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Database: UniProt
Entry: A0A0D0ECB1_9HOMO
LinkDB: A0A0D0ECB1_9HOMO
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ID   A0A0D0ECB1_9HOMO        Unreviewed;       903 AA.
AC   A0A0D0ECB1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PAXRUDRAFT_794423 {ECO:0000313|EMBL:KIK99060.1};
OS   Paxillus rubicundulus Ve08.2h10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Paxilineae; Paxillaceae;
OC   Paxillus.
OX   NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK99060.1, ECO:0000313|Proteomes:UP000054538};
RN   [1] {ECO:0000313|EMBL:KIK99060.1, ECO:0000313|Proteomes:UP000054538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK99060.1,
RC   ECO:0000313|Proteomes:UP000054538};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; KN824871; KIK99060.1; -; Genomic_DNA.
DR   EnsemblFungi; KIK99060; KIK99060; PAXRUDRAFT_794423.
DR   Proteomes; UP000054538; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
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-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3260.10; -; 1.
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|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054538};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054538}.
FT   DOMAIN      582    744       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
SQ   SEQUENCE   903 AA;  100469 MW;  2BA0536BF3BE5FC8 CRC64;
     MSKRTSSTPS TRNKKRARVV TDQAVLDTYF RNPIRPPSPT KGQHTATNTR RAQLGNHDQR
     SAVISDEQST SLVSGEEPYR PELFQGEHHW HHHGTQARPI QLDSDEDYHP KAEGTAGQES
     IAGPSHLSPL APSLPPSEVH SHLSVKGHND FPKFGPSALG STGHSPPVDY SSVAVDPLVY
     PIDICPWRLG SPAPYSFLVN AFVALAETRS RIAILNALTN TLRCFLLYDP TSLLPALYLL
     SNSLSPPYSP IELGIGVSVI SKAIQHVSGL TPSALRKLYN SSGDPGDVAF EAKSNVRTLV
     PHPPLHIKVV YESLLKIANL KGQGAARQKQ SIVERLLVSA TGEETRYLVR TLSLNLRVGA
     VRTSMLTALA RALVLTPPSN PSLPRQVESL YYATPHPTPS AKSLRSDTKK RTADPQRDEL
     LVKFARAEAL VKQVYVQHPN YDHIVEGILE GDLDGLSKRV PLTVGIPLHP TLGSPTRSLD
     EIYDRLGELQ FAAEFKYDGQ RAQIHASRVG GDNPQVHIFS RHLENMTTKY PDVVSLVRCM
     FERASNLQSF IIDSEVVAID PTDGGLRSFQ ELSNRAKKDV EIKGIKVPVC AFAFDLMYLD
     GEALLERPFR ERRALLRTRF PILAPEEPGI ARFDHVESCE SEQGREYIEE FWQKAVESRC
     EGLMVKLLDN GQIQEDVPHQ KCKSRNKHLP ATYEPDKRTC AWLKLKKDYV EGLGDTLDLV
     PVGAWHGNGR KAGWWSPLLL AVWDPAKEKL VAVCKCMSDL GVTKFSTGFS DAFYKDLSSR
     YAEDSDNCSR QPLWECETGG FKPDVYFRPH EVWEIRGADV TLSPVSLAAL GEVSATRGMS
     LRFPRFVRVR EDKDREQAST PQFLARMYRD EQSRGKDMTG VDDGDLVDME LEADEQIEED
     SGD
//
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