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Database: UniProt/TrEMBL
Entry: V2X6X4_MONRO
LinkDB: V2X6X4_MONRO
Original site: V2X6X4_MONRO 
ID   V2X6X4_MONRO            Unreviewed;      1044 AA.
AC   V2X6X4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, 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=Moror_14085 {ECO:0000313|EMBL:ESK94918.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Marasmiaceae;
OC   mitosporic Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK94918.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK94918.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94918.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E.,
RA   Shao J., Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ESK94918.1}.
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DR   EMBL; AWSO01000118; ESK94918.1; -; Genomic_DNA.
DR   RefSeq; XP_007845801.1; XM_007847610.1.
DR   EnsemblFungi; ESK94918; ESK94918; Moror_14085.
DR   GeneID; 19284983; -.
DR   KEGG; mrr:Moror_14085; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000017559; 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; PF00533; BRCT; 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   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:UP000017559};
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:ESK94918.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN      372    506       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      667    749       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      929   1035       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   1044 AA;  119017 MW;  113EA32073439C5A CRC64;
     MMQPTPAPTS PPRSPPPAEY EHEQNYPIPP QNMGSAPFSV LVGLFEKLQN ERRQERRKKL
     ISAWFDHWRE EVGNDLYPVL RLILPQKDRE RAVYGLKEKN LAKTYIKLIP LQRQDPDAQR
     LMNWKKPDER NKASGDFPTV LYEVVSKRSS VIEGSLSIED LNEILDELSK SMGKQDVQSK
     ILQRVYNRTT PEEQRWIVRI ILKDMVISVK ETTVFSVFHP DAMDLYNTCS DLKKVAWTLW
     NTSNKLHEDQ KNVSLFQAFA PMLCKRPTRT IEQTVNEMGG SEFIIEEKLD GERMQLHKRG
     NEYFYCSRKG KDYTYLYGKH VGVGSLTPYI HKAFHPGVEN IILDGEMLVW DPVSERNLPF
     GTLKTAALDK SKKELNPRPC FKIFDLLYLN NKSLLDRTTS SRKKNLRNCL TEVKGRVEFV
     EDFKGKTAKD VREKMEEIMN NRGEGLVVKH PRSKYVLNGR NMDWIKVKPE YMDNMGETVD
     VLVVAGNYGT GSRGGGVSTL ICAVVDDRGA NKESADTEDK KYSTFVRIGS GLSYSDYAWV
     RDKPWKVRDP KNPPEWLQVS KKGQEDKGDV YLEPSDSFIL KVKAAEIVPS EQYHMGYTMR
     FPRALAIRGD MDVENCMRAT EVEDSLKSER KRKMENNAEV TKKRKITAKK AMILPSYQGP
     SAKDFQRRSN IFEGLKFVVI PDPKSRTGNE DKANLVKIIC ENGGSCAQIA TNQPDLFVVY
     GGSMTPYNVK LIIDKGIHDI IKPEWVRDSD ALKGRAPLSK RYFFHATASR EDTDEYQREE
     DEEQPSIADE ETSHPVDLTE GEDSKMSDNK PDLRTRDQGR ASEIAPSNGT KLDPRLAAWL
     KPEDDSHDAT EKSSAGAADA SETESEYDSD NADVTEDAEQ VKEEDLDDWF STRADDLNET
     APASSLKEGD SQVKGPIKMG EDDSVMEYDQ NLIFKHLCFY LDSPASAHQH GMSIKTRSPE
     EINQSFNNLR MLIIENGGRV VDLDEPKLTH VVLDKRDTGR RTELLKRTSK PKRRHLIISE
     YIQACIDEGT LLNEDGKCGV FFRC
//
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