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Database: UniProt/TrEMBL
Entry: R1GCB1_BOTPV
LinkDB: R1GCB1_BOTPV
Original site: R1GCB1_BOTPV 
ID   R1GCB1_BOTPV            Unreviewed;      1025 AA.
AC   R1GCB1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   07-JUN-2017, entry version 23.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=UCRNP2_7417 {ECO:0000313|EMBL:EOD45866.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetes incertae sedis; Botryosphaeriales;
OC   Botryosphaeriaceae; Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD45866.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomeA.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a
RT   fungal vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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; KB916531; EOD45866.1; -; Genomic_DNA.
DR   RefSeq; XP_007586672.1; XM_007586610.1.
DR   EnsemblFungi; EOD45866; EOD45866; UCRNP2_7417.
DR   GeneID; 19027011; -.
DR   KEGG; npa:UCRNP2_7417; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000013521; 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   CDD; cd00027; BRCT; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 1.
DR   Pfam; PF16589; BRCT_2; 1.
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   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
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:UP000013521};
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, ECO:0000313|EMBL:EOD45866.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT   DOMAIN      432    555       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      728    807       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      952   1024       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   1025 AA;  115997 MW;  D036661A1688E42D CRC64;
     MAGASVMQSQ EAVDEEKRQY GHGSMTEEEL DEKYPNRPHN HSKTLPFHTL YLDLFNPLND
     NKKKPTGPPT ARRRQGPHGQ AHMTPNEIRR NIIERFISRW RQEVGSDIYP AFRLIVPEKD
     RDRAMYGLKE KAIGKLLVRV LRIDKDSEDG FNLLNWKLPG QKATVAMAGD FAGRCFDVIS
     KRPILTKPGN MTIAEVNERL DKLSVVSKEE DQLPIFQEFY QRMNAEEMMW LIRVILRQMK
     VGATERTIFS IWHPDAESLF NVSSSLRRVC WELYDPSIRL DGDETGVNLM QCFQPQLAAF
     QMHSFEKMVQ RMKPTEDDDE FWIEEKLDGE RMQLHMIEDE SVPGGKRFGF WSRKAKDYTY
     LYGSSFEDDD SALTRHLKEA FHSGVRNIIL DGEMITWDME QDAMVPFGTL KTAALSEQKN
     PYSTGQRPLY KIFDLLYLND EPLTKYTLRD RRKALDTSIH PVHRRFEIHT YTTANSPGEI
     EPLLRKVVSE ASEGLVIKNP RSMYRLNQRN DDWIKVKPEY MTEFGEELDC VIVGGYYGSG
     HRGGRLSSFL CGLRVDQNQI ERGANPMKCF SFFKVGGGMT AADYAAIRHN TNDKWQKWDP
     KRPPTEYIEL AGGDRQYERP DVWIKPCDSV VVSVKAASVG TTEQFRMGMT LRFPRFKKLR
     ADKSWKDALS IQDFLTLKSN AEQAHAEKEF KVDDGRRKRQ RTTRKRPMTV AGFDDASRSP
     TAADDASSRP QVFAGLTFYI MTDALAPKTP KPDLEALVKA HGGRLVHSPT AAPHVVCVAD
     RRLVPVASLV KKNERSVVRP AWLLDCVAQA AADAALGRAT DDGVPPLLLP YEGRRHLFHA
     TDDDAVQADG AVDAWGDSFA RDVASGAELK RDVLDRMAVP PVKAEEENDD VVVGARFLDQ
     MEERDVPLFG DGEVSGWLFR GARVWFDDDD DDDDDDAGSP AAAATRLYLA AQVVRFAGGA
     VAAGLGEEGV TQVVVAPGVR KERLREIREA VAAKGGPVPR VVSVEWVEES WKERTLLDEE
     RFVAL
//
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