ID Q0U177_PHANO Unreviewed; 869 AA.
AC Q0U177;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=SNOG_14590 {ECO:0000313|EMBL:EAT78130.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT78130.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
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DR EMBL; CH445356; EAT78130.1; -; Genomic_DNA.
DR RefSeq; XP_001804772.1; XM_001804720.1.
DR AlphaFoldDB; Q0U177; -.
DR STRING; 321614.Q0U177; -.
DR EnsemblFungi; SNOT_14590; SNOT_14590; SNOG_14590.
DR GeneID; 5981697; -.
DR KEGG; pno:SNOG_14590; -.
DR VEuPathDB; FungiDB:JI435_145900; -.
DR eggNOG; KOG0967; Eukaryota.
DR HOGENOM; CLU_005138_1_1_1; -.
DR InParanoid; Q0U177; -.
DR OMA; RDFSCEY; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR GO; GO:0006266; P:DNA ligation; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR CDD; cd07900; Adenylation_DNA_ligase_I_Euk; 1.
DR CDD; cd07969; OBF_DNA_ligase_I; 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:UP000001055}.
FT DOMAIN 537..730
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 96820 MW; F3D48F106283F12C CRC64;
MNSPSKRRKK NDGSSQPVRK LEHFFARQTA KAAAKDAPNK ADEDQDATTL TDEEYARKLQ
EEWNREDQQQ AQATEPVSSN ELYEDAERPC VRVTAEEGAD TTTAVQRDSL KAEELVEPMP
PKQKNTLTLQ STATEEDTIT ANIPFDQSPL EFDPIKYIPD LQKHWAVDGG LATYALLTRC
FILINSTTSR IKIVDTLVNL LRTIIEGDPG SLLPAVWLAT NAISPPYIDL ELGLGGSAIS
KALKKVCGLD NAGLKVLNNK YGDAGDVAFE AKKKQSFTLR KPKPLTIKAV FDSLVKIANS
KGNGSVENKQ RIVERLVQDA RGAEESRYIV RTLVQHLRIG AVKTTMLIAL SRAFMLSEPP
SADFETRGQK ELAELKKEEL AEIYSRNEEI VKACFARRPN YNDLIPALLE IGVCDELLLR
CGLALHIPLR PMLGSITRDM GEMFTKLQGR DFACEYKYDG QRAQVHCDEK GKVTIFSRHL
EVMTDKYPDL VALVPQIRGE GVSSFILEGE VVAIDRNSGE LKTFQTLANR ARKDVAIGAV
TIDVCLFAFD LMYLNGEELL NRPFRERRSL LKSLFVEIPH TFTWVKCLDA TSADVDAVQA
FFQSALDIKC EGIMVKVLDN LPNPDLLDNT NDLNDKTPSL PPTPKKKKST KSKSKAKSTD
DGDKDEAKSH GRRKALLSTY EPDKRLDSWL KVKKDYSTTS ETLDLIPVGA FHGSGRKAAW
WSPILLAIRN AETGQLEAVT KCMSGFTDAF YKANRAKYDK DDPDCTTVLA SKPRYVEYNG
GAGTPDVWFE PQEVWEVAFA DLTLSPTYTA AIGLVSEERG LSTRFPRFLK VREDKGIDEA
TEAQELADLY RKQEAKAPRK EGDGEEEGD
//
