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Database: UniProt
Entry: A0A094AY80_9PEZI
LinkDB: A0A094AY80_9PEZI
Original site: A0A094AY80_9PEZI 
ID   A0A094AY80_9PEZI        Unreviewed;      1002 AA.
AC   A0A094AY80;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=V493_03091 {ECO:0000313|EMBL:KFY28085.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY28085.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY28085.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in ds DNA break repair. Has a role in non-homologous
CC       integration (NHI) pathways where it is required in the final step of
CC       non-homologous end-joining. {ECO:0000256|ARBA:ARBA00002476}.
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:KFY28085.1}.
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DR   EMBL; JPJV01001209; KFY28085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AY80; -.
DR   STRING; 1420906.A0A094AY80; -.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000029327; 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; cd17722; BRCT_DNA_ligase_IV_rpt1; 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; 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; 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; 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|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:UP000029327};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          434..559
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          726..808
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1002 AA;  114920 MW;  E0C682AF9B691623 CRC64;
     MSSQRTPRHI DKEAREDDDL QYGHGPLSKE ELEAKYPNRP INQHKTLPFH ELLVSLFTPL
     SENKKKPTGP SATGRAKRGP HGPTHQSPHE VRRIIIERFI SRWRSDVGHD FYPALRLIIP
     EKDRDRAMYG LKEKTIGRLL VKLMKIDKNS EDGYNLLNWK LPGQTFASRM AGDFAGRCFE
     VLSKRPMRTS MGNMRIAEVN QLLDQLSSAP KEEAQLPIFQ IFYNRMNADE LMWLIRIILR
     QMKVGASEKT FLDLWHPDGE TLFNVSSSLR RVCWELTDPS IRLEGNETGV TLMQCFQPQL
     AQFQMHSFQK MVDNMRPTPD DTEFWIEEKL DGERMQMHMV EDDSVPGGKR FGFWSRKAKD
     YTYLYGSGFE DENCAITRHL KGAFDLGVRN LILDGEMITW DPEADIMVPF GTLKTAAISE
     QRNPFAGNGP RPLFRIFDII YLNDEPLTQY TLRDRRRALE RCVTNVHRRF EVHSYTPAYS
     VEAIDPLLRK VVAEASEGLV LKNPRSIYRL NSRNDDWMKV KPEYMTGFGE SLDCVIIGGY
     YGSGRRGGRL SSFLCGLRVD QNHIQKGADP MKCYSFFKVG GGFKAEDYAN IRHHTENKWV
     DWDPKKPPTN LIELAGGEAQ LERPDVWIRP CDSVVVSVKA ASVSASDSFK TGLTLRFPRF
     KHLRLDRDWS TSLSIQEFIN LKSRLEEESR EKEFTVDTRR KAARTSKKPL LVAGDENKMT
     KPYVGQGSEA FHGLNFCVLS EATKSPKKSK AELEQYIKAN GGSIFQSPTI QADTIVIADK
     KVVKVASIIK SGLQNVVRPR WLFDAVQQYE ADLGREKHLV PFEPRHMFYT INQEVEMIEQ
     NVDRFGDSYA RDVGATEMKE ICDDMPKEEQ ESGFETDKLL SQLQWQHHNL DLRDMKGFMF
     SGFRAHIASW QACEGVANLS EDGLRCLLVE HKLRFGLASM AWDLEDTSIT HIVVPGSIDT
     LGSIREKISH RRVVPRTVTL EWVEDSWREG TLLDEDRYAP RG
//
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