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Database: UniProt
Entry: A0A0V0XMD6_TRIPS
LinkDB: A0A0V0XMD6_TRIPS
Original site: A0A0V0XMD6_TRIPS 
ID   A0A0V0XMD6_TRIPS        Unreviewed;      2171 AA.
AC   A0A0V0XMD6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=MAU2 chromatid cohesion factor homolog {ECO:0000256|ARBA:ARBA00017198};
GN   Name=LIG4 {ECO:0000313|EMBL:KRX89089.1};
GN   ORFNames=T4E_3124 {ECO:0000313|EMBL:KRX89089.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX89089.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX89089.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX89089.1};
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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572}.
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:KRX89089.1}.
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DR   EMBL; JYDU01000210; KRX89089.1; -; Genomic_DNA.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:InterPro.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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; IPR036420; BRCT_dom_sf.
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   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 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; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 4.
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; 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   Kinase {ECO:0000313|EMBL:KRX89089.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
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:UP000054815};
KW   Transferase {ECO:0000313|EMBL:KRX89089.1}.
FT   DOMAIN          1171..1434
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1849..1973
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   BINDING         1200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2171 AA;  247706 MW;  4DCB7EF5F82391C9 CRC64;
     MLPFQDAYYL GLLSMAEDFR TRSPPEIVNA LRCLLSIFEF SPPIGIEARL HFQVGHMYWS
     FTENIDHARQ HLERAITLAR SHHAFEDVLS DAAYSLAQLY FKTNESALGR NLLYQTIETL
     KNCQGMFCWQ IKLVFQLAQH LVNDRDYITA REVLQLGYQA AVNENCIYIR IMILLSISQL
     YMFESRVKEL HQTLSKVSQL IDSWQGSSIR RAHLRAWFFV IQICYFMSEG KAKSSKACLI
     ELQQLVQMIT HTVHQEQKDE QQQYEYFQWI SDEHLCILVY AMTVMQALHC GKFNKARQYA
     ERALAHVEKL RRLNEEDNVA QSLWLLLLEH SILSQLNTGH YVSAVKEISL LKSACHCSPR
     LFYQYGSRLH MLLGLYAVSM DQAQAAEAQF AAALRFNRDP KLSFYLNLNL AVLYLQCGRE
     SEFYNLMDIN PERLAEQSIN LRAASLFVRG MHLMLQRRYS EAKKVLCDAL EVTSKEDLNH
     LVSFCFVLIG QMLLGVNPRP EHLQEALKLF TSSLHLAQNN ADATAQLWSS GALKNLYAIC
     QNADQQKHYG QLEGDLVRAM LQEQEHSRQL AEHQLINITD LMDPLALLNL CMAEISQASS
     HVDAFSMPHS VPTDKKNSGT TESELPSYRS VPKITDEMES LAITEQILDT VICDKLVTSV
     FCEESLHLHS CSKSSESRSS DALQSYVTTL LSDHDKHVFV LSDAGKPVYT RHGSEEELSS
     LMGVIQALVS FVSSQNEGDE LRTIRAGVWT FVFSHRAPLI LCLVSRRSDS AEQLSRQLDL
     VHRQILTVLT QVQLSRIFEE RKNFDLRRLL AGTERTLERL ILVMETDFSL LLNAVRCYTL
     PHSTRETIVQ VMSSCCSQPK CIVFAVLLVH DQLVAYSGKK KATLSPSDLA LLINLVASNI
     SFKDAESWSP ICLPAYDEST FLSAHISYLT ENSPACLLLL TAEKDSFFTM SEKFTRTKAL
     AILNELQQER KRFEINELGI PDLIHFIYKH RTKSQFTSMS LSLPYRDEYF EKHLFNRYLL
     IHNFMHSEKH KHNIFYVTGD LENILGWVTT AFEVYAVFSP LITKPEAVSR VEQLMKWIKK
     EENNLFLINP VFFFKNMSSK SSTTVMNNGQ STVKAVDGRS DVVSALKKKS SASNTVDNAG
     GADDKQQFSF TYDANGVHLK PLTRMITEDY RVSKTVLGVG LNGKVVECFK RKTGEKFALK
     VLCDTPKARR EVELHCLARN HKNIVTIYDV YLNSFSNTKC LLIVMECMEG GELFSRIQRR
     GEHAFTEREA ASIMYDICSA VRFLHSLQIA HRDIKPENLL YTKVSDDAVI KLTDFGFAKR
     TEPSAVKSLE TPCYTPYYVA PEILGTEKYD KSCDMWSLGV VMYILLCGFP PFYSSHGLPM
     SPGMKSRIRS GQYVFPSPEW DNVSDSAKDL IRGLLKTDPS DRLRIDQVMT HSWITGCQAV
     PETPLCTVSV LSEKKVIWND VQEEMSNALA SMRVDCDQMQ IKNLSDSKNK LLEKRKKRLF
     GLKLKMEQSC SSIESEIPFV DLCSIFQACA STRNQAEKRR ILGKFFHCWR ERFKSKYQNC
     VASKNNNNNS NSLEESFFPV LRLLVPKLDN ARGPIGLKEN MLAKKFIQIM AIDKNSPDAK
     ALLGFHLPAT KSRMSSTTGR LDGDFAALIS SMLKCRVLAN ADRQISLLDI NRCLDQLASA
     HANRSRDQVE RQIDWCCRNL NSEQFKWFVR IVLKDVRLKP LESSSAGGCC SIELFKAYRP
     MLAALIFPDQ IICQIVAGCK FYVETKFDGE RVQLHKDDNN NYKYFSRNGI DFTSSYGSTP
     FVGNLTQFIH RAFENHVHNC ILDGEMIAWD RTARRFVGKG EHVDVKTLKL DSHLNPCYMV
     FDCLFLNDCP LASMPLSERL QKLRSSVRDV PERLQIVHQQ LTDSAYPDYI NGLIDDLDVL
     IVGGYFGTGR RSNLLSHFMI ALMENYDKEK VETVDDCSSS TPWFVALGRV GSGYSLKELY
     DFNAKLVQLR LKRGQPPSWL KLGSEKPEVY IHPEQSTIVQ VKAAQIVTSG QFPLGFTLRF
     PRVQAIRHDK TWRDCMTVEQ FLNFKDLSVD CTSKRLAEMK NDNQIMNLKN ISKKRKRKAT
     VAADRRCRVE AMKNLDQSKR MREFKAISNI FQGRELCILN GNDTFTKENL EAKVVELGGT
     VVQHPGKFYF T
//
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