ID M7ZVW1_TRIUA Unreviewed; 609 AA.
AC M7ZVW1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Crossover junction endonuclease MUS81 {ECO:0000256|RuleBase:RU369042};
DE EC=3.1.22.- {ECO:0000256|RuleBase:RU369042};
GN ORFNames=TRIUR3_18043 {ECO:0000313|EMBL:EMS64232.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS64232.1};
RN [1] {ECO:0000313|EMBL:EMS64232.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
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}.
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DR EMBL; KD058376; EMS64232.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ZVW1; -.
DR STRING; 4572.M7ZVW1; -.
DR eggNOG; KOG2379; Eukaryota.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; 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 CDD; cd06222; RNase_H_like; 1.
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; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033309; Mus81.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR044730; RNase_H-like_dom_plant.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
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; PF02732; ERCC4; 1.
DR Pfam; PF13456; RVT_3; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
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 Magnesium {ECO:0000256|RuleBase:RU369042};
KW Metal-binding {ECO:0000256|RuleBase:RU369042};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU369042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369042}.
FT DOMAIN 166..264
FT /note="ERCC4"
FT /evidence="ECO:0000259|SMART:SM00891"
SQ SEQUENCE 609 AA; 68480 MW; 93DC1A166A07AD56 CRC64;
MAFISSMRWT MFADITNLLE LLLAYKVYAE IDSGHCHFYM GRGVGGWFVD VMEDSFPGSS
LDLSPPTRKK NTRNKPYVPR LKSAAYAIMI TLYSPNNSRN SRNEGYSYTG WNSMKTLTNK
DLVLKEVDFQ TQKQAVPVPL GSAEKSLLAM PPHQSNESFL KVYDVVLILD DRDTFGPRSR
RKVVDNIRSH FNIPVEIKHL PVGDALWIAR HKELDTEYVL DFIVERKNVD DLLGSIKDNR
YKDQKLRLKK CGLTKLIYLV EGDVNTVDGS ESVKTACFTT EVLEGFDVQR TTGYADTEKK
YGHLTGSIID YYSRNFSAGA DTSRLCLTYD EFVKRCSDLE KVTMGDIFAL QLMQVPQVTE
EAALAVTSLY PTLLSLAKAY TLLVHVLQEQ HVEQILFCED CGVEFCEDCG VEETIERRCF
LPNRMLLPLC VGAGRFGLKE TIGDMKNFKW AIDTIHDLAA LVGLKTAREL REKSVWIPPE
ITYNKVNVDP SYYEQDGYGS TGVVIWDHIE ALVQSTSNFG INFAQNASTM EALALGDGIR
LALGHLKVII ESDAQDVRML NEAKFSRADL VSLSISNKKA NAYARSSFQS CSIVHINREA
NEAAHICAK
//
