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Database: UniProt
Entry: A0A2B7XQV8_9EURO
LinkDB: A0A2B7XQV8_9EURO
Original site: A0A2B7XQV8_9EURO 
ID   A0A2B7XQV8_9EURO        Unreviewed;       849 AA.
AC   A0A2B7XQV8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=AJ79_04941 {ECO:0000313|EMBL:PGH11325.1};
OS   Helicocarpus griseus UAMH5409.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX   NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH11325.1, ECO:0000313|Proteomes:UP000223968};
RN   [1] {ECO:0000313|EMBL:PGH11325.1, ECO:0000313|Proteomes:UP000223968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH11325.1,
RC   ECO:0000313|Proteomes:UP000223968};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:PGH11325.1}.
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DR   EMBL; PDNB01000074; PGH11325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XQV8; -.
DR   STRING; 1447875.A0A2B7XQV8; -.
DR   OrthoDB; 961at2759; -.
DR   Proteomes; UP000223968; 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
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; 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   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
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|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223968}.
FT   DOMAIN          529..708
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  94303 MW;  574FBF351C3B23D7 CRC64;
     MSSPAKKRKT NDSKPASQRT RGIESFFTSR NATPTATPPS QPEPQASLTD EELARKLQAE
     WDEETKPDLR GSGALQGDLT PTRQDSKPEN HNQQLDLQSQ APTPSSASVP RIDNSKSVLS
     LQTSSNAEDN ISQSIPFDQS PLTFDPSNYA EPLRAHWAVE GGRASYGVLT KAFVLVNSTQ
     SRIKIVDTLV NVLRIIIEAD PDSLVPAVWL ATNAIAPPYV PVELGLGGSA ISKALKTAYG
     LNNHGLKTLY EKHGDAGDVA FEAKKRQTFT LRKPRPLSIR GVYESLLKIS RSKGQGSQEA
     KQRIVEKLLR DARGAEESRY IVRTLVQHLR IGAVKTTMLI ALARAFLYSK PVKSDFSVYD
     PAHLAKLKKE EIANIYSRAE EIVKACYARH PNYNDLVPCL LEIGISEELL VRCGITLHIP
     LLPMLGSITR DLAQMLTKLQ GRAFTCEYKY DGQRAQVHCD SSGKVSIFSR HLELMTEKYP
     DLVALIPRIR GEGVSSFILE GEIVAVNQES GELLAFQTLT NRAKKNVGID SIKISVCLFA
     FDLMLLNGEP LLDRPLRERR ELLRGLFIEV PHHFTWVKSL DATSSDSEAV LSFFKGATDS
     KCEGLMVKLL DDAALPELSK EESVAGPVLN SDLPVTPAPV EPNGNTRGKN RRSLLSTYEP
     DKRLESWLKV KKDYSASSDT LDLIPIAGWH GQGRKAKWWS PILLAVRNPE SGLLEAVTKC
     MSGFTDKFYQ ANKEKYAEDG DNVISRPSYV DYRSEPEVWF EPQEVWEVAF ADITLSPTYT
     AAIGLVSEER GLSLRFPRFL RGREDKTIDE ASTSEYLASL WRKQTERLRK EGEIAEPAAE
     NDPLGLDED
//
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