UniProt: A0A0F4Z9G2

Database: UniProt
Entry: A0A0F4Z9G2_9PEZI

LinkDB:  A0A0F4Z9G2_9PEZI 
Original site:  A0A0F4Z9G2_9PEZI

All links

Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (12)   
   Pfam (5)   
   PROSITE (3)   
   SMART (1)   
All databases (31)   

Download RDF

ID   A0A0F4Z9G2_9PEZI        Unreviewed;      1035 AA.
AC   A0A0F4Z9G2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=TD95_004835 {ECO:0000313|EMBL:KKA26523.1};
OS   Thielaviopsis punctulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX   NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26523.1, ECO:0000313|Proteomes:UP000033483};
RN   [1] {ECO:0000313|EMBL:KKA26523.1, ECO:0000313|Proteomes:UP000033483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26523.1};
RA   Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC       required for double-strand break (DSB) repair.
CC       {ECO:0000256|ARBA:ARBA00043870}.
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:KKA26523.1}.
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; LAEV01002146; KKA26523.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4Z9G2; -.
DR   OrthoDB; 8251at2759; -.
DR   Proteomes; UP000033483; 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; IPR021536; DNA_ligase_IV_dom.
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   Pfam; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 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   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:UP000033483};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          427..581
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          755..834
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          918..1034
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   1035 AA;  117589 MW;  A3A063D5D62CF955 CRC64;
     MDKNTNPDPE AIDEDARQYA SLFKDESIAK RYPNRPQNLH RTLLFSELYR SLFDPLTQIQ
     KKPTGVAGRS KPTGVGATAA ANQPSKLTVY EQKRHVIDKF ISRWRQAVGP DFFPAMRLIL
     PDRDSDRAVY GLKEAAIGKL IVRLTKIDKN SDDGRSLLHW RVPGNTHASR MAGDFPGRCY
     NVIAKRPMCS TPGSMTIADV NEQLDRLAAA SGEAEKLAMF EMFYMRMCPK EMLWLIRIVL
     KQMRIGTSTR SLLHMWHRDA EALFNVSSSL RRVCWELYDP ATSLAQEDSV VRIGQCFQPQ
     LAQYQMPASF ERMVKYLRPE PGDAEFWIEE KLDGERMQMH MQTDPQVPGG KRFCWFSRRT
     KDYTYLYGSN LEERDSALTK YLKGCFDERL ENVILDGEMI TWDPQNDIIM PFGTLKTAAL
     NEKRRVESEQ GYQPFFIVFD ILYMNGHDLT KYTLRDRRAA LEQIVREHPA ETQSDKDAHI
     ANAPIKGIFR RLEVHSYIKT TSPDAIEPAL RDVIESSSEG LVLKNPRSMY RLNSRNDDWL
     KVKPEYMNEF GESLDCVVIG GFFGSGRRGN MLASFLCGLR ASENHIQAGA NPEKCWSFFR
     VGGGFNADDY QAIKHHTQGK WMPWDTRNPP TQFIELAGGS RQIERPDMWI RPCDSVVLEV
     KAANVTPSDC FATGKTLRFP RFRRLRLDKS WYSALSVDEF EELNARVNIE AQRNEEMTVE
     SRRRARPLKR PRKKLVIAGA QEDVEIKVPK QAEVANPELF AGMQFCIMSD AGKPLKKSKA
     ELEALVKAHG GTIKQHAGDD KNTILIADRK LVPVASAIKK GSFDIIQPQW LIDCTKQANG
     GFVLPYEARH LLHATSERMA RVPETIDRYG DSFARDITLQ ELRDVLAGMT GPDDTKNTAG
     IDFLHSLQEK GTDLHSGLRG YLFSGVSVVF RRSDGGVSGG LGVELEGILE RDELRLSNYV
     RFCSGTILEK LQEGVSHVII IGDDIEGARQ IKKEVERQVA GWDKKDAEPA IVWGAWIEEC
     WRKRTISDIT MYSVK
//

DBGET integrated database retrieval system