ID A0A0V0S7H3_9BILA Unreviewed; 2504 AA.
AC A0A0V0S7H3;
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=LIG4 {ECO:0000313|EMBL:KRX22583.1};
GN ORFNames=T07_509 {ECO:0000313|EMBL:KRX22583.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22583.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22583.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22583.1};
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:KRX22583.1}.
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DR EMBL; JYDL01000030; KRX22583.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0S7H3; -.
DR Proteomes; UP000054630; 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; PF00533; BRCT; 1.
DR Pfam; PF10345; Cohesin_load; 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 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; SM00292; BRCT; 2.
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; 1.
DR PROSITE; PS50172; BRCT; 2.
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:UP000054630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1186..1446
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1857..1993
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 2177..2259
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 2318..2423
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT BINDING 1215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2504 AA; 285497 MW; 56E671048E7C7560 CRC64;
MLPFHDACYL GLLSMAEDFR TRSPPEIVNA LRCLLSIFEF SPPIVIEARL HFQVGHMYWS
FTENIDHARQ HLERAITLAR SHRAFEDVLS DAAYSLAQLY FKTNENALGR NLLYQTIETL
KNCQGMFCRQ IRLVFQLAQH LVNDRDYITA REVLQLGYQA AVNENCIYIR IMILLSISQL
YMFESRVKEL HQTLSKVSQL IDSWQGSSIR KAKSSKACLI ELQQLVQMIT HTGHQEQKDE
QQQYEYFQWI SDEHLCILVY AMTVMEALHC GKFNKARQYA ERALAHVEKL RRLNEEDNMA
QGLWLLLLEH SILSQLNTGH YVSAVKEISL IKSACHCNPR LFYQYGSRLH MLLGLYAVSM
DQAQAGEAQF AAALRFNRDP KLSFYLNLNL AVLYLHCGRE SEFYNLMDIS PERLAEQSVN
LRAASLFVRG MHLMLQRRYP EAKKVLCDAL EVTSKEDLNH LVSFCFVLIG QMLLGVNPRP
EHLQEALKLF TSSLHLAQSS ADVTAQVWSS GALKNLYAIC QNADQQKHYG QLEGDLVRGM
LQEQEHSRQL AEHQLINITD LMDLCDFRSV SDGEITKLTR SGVLLHCFRV LLLKLLLNLC
MAEISQASSH VDAFSVPRCV PDDKKSDETT ESELPPYRSV PKITDEMETL AITEQILDTV
ICDKLSVFCE ESLHLHSCSR SSEPRSSDAL QSYVTTLLSD HDKHVFVLSD AGKPVYTRHG
SEEELSSLMG VIQALVSFVS SQNEGDELQT IRAGVWTFVF SHRAPLILCL VSRRSDSAEQ
LSRQLDLVHR QILTVLTQVQ LSRIFEERKN FDLRRLLAGT ERTLERLILV METDFSLLLN
AVRCYTLPHS TRETIVQAMS SCCSQPKCIV FAVLLVHDQL VAYSGKKKAT LSPSDLALLI
NLVASNISFK DAESWSPICL PAYDENTFLS AHISYLTENS PACLLLLTAE KDSFFTMSEV
RNKIIDVSIH SVHKFTRTKA LAILNELQQE RKRFEINELG IPDLIHFIYK HRTKSQFTSM
SLSLPYREEY FEKYLFNRYL LIHNFMHSEK HKHNIFYVTG DLENILGWVT IAFEIYAVFN
PLITKPEAVS RVEQLMKWIK KEENNLFLIN PGHMSSKSTT VMNNVQSTVK VVDGRSDVVS
ALKKKSSASD TVENNGADDK QQFSFTYDAN GVHLKPLTRM ITEDYRVSKT VLGVGLNGKV
VECFKRKTGE KFALKVLCDT PKARREVELH CLARNHKNIV TIYDVYLNSF SNTKCLLIVM
ECMEGGELFS RIQRRGEHAF TEREAASIMY DICSAVRFLH SLQIAHRDIK PENLLYTKLT
DDAVIKLTDF GFAKRTEPSA VKSLETPCYT PYYVAPEILG TEKYDKSCDM WSLGVVILCG
FPPFYSSHGL PMSPGMKSRI RSGQYVFPSP EWDNVSESAK DLIRGLLKTD PSARLRIDQV
MNHSWITGCK AVPETPLCTV SVLSEKKVIW NDVQEEMSNA LASMRVDCDQ MQIKNLSDSK
NKLLEKRKKR LFGLKLKMEQ SRCSIESEIP FRDLCSIFQA CASTRNQAEK RRILGKFFHC
WRERFKRKYE NSLANSNSSV ESFFPILRLL VPKLDNARGP IGLKENMLAK KFIQIMAIDK
NSPDAKALLG FHLPATKWKM SSTTTGKSDV DFAALISSML KSRVLANVDE EISLFDINRC
LDHLASAHAN RSRDQVEKQI DWCCRNLNSE QFKWFVRIVL KDVRLWESSS TDDDGYCCSV
ELFKAYRPML ATLIFPGNRI CQIFSGSKFY VETKFDGERV QLHKDENNNY KYFSRNGIDF
TSSYGSTPFV GNLTQFIHGA FENHVRNCIL DGEMIAWDRT AKRFVGKGEH VDVKGLKFDS
HLNPCYMVFD CLLLNDRPLA GLPLSERLKQ LRSAVRDVPE RMQIVHQQLV DSADQVIELL
NETVGRGEEG IMVKDPASLY KPNARTSSAG WFKIKPDYIN GLVDDLDVLI VGGYFGTGRR
SNLLSHFMIA LMENYDKKII ETVDDCNFST PRFVALGRVG SGYSLKELYD FNAKLVQLRL
KRGQPPPWLK LGVEKPEVYI HPEQSTIVQV KAAQIVTSGQ FPLGFTLRFP RVQAIRHDKT
WRDCMTVEQF LNFKDLSADC TSKRLAEMKN DNNGQIMNLK TISKKPKRKA IVAADRRCRV
EAMKNLDQSK RMRKFKPISN IFQGRELCIL NGNDTFTKEN LEGKVVELGG TVVQHPVAGR
QTVKVKSVVR ASTVDVLKLS WLIRCIQTNS FIQWTPKDML LTTATMKRHF KRNFDQYGDS
YTDPVDSETL HDLLTTVPVE KTDVDDSKSQ KFLSTISYKY GIFLNCTIYL DFYDDLLSPL
RRRIALSALD RYELLLYEFR ANIVDTLTDS LTHVIVHSDD LSRLDDLLRF KSDFNANFHI
VTESWVTHCI GEFAIVDESL HSVRTSGDSH PAIIDEEEVE EGDDVINENP SSSVIVSCSS
AEASQKQRDF HRKRLPPNEA LLKHLGQDSG HSNCLGTDGA TIKI
//
