ID A0A0V1DE21_TRIBR Unreviewed; 1020 AA.
AC A0A0V1DE21;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Crossover junction endonuclease MUS81 {ECO:0000256|ARBA:ARBA00017114, ECO:0000256|RuleBase:RU369042};
DE EC=3.1.22.- {ECO:0000256|RuleBase:RU369042};
GN Name=ULK3 {ECO:0000313|EMBL:KRY59840.1};
GN ORFNames=T03_12080 {ECO:0000313|EMBL:KRY59840.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59840.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59840.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59840.1};
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: Interacts with EME1 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, D-loops, replication forks and nicked Holliday junctions.
CC May be required in mitosis for the processing of stalled or collapsed
CC replication fork intermediates. May be required in meiosis for the
CC repair of meiosis-specific double strand breaks subsequent to single-
CC end invasion (SEI). {ECO:0000256|RuleBase:RU369042}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU369042};
CC -!- SUBUNIT: Interacts with EME1. {ECO:0000256|RuleBase:RU369042}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369042}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000256|ARBA:ARBA00010015,
CC ECO:0000256|RuleBase:RU369042}.
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:KRY59840.1}.
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DR EMBL; JYDI01000009; KRY59840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DE21; -.
DR STRING; 45882.A0A0V1DE21; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008821; F:crossover junction DNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21036; WH_MUS81; 1.
DR CDD; cd20074; XPF_nuclease_Mus81; 1.
DR Gene3D; 3.40.50.10130; -; 1.
DR Gene3D; 1.10.150.670; Crossover junction endonuclease EME1, DNA-binding domain; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR033309; Mus81.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR047417; WH_MUS81.
DR InterPro; IPR047416; XPF_nuclease_Mus81.
DR PANTHER; PTHR13451; CLASS II CROSSOVER JUNCTION ENDONUCLEASE MUS81; 1.
DR PANTHER; PTHR13451:SF0; CROSSOVER JUNCTION ENDONUCLEASE MUS81; 1.
DR Pfam; PF21292; EME1-MUS81_C; 1.
DR Pfam; PF02732; ERCC4; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF21136; MUS81-like_WH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00891; ERCC4; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 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}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU369042};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU369042};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU369042};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW ECO:0000256|RuleBase:RU369042};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU369042};
KW Kinase {ECO:0000313|EMBL:KRY59840.1};
KW Magnesium {ECO:0000256|RuleBase:RU369042};
KW Metal-binding {ECO:0000256|RuleBase:RU369042};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU369042};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369042};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000313|EMBL:KRY59840.1}.
FT DOMAIN 645..911
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 143..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1020 AA; 115850 MW; C32D6AD8DFDCE31C CRC64;
MNDREVSLSM QSIQVTCRRQ FPLNMLIEHW LGLMVTEAEK KDSKSAFSYR RALTSVRKFP
AQLHSVDEAK LLLQYFGDKM CMVLKKKLDE FCAEHGEPTL TNVAGYVGKS VGDKLLHSNA
NRAVSVVKKR CSCAESVEKC FKQPTTSSSS PSLSSSTKSR RKSSSFIPKN RSGAYAILRA
LYDALNLDNL EWVGTAELQR RAQAYCDQYI GPSTRNQHYT AWMGRKTLIA HGLVESRRSR
GNDYRLTECG KRLAAQLDQM TNVVDCATDS IAMQNHLASQ KADPGLEPRS TDWHCCTVCG
TRHVLLAADG YDVLMLVDNS ETKGGPTGRA GPRSQLQSSK AKMKAALLRA GIDFEERELS
VGDYLWLARS KTDSRDEFVL DVIVERKRVD DLANSVLEKE GRYREQKFRL KRCGLKNVVY
LVEDFDGMDS MAEYKKLLVR GACAKTQLID QFHFVRTHNL EETVVYLKTM TEYLRQSYAG
KSIWLKIESS TTCDTQSTLN DASCCAQQLT VLQRFAEFDL NNRKQKQWTV SEVFARMLLQ
FHGISAERAQ QIVNKYPTVA HLLNAYATAE RDIDGNEPTG EIPLLAEIRS GMLGRNLGEK
LAKKIQFFFT STEPFQIKMG PLIGWSPRFW RNHIMETVKP QPKGYVLSEC LGSGSFGTVY
KARSSTTQTG GESSRGNYVA VKCILRRQIV RYKESEDNLI AEISLLKKLK HPHIVELVDF
SWDLNFIYLI LEYCADKDLE ELLKKQGHFS ESETKQLIRQ LASALQYLRS KSIGHFDLKP
QNILVACKKP NPVLKLGDFG FARSFSVEDK AVGLRGSLLY MAPEMLLRRQ FDPKADLWSV
GVILYRCLYG RTPFIGNMQS IRRQLQAVRG SVPLPTTLSL SVDCRDLMIR LLRVDPKQRI
EFDHFFSHPF VDMQHYPSAA CLARADSYAK MAIAADEAGR VHQAFLLYRE ALEYYMPCLL
CSENVCWNRD DLRDKMCQYL NRAEALKRSL ANRDPKTPLT RSTNQVDIAR LFSVCTVESR
//
