ID A0A3Q3LSZ0_9TELE Unreviewed; 1004 AA.
AC A0A3Q3LSZ0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000013291.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000013291.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
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 AlphaFoldDB; A0A3Q3LSZ0; -.
DR STRING; 205130.ENSMAMP00000013291; -.
DR Ensembl; ENSMAMT00000013658.2; ENSMAMP00000013291.2; ENSMAMG00000009016.2.
DR GeneTree; ENSGT00940000157783; -.
DR InParanoid; A0A3Q3LSZ0; -.
DR Proteomes; UP000261640; Unplaced.
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: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:UP000261640}.
FT DOMAIN 736..872
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 111378 MW; 8014D1BB5DB6FE5F CRC64;
MQRSIASFFQ PKSKDVQRKT TDDPVKKPVK SPLKVQNGVS EADSPIKKVV KRSRQILDSD
DDEAPAVKEQ VATNGQVDKE TPSKTGKKDD ASKAVPTPRF SPPPAVASPV TPATPATPAS
SVSSGTPGTP NSISPSGIVK RKTARKMFPK RKLDESRSGS ESQKEEAEVE EDQGQQNKRP
RVESSASSAG NTSEPMEEGA KEERVEKAVT ETSSPDEEVE NKKKEEGKKA EEEEQVGRKS
SDEKEKKAEG AEKKNEAKEK TDDEKGPAVA KEEAVEKDTR EGGDSPKSQT AKKQKDKEPA
KKAPISSFFA PRKAVVRMEK PENGGEKSTS AERKSSTEES KETKGESTSG QTDYDPSRPG
YHPVDHACWK QGQKVPYLAV ARTFEKIEED SGRLRNIETL SNLFRSVLLL SPDDLLCCVY
LCLNQLGPAY LGMELGVGET VLMKAVAQAT GRQLDKIKAE AQEKGDLGLV AESSRSNQRM
MFQPASLTAG GVFRKLKEIA SMSGNSAMNK KIDIIKGLFV ACRFSEARYI VRSLAGKLRI
GLAEQSILSA LSQAVCLTPS GQGFPPAVID AGKGMSAESR RAWIEEKSLI LKQTYCEMPN
YDVLIPVLLK EGIDQLPNHC KLTPGVPLRP MLAHPTKGVS EVMKKFDEAA FTCEYKYDGE
RAQIHILESG EVRIFSRNQE DNTSKYPDII SRIPKVKKDS VVSCVLDSEA VAWDREKKQI
QPFQVLTTRK RKDVDASEIK VQVCVYAFDL LYLNGESLVR QPLCRRRALL RESFSEVEGE
FVFARSIDSD NTDTIAEFLE QSVRDSCEGL MVKTLEKDAT YEIAKRSHNW LKLKKDYLEG
VGDTVDLCVI GAYLGKGKRT GTYGGFLLAC YDDENEEFQS VCKIGTGFKD EDLEQHYKFL
KEHLLPKPRA YYRVDQSAEP DVWLDAVQVW EVKCADLSLS PIYKAAMGMV DSVKGISLRF
PRFLRIRDDK KPEDATTGAQ IADLYKKQQQ IQNQGEKADL EDYY
//
