MUS81_DANRE
ID MUS81_DANRE Reviewed; 604 AA.
AC Q7SXA9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Crossover junction endonuclease MUS81;
DE EC=3.1.22.-;
GN Name=mus81;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 295-604.
RX PubMed=18413719; DOI=10.1101/gad.1618708;
RA Chang J.H., Kim J.J., Choi J.M., Lee J.H., Cho Y.;
RT "Crystal structure of the Mus81-Eme1 complex.";
RL Genes Dev. 22:1093-1106(2008).
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; BC055679; AAH55679.1; -; mRNA.
DR RefSeq; NP_998683.1; NM_213518.1.
DR PDB; 2ZIU; X-ray; 2.70 A; A=295-604.
DR PDB; 2ZIV; X-ray; 2.70 A; A=295-604.
DR PDB; 2ZIW; X-ray; 2.80 A; A=295-604.
DR PDBsum; 2ZIU; -.
DR PDBsum; 2ZIV; -.
DR PDBsum; 2ZIW; -.
DR AlphaFoldDB; Q7SXA9; -.
DR SMR; Q7SXA9; -.
DR STRING; 7955.ENSDARP00000091555; -.
DR PaxDb; Q7SXA9; -.
DR GeneID; 406839; -.
DR KEGG; dre:406839; -.
DR CTD; 80198; -.
DR ZFIN; ZDB-GENE-040426-2923; mus81.
DR eggNOG; KOG2379; Eukaryota.
DR InParanoid; Q7SXA9; -.
DR OrthoDB; 738810at2759; -.
DR Reactome; R-DRE-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-DRE-6783310; Fanconi Anemia Pathway.
DR EvolutionaryTrace; Q7SXA9; -.
DR PRO; PR:Q7SXA9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0048856; P:anatomical structure development; IEA:UniProt.
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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..604
FT /note="Crossover junction endonuclease MUS81"
FT /id="PRO_0000223637"
FT DOMAIN 314..423
FT /note="ERCC4"
FT REGION 93..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:2ZIU"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2ZIW"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 376..387
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 388..396
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 457..473
FT /evidence="ECO:0007829|PDB:2ZIU"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:2ZIU"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2ZIV"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:2ZIV"
FT HELIX 509..519
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:2ZIU"
FT TURN 570..575
FT /evidence="ECO:0007829|PDB:2ZIU"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:2ZIU"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:2ZIU"
SQ SEQUENCE 604 AA; 68017 MW; 5AC33516404D3CE9 CRC64;
MPTDQVCLGR KRPLPSCPNP LFLQWLTELR DSAKEKGLKT HFVYQKAINS LKKYPLPLKN
GKEAKILQNF GDGICKILDE RLQKHYRENG SDAAVHLASS KQMEESQKEP SGNFSEHTKL
TQKEVRKEKG AKKKREYVPQ KRSGGYAVLL TLYRHMQMPG SKGFMFRNEL QTEAQPLCEK
SFTVPDLGSK YTAWSSVSTL IQKELVVKTH NPARYSLTDQ GLSLAEKLDS EETGTRHEDV
DSQDGQNVVD LTLEEEDEDE EKESWSSERP AVALPVNQAR GLMSESDPMG KSQTSETGRT
AMGWHLSPGS YDIVLCVDLC ETTGGSSVRK QELVKELQRN SVTFDVRKLN VGDFLWVARE
RVTPVPGQLR PPVGKELVLD YIIERKRMDD LCGSIIDGRF REQKFRLKRC GLRKPIYLVE
ECGSAAAHLS IPESTLQQAI VNTQVVDGFF VKRVQDAKES AAYLTIMTRY LQKLYQNCTL
LCRSRELEGD GEAESEKMVA NLSCSLMAFT EFNYGAIKNK CQTVREVFAR QLMQISGVSG
DKAAAVLKHY STVSSLLQAY DKCSSETEKE KLLSSVKYGK LKRNLGPALS RTIYQLYCTR
GPLS
