ID   MUS81_XENTR             Reviewed;         612 AA.
AC   Q640B4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Crossover junction endonuclease MUS81;
DE            EC=3.1.22.-;
GN   Name=mus81;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interacts with eme1 and eme2 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, replication forks and nicked Holliday junctions. May be
CC       required in mitosis for the processing of stalled or collapsed
CC       replication forks (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Binds eme1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
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DR   EMBL; BC082716; AAH82716.1; -; mRNA.
DR   RefSeq; NP_001011004.1; NM_001011004.1.
DR   AlphaFoldDB; Q640B4; -.
DR   SMR; Q640B4; -.
DR   PaxDb; Q640B4; -.
DR   DNASU; 496413; -.
DR   Ensembl; ENSXETT00000063029; ENSXETP00000061734; ENSXETG00000020588.
DR   GeneID; 496413; -.
DR   KEGG; xtr:496413; -.
DR   CTD; 80198; -.
DR   Xenbase; XB-GENE-5904230; mus81.
DR   eggNOG; KOG2379; Eukaryota.
DR   InParanoid; Q640B4; -.
DR   OrthoDB; 738810at2759; -.
DR   PhylomeDB; Q640B4; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000020588; Expressed in skeletal muscle tissue and 13 other tissues.
DR   ExpressionAtlas; Q640B4; differential.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048257; F:3'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IEA:InterPro.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.110; -; 1.
DR   Gene3D; 1.10.150.670; -; 1.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR042530; EME1/EME2_C.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR033309; Mus81.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR13451; PTHR13451; 1.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SUPFAM; SSF47802; SSF47802; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..612
FT                   /note="Crossover junction endonuclease MUS81"
FT                   /id="PRO_0000223638"
FT   DOMAIN          325..434
FT                   /note="ERCC4"
FT   REGION          89..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  69118 MW;  EA965A3EED931E7E CRC64;
     MPGEITYGRK RPLPACPNPL FLKWLTEWRD SAAEKNLKTQ FVYQKAISSL KKYPLPLNSG
     KEAKILQNFG DSICKMLDDR LEKHYAECGP NIPIHTVPSS SSTLRKAQRQ PKAPSPLSIP
     HALEPPEQES QDLSPSKKKK TGGKKQREYV PQRRSGGYAV LLTLYRDTKS PSSRGYMTKA
     ELQKEAQPLC DKSFTLTDPN SKYTAWTSVS TLIQKELVIK THSPARYSLT EKGLELAQRL
     EEAEDQGRAD GFPRQVQASS NEEEEQEEAE SETNPYIHAD PVQCPDQQLN LAYSHNAKNT
     SSDPPSVQYN HVPEFTLHPG DFNILLCVDF IETTGGAAHR KQELVTELRR NGVNFDVRKL
     HIGDFLWIAQ EKVQPVPGQL RIPQARELVL DYVVERKRMD DLCGSIIDGR FREQKFRLKR
     CGLRRPIYLV EDHGSAQHLS IPETTLQQAI VNTQVVDGFF IKRTKDVRES AAYLTIMTRY
     LQGIYSRKSL LSCTKEEEWK CDRSLRPDAS SCILVEFKDF NEGAMKNKAQ TVKEVFARQL
     MQISGVSGEK AAAILEKYST PASLMSAYES CSSAEEKEKL LSSVKCGKLQ RNLGPVLSKT
     ISQLYCTKEP LS