ID A0A0V1PND7_9BILA Unreviewed; 2452 AA.
AC A0A0V1PND7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=MAU2 chromatid cohesion factor homolog {ECO:0000256|ARBA:ARBA00017198};
DE AltName: Full=DNA ligase IV {ECO:0000256|ARBA:ARBA00031942};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4 {ECO:0000256|ARBA:ARBA00030676};
GN Name=LIG4 {ECO:0000313|EMBL:KRZ97689.1};
GN ORFNames=T08_5442 {ECO:0000313|EMBL:KRZ97689.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ97689.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ97689.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ97689.1};
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 -!- 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}.
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:KRZ97689.1}.
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DR EMBL; JYDM01000002; KRZ97689.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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: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: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; 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 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 recombination {ECO:0000256|ARBA:ARBA00023172};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRZ97689.1};
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:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1172..1435
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1846..1959
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 2143..2225
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 2284..2389
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT BINDING 1201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2452 AA; 280272 MW; 806C56C6D21E991F CRC64;
MLPFHDACYL GLLSMAEDFR TRSPPEIVNA LRCLLSIFEF SPPIVIEARL HFQVGHMYWS
FTENIDHARQ HLERAIALAR SHRAFEDVLS DAAYSLAQLY FKTNENALGR NLLYQTIETL
KNCQGMFCRQ IRLVFQLAQH LVNDRDYITA REVLQLGYQA AVNENCIYIR IMILLSISQL
YMFESRVKEL HQTLSKVSQL IDSWQGSSIR KAKSSKACLI ELQQLVQMIT HTGHQEQKDE
QQQYEYFQWI SDEHLCILVY AMTVMEALHC GKFNKARQYA ERALAHVEKL RRLNQDDNMA
QGLWLLLLEH SILSQLNTGH YVSAVKEISL LKSACHCNPR LFYQYGSRLH MLLGLYAVSM
DQAQAGEAQF AAALRFNRDP KLSFYLNLNL AVLYLQCGRE SEFYNLMDIS PERLAEQSVN
LRAASLFVRG MHLMLQRRYP EAKKVLCEAL ELTSKEDLNH LVSFCFVLIG QMLLGVNPRT
EHLKEALKLF TSSLHLAQSS ADVTAQVWSS GALKNLYAIC QNADQQKHYG QLEGDLVRGM
LQEQEHSRQL AEHQLINITD LMDQFIDRRA LTHCYRVLSL LHHFRVLLLK LLLNLCMAEI
SQASSHVDAF NVPRCVPDDK KSDETTESEL PPYRSVPKIT DEMETLAITE QILDTVICDK
LSVFCEESLH LHSCSRSSEP RSSDALQSYV TTLLSDHDKH VFVLSDAGKP VYTSEEELSS
LMGVIQALVS FVSSQNEGDE LQTIRAGVWT FVFSHRAPLI LCLVSRRSDS AEQLSRQLDL
VHRQILTVLT QVQLSRIFEE RKNFDLRRLL AGTERTLERL ILVMETDFSL LLNAVRCYTL
PHSTRETIVQ AMSSCCSQPK CIVFAVLLVH DQLVAYSGKK KATLSPSDLA LLINLVASNI
SFKDAESWSP ICLPAYDENT FLSAHISYLT ENSPACLLLL TAEKDSFFTM SEVRNKIIDK
FTRTKALAIL NELQQERKRF EINELGIPDL IHFIYKHRTK SQFTSMSLSL PYREEYFEKH
LFNRYLLIHN FMHSEKHKHN IFYVTGDLEN ILGWVTTAFE IYAVFNPLIT KPEAVSRVEQ
LMKWIKKEEN NLFLINPGHM SSKSTTVMNN VQSAVKVVDG RSDVVSALKK KSSASDTVEN
NGADDKQQFS FTYDANGVHL KPLTRMITED YRVSKTVLGV GLNGKVVECF KRKTGEKFAL
KVLCDTPKAR REVELHCLAR NHKNIVTIYD VYLNSFSNTK CLLIVMECME GGELFSRIQR
RGEHAFTERE AASIMYDICS AVRFLHSLQI AHRDIKPENL LYTKLTDDAV IKLTDFGFAK
RTEPSAVKSL ETPCYTPYYV APEILGTEKY DKSCDMWSLG VVMYILLCGF PPFYSSHGLP
MSPGMKSRIR SGQYVFPSPE WDNVSESAKD LIRGLLKTDP SARLRIDQVM NHSWITGCKA
VPETPLCTVS VLSEKKVIWN DVQEEMSNAL ASMRVDCDQM QIKNLSDSKN KLLEKRKKRL
FGLKLKMEQS CCSIESEIPF RDLCSILRAC ASTRNQAEKR RILGKFFHCW RERFKRKYEN
SVANSNSSVE SFFPILRLLV PKLDNARGPI GLKENMLAKK FIQIMAIDKN SPDAKALLGF
HLPATKWKMS STTTGKSDVD FAALISSMLK SRVLANVDEE ISLFDINRCL DHLASAHANR
SRDQVEKQID WCCRNLNAEQ FKWFVRIVLK DVRLWDSSSM DDDGYCCSVE LFKAYRPMLA
TLIFPGNRIC QIFSGSKFYV ETKFDGERVQ LHKDENNNYK YFSRNGIDFT SSYGSTPFVG
NLTQFIHGAF ENHVRNCILD GEMIAWDRTA KRFVGKGEHV DVKGLKFDSP LNPCYMVFDC
LLLNDRPLAG LPLSERLEQL RSAVRDIPER MQIVDQQLVD SADQVIELLN ETVGRGEEGI
MPDYINGLVD DLDVLIVGGY FGTGRRSNLL SHFMIALMEN YDKKIIETVD DCNFSTPRFV
ALGRVGSGYS LKELYDFNAK LVQLRLKRGQ PPPWLKLGVE KPEVYIHPEQ STIVQVKAAQ
IVTSGQFPLG FTLRFPRVQA IRHDKTWRDC MTVEQFLNFK DLSADCTSKR LAEMKNDNND
QIMNLKTISK KPKRKAIVAA DRRCRVEAMK NLDQSKRMRK FKPISNIFQG RELCILNGND
TFTKENLEGK VVELGGTVVQ HPVAGRQTVK VKSVVRASTV DVLKLSWLIR CIQTNSFIQW
TPKDMLLTTA TMKRHFKRNF DQYGDSYTDP VDSETLHDLL TTVPVEKTDV DDSKSQKFLS
TISYKYGIFL NCTIYLDFYD DLLSPLRRRI ALSALDRYEL LLYEFRANIV DTLTDSLTHV
IVHSDDLSRL DDLLRFKSDF NANFHIVTES WVTHCIGEFA IVDESLHSAR TSGESHPAII
DEEEGDDVID ENPSSSVIVS CIRNVASFFY SFTGNFSTNE EEEEEDDEEQ KL
//
