ID A0A177DS01_ALTAL Unreviewed; 893 AA.
AC A0A177DS01;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=AA0117_g54 {ECO:0000313|EMBL:RYN83791.1}, CC77DRAFT_1007425
GN {ECO:0000313|EMBL:OAG21921.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG21921.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG21921.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG21921.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN83791.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN83791.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
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; KV441475; OAG21921.1; -; Genomic_DNA.
DR EMBL; PDXD01000001; RYN83791.1; -; Genomic_DNA.
DR RefSeq; XP_018387342.1; XM_018523478.1.
DR STRING; 5599.A0A177DS01; -.
DR GeneID; 29109072; -.
DR KEGG; aalt:CC77DRAFT_1007425; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1007425; -.
DR OMA; WIKYKRD; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; 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; 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:SF4; DNA LIGASE 1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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; PS00333; DNA_LIGASE_A2; 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:UP000077248}.
FT DOMAIN 620..757
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 99258 MW; F49B557ABE0EB528 CRC64;
MAPKQATLGK FFGKPNGDAT KQQSKLSFST RPKPVKNEVE TKEEPRSSPE EVKEGQNDDV
DSDAEVRAPV KKEVETDDDA MEVDSTASDT GKKRQIKEEE EEESEEEPPT KRQRRKTTEG
KNSPKKAPAK PKADKAPEKS KKRAAKPKAA TPEDDDEEVS APTKVAKSKK GAESSPVPVE
DDAVSNKEEE DEVGSSEEEP EEVKTKARKK VQTTLSSNIK DPYPDWKPGE PVPYAALCTT
FSKIEMTTKR LEILAHCSLF LRQVLRLTPS DMLPTVMLMV NKLAADYAGI ELGIGESLIM
KAISESTGRN LQQIKSDQNE IGDLGLVAAK SRSKQPTMFK PKSLTIEGVR KGLIGIATVE
GQGAQGRKVD GIKKLLSAAD AHNAGKHIDI EKDKGGPSEA KFIVRTLEGK LRLGLAEKTV
VVAVAQAMIF HDMSQEGKTP STADLAKAEA MLKTVYSELP SYEVIIPAML EHGIMNLREN
CRLQPGVPLK PMLAKPTKSI TEVLDRFEGK DFTCEYKYDG ERAQIHFVAH DAKQEGEKME
LATIAPSAGK SDRGVSNIFS RNSEDLSKKY PDILAKLPTW VKEGTKSFVL DCETVAWDMV
EKKVLPFQQL MTRKRKDVKV EDVKVKVCVF AFDILYLNGE ALVTKSFRER REHLNEVFVP
VEGEFAFAKY GNTNELEEIQ TLLEDSVKSG SEGLMVKMLD GPESFYEPSK RSQNWLKVKK
DYLAGVGDSL DLVVLGAYYG KGKRTSWYGA FLLACYNPST EKYETVCNIG TGFSEAILET
LHKTLSEIVI DRPKPFYTHS TGNKDQPDVW FEPRYVWEVK TADLTLSPRY RAAADEVSGG
GKGVSLRFPR FIKERDDKKP DQASSSRMIA EMYQRQESVS KNKGPSADDD FEY
//
