ID A0A0V1MXZ3_9BILA Unreviewed; 807 AA.
AC A0A0V1MXZ3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=lig1 {ECO:0000313|EMBL:KRZ76444.1};
GN ORFNames=T10_13396 {ECO:0000313|EMBL:KRZ76444.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ76444.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ76444.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ76444.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KRZ76444.1}.
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DR EMBL; JYDO01000028; KRZ76444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MXZ3; -.
DR STRING; 268474.A0A0V1MXZ3; -.
DR Proteomes; UP000054843; 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:UP000054843}.
FT DOMAIN 530..666
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 98..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 90742 MW; C4C6CE173A958C6C CRC64;
MNFGITVLRL FNRKFLFNTF CCKFPSKYSS IMSQASLTSF FAPKGSADSE KRILSKRKSE
LSSAQSSVEA SNSNPASVIS DVKTKDLSKV SEIDEKKRKV QKFDSNEDRS ENGSVKNASE
NSACTSKKGY TILAKEREQD VIEPKNYKPD ATTYDPECNA CWRAGEQVPY LAFAYTMKAI
ENTSSRLEII RILSNFFQSV IWLNPDDLLP CIYLCLNRLG PSYEAVELGI AEGTLQKAVA
QSTGRSMEKI KADIADKGDL GIVAEMSRNM QRTIFATRPL LVAGIFAKLN QIAHLSGSSS
MNKKLEMVKG LLVSCRDCEA RYLIRCLSGK MRIGLAEQSL LVALAHAFAF IERKKENKKK
LRDDALKEYL DECALIMKTA YCECPDYGKI VDIALRHGLH ALPEHCHITP GIPLKPMLAF
PSKGIEEVLK RFGSAEFACE WKYDGERAQI HFYDGTVKVF SRNQENHTGK YPDIVELIPK
VLSATNNKNN QTDPISSCII DSEIVAWNTE NQSILPFQVL STRKRKDAES GDVKVNVSVF
AFDLLYLNGQ SLTTQPFRER RSKLRSLIEE MDGHFFFTKS LVTNDSDEIG QFLEEAVKGN
CEGLMLKTLD KDATYEIAKR SHKWLKLKKD YLDNTGDTLD LVVIGGYLGV GRRVGVYGGY
LLACYHPATE EYQSICKIGT GFKDEDLQKQ AEYFKQHIIS VPKSYYRYSS SLAPDHWFDP
VQVWEVKAAD LSISPKHFAA IGIVDDEKGI SLRFPRFIRV RDDKNPEDAT TAEEVAEIYY
NQESVKNAKA AATKDVHSDD NDADDDF
//
