GenomeNet

Database: UniProt/TrEMBL
Entry: D2BAP0_STRRD
LinkDB: D2BAP0_STRRD
Original site: D2BAP0_STRRD 
ID   D2BAP0_STRRD            Unreviewed;       508 AA.
AC   D2BAP0;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   25-OCT-2017, entry version 56.
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=Sros_7176 {ECO:0000313|EMBL:ACZ89870.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 /
OS   NI 9100).
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ89870.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ89870.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001814; ACZ89870.1; -; Genomic_DNA.
DR   RefSeq; WP_012893600.1; NC_013595.1.
DR   ProteinModelPortal; D2BAP0; -.
DR   STRING; 479432.Sros_7176; -.
DR   EnsemblBacteria; ACZ89870; ACZ89870; Sros_7176.
DR   KEGG; sro:Sros_7176; -.
DR   eggNOG; ENOG4107RYT; Bacteria.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG091H0BGA; -.
DR   Proteomes; UP000002029; 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; -; 1.
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; IPR012308; DNA_ligase_ATP-dep_N.
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   Pfam; PF04675; DNA_ligase_A_N; 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; 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:UP000002029};
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:ACZ89870.1};
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:UP000002029}.
FT   DOMAIN      288    412       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    211    211       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     209    209       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     216    216       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     231    231       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     260    260       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     372    372       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   508 AA;  54506 MW;  43692F64EB3D1C86 CRC64;
     MLLIDLARTS AAVTADSARL AKIGHLAELL GRVDADEAEI AISYLSGELP QRHIGVGWAG
     LQDPPDPRLA ATATLRQVND LLDRIKAQAG PGSQAARKAL IIELFAALTR QEQTFLSRLL
     RSELRQGALD GVMIEAIAKA SAVPTAEVRR ALTLRGWLPA VGAAALSGGV NALRAFHLEV
     GRPVSPMLAQ SATSVAAALG KLGGPAAIEW KLDGVRVQAH RSGDAVSVFT RTLDDITAQV
     PELVEAVRAL SSQDLVLDGE VIALRPDGRP EPFQVTSGRV SSRIDVARVR ERTPLRVFFF
     DALRVDGVDL LDLPGEVRHA ALAATVPSEL VTPRLVTGDA ASGEAFFKDV VRAGHEGVVV
     KSLQTPYAAG RRGAGWIKVK PRHTLDLVVL AAEWGSGRRE GRLSNLHLGA RDPQTGGFVM
     LGKTFKGLTD EVLAWQTERF LEIAEGPTDG WTVVVRPELV VEIAFDGVQQ SPRYPGGMAL
     RFARVVRYRP DKNADQADTV EMVRSLML
//
DBGET integrated database retrieval system