ID A0A0V0S7T0_9BILA Unreviewed; 2468 AA.
AC A0A0V0S7T0;
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:KRX22586.1};
GN ORFNames=T07_509 {ECO:0000313|EMBL:KRX22586.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22586.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22586.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22586.1};
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:KRX22586.1}.
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DR EMBL; JYDL01000030; KRX22586.1; -; Genomic_DNA.
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 1150..1410
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1821..1957
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 2141..2223
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 2282..2387
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT BINDING 1179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2468 AA; 281403 MW; 055A5EBDC2DCAC0B 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 LMDPLALLNL CMAEISQASS HVDAFSVPRC VPDDKKSDET
TESELPPYRS VPKITDEMET LAITEQILDT VICDKLSVFC EESLHLHSCS RSSEPRSSDA
LQSYVTTLLS DHDKHVFVLS DAGKPVYTRH GSEEELSSLM GVIQALVSFV SSQNEGDELQ
TIRAGVWTFV FSHRAPLILC LVSRRSDSAE QLSRQLDLVH RQILTVLTQV QLSRIFEERK
NFDLRRLLAG TERTLERLIL VMETDFSLLL NAVRCYTLPH STRETIVQAM SSCCSQPKCI
VFAVLLVHDQ LVAYSGKKKA TLSPSDLALL INLVASNISF KDAESWSPIC LPAYDENTFL
SAHISYLTEN SPACLLLLTA EKDSFFTMSE VRNKIIDKFT RTKALAILNE LQQERKRFEI
NELGIPDLIH FIYKHRTKSQ FTSMSLSLPY REEYFEKYLF NRYLLIHNFM HSEKHKHNIF
YVTGDLENIL GWVTIAFEIY AVFNPLITKP EAVSRVEQLM KWIKKEENNL FLINPGHMSS
KSTTVMNNVQ STVKVVDGRS DVVSALKKKS SASDTVENNG ADDKQQFSFT YDANGVHLKP
LTRMITEDYR VSKTVLGVGL NGKVVECFKR KTGEKFALKV LCDTPKARRE VELHCLARNH
KNIVTIYDVY LNSFSNTKCL LIVMECMEGG ELFSRIQRRG EHAFTEREAA SIMYDICSAV
RFLHSLQIAH RDIKPENLLY TKLTDDAVIK LTDFGFAKRT EPSAVKSLET PCYTPYYVAP
EILGTEKYDK SCDMWSLGVV ILCGFPPFYS SHGLPMSPGM KSRIRSGQYV FPSPEWDNVS
ESAKDLIRGL LKTDPSARLR IDQVMNHSWI TGCKAVPETP LCTVSVLSEK KVIWNDVQEE
MSNALASMRV DCDQMQIKNL SDSKNKLLEK RKKRLFGLKL KMEQSRCSIE SEIPFRDLCS
IFQACASTRN QAEKRRILGK FFHCWRERFK RKYENSLANS NSSVESFFPI LRLLVPKLDN
ARGPIGLKEN MLAKKFIQIM AIDKNSPDAK ALLGFHLPAT KWKMSSTTTG KSDVDFAALI
SSMLKSRVLA NVDEEISLFD INRCLDHLAS AHANRSRDQV EKQIDWCCRN LNSEQFKWFV
RIVLKDVRLW ESSSTDDDGY CCSVELFKAY RPMLATLIFP GNRICQIFSG SKFYVETKFD
GERVQLHKDE NNNYKYFSRN GIDFTSSYGS TPFVGNLTQF IHGAFENHVR NCILDGEMIA
WDRTAKRFVG KGEHVDVKGL KFDSHLNPCY MVFDCLLLND RPLAGLPLSE RLKQLRSAVR
DVPERMQIVH QQLVDSADQV IELLNETVGR GEEGIMVKDP ASLYKPNART SSAGWFKIKP
DYINGLVDDL DVLIVGGYFG TGRRSNLLSH FMIALMENYD KKIIETVDDC NFSTPRFVAL
GRVGSGYSLK ELYDFNAKLV QLRLKRGQPP PWLKLGVEKP EVYIHPEQST IVQVKAAQIV
TSGQFPLGFT LRFPRVQAIR HDKTWRDCMT VEQFLNFKDL SADCTSKRLA EMKNDNNGQI
MNLKTISKKP KRKAIVAADR RCRVEAMKNL DQSKRMRKFK PISNIFQGRE LCILNGNDTF
TKENLEGKVV ELGGTVVQHP VAGRQTVKVK SVVRASTVDV LKLSWLIRCI QTNSFIQWTP
KDMLLTTATM KRHFKRNFDQ YGDSYTDPVD SETLHDLLTT VPVEKTDVDD SKSQKFLSTI
SYKYGIFLNC TIYLDFYDDL LSPLRRRIAL SALDRYELLL YEFRANIVDT LTDSLTHVIV
HSDDLSRLDD LLRFKSDFNA NFHIVTESWV THCIGEFAIV DESLHSVRTS GDSHPAIIDE
EEVEEGDDVI NENPSSSVIV SCSSAEASQK QRDFHRKRLP PNEALLKHLG QDSGHSNCLG
TDGATIKI
//
