MUS81_KLULA
ID MUS81_KLULA Reviewed; 614 AA.
AC Q6CPQ8;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Crossover junction endonuclease MUS81;
DE EC=3.1.22.-;
GN Name=MUS81; OrderedLocusNames=KLLA0E02948g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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) (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with EME1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
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DR EMBL; CR382125; CAG99168.1; -; Genomic_DNA.
DR RefSeq; XP_454081.1; XM_454081.1.
DR AlphaFoldDB; Q6CPQ8; -.
DR SMR; Q6CPQ8; -.
DR STRING; 28985.XP_454081.1; -.
DR EnsemblFungi; CAG99168; CAG99168; KLLA0_E03015g.
DR GeneID; 2893880; -.
DR KEGG; kla:KLLA0_E03015g; -.
DR eggNOG; KOG2379; Eukaryota.
DR HOGENOM; CLU_014329_1_0_1; -.
DR InParanoid; Q6CPQ8; -.
DR OMA; WIKEWLD; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:EnsemblFungi.
DR GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:EnsemblFungi.
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:0006265; P:DNA topological change; IEA:EnsemblFungi.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR GO; GO:0051097; P:negative regulation of helicase activity; IEA:EnsemblFungi.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Magnesium; Meiosis; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..614
FT /note="Crossover junction endonuclease MUS81"
FT /id="PRO_0000223645"
FT DOMAIN 333..430
FT /note="ERCC4"
FT REGION 80..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 70413 MW; A77B5B8FD8273F3C CRC64;
MSIPSDAKQL YAEFLQQEVN QSTSAHQEKL VMVLNRALFA LKNYPDPIYH PKDLLKVKGI
GQTTMNKLSK RLKTYCEENG YSFPEESSST DNTQSTQNDS NPSNTQKTRV RTLEPEENES
QGTRKRRKKK YIPRNRSGGY GILLGLLELG CDKDGTACTR RQLIAVASKY CDQSYEKNPS
TKEFYSAWSA IKSLKTNDLV IEQGRPSQFS LTEAGTILAD SLKTANNIEF DVSSVYERRL
NRGNTQNSFT NDEHDHTVNF SGLMNHANMS INESANSSRL FLDATANSSR IEQNEEPEVS
AEISTPIPKQ KVSKGRWKGV KYELWKPDSY DIILHIDHRE VRSKEDRGFF ARKLLQRGIE
TESSSLTVGD MIWLAKHKQS GQQCALDFIV ERKRLDDLVI SIRDNRFSEQ KNRLQKTGCK
HIFYLVEETT GYNVSDSADM MKTSIWTTVI YNDFHIKRTR NADTTVQWLT DMSLIIKELY
SRKSLVVINH DHITNQSIYL TSLKMFRTEF ERNKEIECCH NYESMQSAMV KTNLMTVKEL
YLRALMSVKG ISLEKALMIQ SRYPTFKTLL KAYRRCAAEA DAKTLIQNEL KDAPGNRKIG
KSLSHTLWET FGKL
