ID A0A0V1A4E5_9BILA Unreviewed; 2503 AA.
AC A0A0V1A4E5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN Name=mau2 {ECO:0000313|EMBL:KRY19723.1};
GN ORFNames=T12_1345 {ECO:0000313|EMBL:KRY19723.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY19723.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY19723.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY19723.1};
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 -!- FUNCTION: Required for association of the cohesin complex with
CC chromatin during interphase. Plays a role in sister chromatid cohesion
CC and normal progression through prometaphase.
CC {ECO:0000256|ARBA:ARBA00025632}.
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 -!- SIMILARITY: Belongs to the MON1/SAND family.
CC {ECO:0000256|ARBA:ARBA00008968}.
CC -!- SIMILARITY: Belongs to the SCC4/mau-2 family.
CC {ECO:0000256|ARBA:ARBA00008585}.
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:KRY19723.1}.
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DR EMBL; JYDQ01000032; KRY19723.1; -; Genomic_DNA.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
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 GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR CDD; cd14089; STKc_MAPKAPK; 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; 4.10.1170.10; MAP kinase activated protein kinase 2; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029710; LIG4.
DR InterPro; IPR027442; MAPKAPK_C.
DR InterPro; IPR019440; MAU2.
DR InterPro; IPR004353; Mon1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR Pfam; PF10345; Cohesin_load; 2.
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; PF19036; Fuz_longin_1; 1.
DR Pfam; PF19037; Fuz_longin_2; 1.
DR Pfam; PF19038; Fuz_longin_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01546; YEAST73DUF.
DR SMART; SM00220; S_TKc; 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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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 Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1181..1444
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1855..1991
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 2175..2257
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT BINDING 1210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2503 AA; 285774 MW; 31CFAC6D46156EDC CRC64;
MLPFHDACYL GLLSMAEDFR TRSPPEIVNA LRCLLSIFEF SPPIVIEARL HFQVGHMYWS
FTENIDHARQ HLERAITLAR SHRAFEDVLS DAAYSLAQLY FKTNENALGR NLLYQTIETL
KNCQGMFCRQ IRLVFQLAQH LVNDRDYITA REVLQLGYQA AVNENCIYIR IMILLSISQL
YMFESRVKEL HQTLIGKDHR FVGPIFEPGK AKSSKACLIE LQQLVQMITH TGHQEQKDEQ
QQYEYFQWIS DEHLCILVYA MTVMEALHCG KFNKARQYAE RALAHVEKLR RLNQEDNMAQ
GLWLLLLEHS ILSQLNTGHY VSAVKEISLL KSACHCNPRL FYQYGSRLHM LLGLYAVSMD
QAQAGEAQFA AALRFNRDPK LSFYLNLNLA VLYLQCGRES EFYNLMDISP ERLADQSVNL
RAASLFVRGM HLMLQRRYPE AKKVLCEALE LTSKEDLNHL VSFCFVLIGQ MLLGVNPRPE
HLQEALKLFT SSFHLAQSSS DVTAQVWSSG ALKNLYAICQ NADQQKHYGQ LEGDLVRGML
QEQEHSRQLA EHQLINITDL MDQFNVCDFR SVSDGEITKS GVVRELLHHF RVLLLKLLLN
LCMAEISQAS SHVDAFNVPR CVPDDKKSDE TTESELPPYR SVPKITDEME TLAITEQILD
TVICDKLSVF CEESLHLHSC SRSSEPRSSD ALQSYVTTLL SDHDKHVFVL SDAGKPVYTR
HCSEEELSSL MGVIQALVSF VSSQNEGDEL QTIRAGVWTF VFSHRAPLIL CLVSRRSDSA
EQLSRQLDLV HRQILTMLTQ VQLSRIFEER KNFDLRRLLA GTERTLERLI LVMETDFSLL
LNAVRCYTLP HSTRETIVQA MSSCCSQPKC IVFAVLLVHD QLVAYSGKKK ATLSPSDLAL
LINLVASNIS FKDAESWSPI CLPAYDENTF LSAHISYLTE NSPACLLLLT AEKDSFFTMS
EVRNKIIDKF TRTKALAILN ELQQERKRFE INELGIPDLI HFIYKHRTKS QFTSMSLSLP
YREEYFEKHL FNRYLLIHNF MHSEKHKHNI FYVTGDLENI LGWVTTAFEI YAVFNPLITK
PEAVSRVEQL MKWIKKEENN LFLINPGHMS SKSTTVMNNV QSAVKVVDGR SDVVSALKKK
SSASDTVENN GADDKQQFSF TYDANGVHLK PLTRMITEDY RVSKTVLGVG LNGKVVECFK
RKTGEKFALK VLCDTPKARR EVELHCLARN HKNIVTIYDV YLNSFSNTKC LLIVMECMEG
GELFSRIQRR GEHAFTEREA ASIMYDICSA VRFLHSLQIA HRDIKPENLL YTKLTDDAVI
KLTDFGFAKR TEPSAVKSLE TPCYTPYYVA PEILGTEKYD KSCDMWSLGV VMYILLCGFP
PFYSSHGLPM SPGMKSRIRS GQYVFPSPEW DNVSESAKDL IRGLLKTDPS ARLRIDQVMN
HSWITGCKAV PETPLCTVSV LSEKKVIWND VQEEMSNALA SMRVDCDQMQ IKNLSDSKNK
LLEKRKKRLF GLKLKMEQSC CSIESEIPFR DLCSILRACA STRNQAEKRR ILGKFFHCWR
ERFKRKYENS VANSNSSVES FFPILRLLVP KLDNARGPIG LKENMLAKKF IQIMAIDKNS
PDAKALLGFH LPATKWKMSS TTTGKSDVDF AALISSMLKS RVLANVDGEI SLFDINRCLD
HLASAHANRS RDQVEKQIDW CCRNLNSEQF KWFVRIVLKD VRLWDNSSMD DDGYCCSVEL
FKAYRPMLAT LIFPGSRICQ IFSGSKFYVE TKFDGERVQL HKDENNNYKY FSRNGIDFTS
SYGSTPFVGN LTQFIHGAFE NHVRNCILDG EMIAWDRTAK RFVGKGEHVD VKGLKFDSPL
NPCYMVFDCL LLNDRPLAGL PLGERLEQLR SAVRDIPERM QIVDQQLVDS ADQVIELLNE
TVGRGEEGIM VKDPASLYKP NARTSSAGWF KIKPDYINGL VDDLDVLIVG GYFGTGRRSN
LLSHFMIALM ENYDKKIIAT VDDCNFSTPR FVALGRVGSG YSLKELYDFN AKLVQLRLKR
GQPPPWLKLG VEKPEVYIHP EQSTIVQVKA AQIVTSGQFP LGFTLRFPRV QAIRHDKTWR
DCMTVEQFLN FKDLSADCTS KRLAEMKNDN NDQIMNWKTI SKKPKRKAIV AADRRCRVEA
MKNLDQSKRM RKFKPISNIF QGRELCILNG NDTFTKENLE GKVVELGGTV VQHPVAGRQT
VKVKSVVRAS TVDVLKLSWL IRCIQTNSFI QWTPNDMLLT TATMKRHFKR NFDQYGDSYT
DPVDSETLHD LLATVPVEKT DVDDSKSQKF LSTISYKYGI FLNCTIYLDF YDDLFSPLRR
RIALSALDRY ELLLYEFRAN IVDTLTDSLT HTLCSAFVNF VQLQRLILLF SQSSDLSRLD
DLLRFKSDFN ANFHIVTESW VTHCIGEFAI VDESLHSART SGESHPAIID EEEVEEGWAE
ASQKQRDFHR KRLPPNEALL KHLGQDSGHS NCLGTDGATL HSI
//
