GenomeNet

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   24-JAN-2024, entry version 47.
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; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; 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., Shao J.,
RA   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:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003,
CC         ECO:0000256|RuleBase:RU000617};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK94918.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWSO01000118; ESK94918.1; -; Genomic_DNA.
DR   RefSeq; XP_007845801.1; XM_007847610.1.
DR   AlphaFoldDB; V2X6X4; -.
DR   STRING; 1381753.V2X6X4; -.
DR   KEGG; mrr:Moror_14085; -.
DR   HOGENOM; CLU_004844_1_0_1; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd18435; BRCT_BRC1_like_rpt1; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR044125; Adenylation_DNA_ligase_IV.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 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; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 2.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          372..506
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          667..749
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          929..1035
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..819
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..852
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..884
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//
DBGET integrated database retrieval system