEAGRRGAA WVKVKPRHTL DLVVLAVERG SGRRAGTLSN
     IHLGARDPAT GGFVMLGKTF KGMTDEMLAW QTQRFRELEV ADDGWTVTLR PEQVVEIAFD
     GLQRSTRYPG GLALRFARVL RYRDDKPAAE ADTIETVHGY LT
//
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