MUS81_EMENI
ID MUS81_EMENI Reviewed; 677 AA.
AC Q5B8L2; C8VIK2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Crossover junction endonuclease mus81;
DE EC=3.1.22.-;
GN Name=mus81; ORFNames=AN3118;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACD01000051; EAA63689.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83374.1; -; Genomic_DNA.
DR RefSeq; XP_660722.1; XM_655630.1.
DR AlphaFoldDB; Q5B8L2; -.
DR SMR; Q5B8L2; -.
DR STRING; 162425.CADANIAP00009958; -.
DR EnsemblFungi; CBF83374; CBF83374; ANIA_03118.
DR EnsemblFungi; EAA63689; EAA63689; AN3118.2.
DR GeneID; 2874172; -.
DR KEGG; ani:AN3118.2; -.
DR eggNOG; KOG2379; Eukaryota.
DR HOGENOM; CLU_014329_1_0_1; -.
DR InParanoid; Q5B8L2; -.
DR OMA; WIKEWLD; -.
DR OrthoDB; 738810at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; IPR018247; EF_Hand_1_Ca_BS.
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..677
FT /note="Crossover junction endonuclease mus81"
FT /id="PRO_0000223643"
FT DOMAIN 367..473
FT /note="ERCC4"
FT REGION 156..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 76241 MW; BBE3A6282428C18C CRC64;
MKYVNHKTIV AFLPEIGKAG SHVTSRPNLE ARVDRDSHGA TKLFLSSICR VMAAKETQAE
RGLISSCFNL ALGWQLSNAM SDDTCANPLL LGWIKEWLDQ ARERNTKGVT VYKKAYESMK
ACPLTFQHPS EAQQLNGLGP KLCERLTNKL KEYCKEHGLP MPEDPRTAKA DKRKSTDGDT
EGQPAKKARK PKPYAPALRS GPFALILALS SLDENSNQSM TKAELIEKAQ PYCDSSFTVP
SDPTKFFTAW NSMKILLTKE LVYTRGHPLK KYSLTEEGWE VAKAIKKTAQ KSIQNTLPFD
VQSDVTADEP RTAQREDLAS QRDFERQIRP GLQAHNSQRH TLDSLENTLD NSTITPIPIS
PDNFTVQLIL DTREVRTSKD RDYISNELIR KGITPEVRAL EVGDTMWVAK FHDPTFLRKY
GEEGDEIMLD WIVERKRLDD LIGSIKDGRF HEQKFRLRRS GIKNVIYLIE EFAVTHHESN
AAAAQKYHDM VASAIAQTQV VNGYFVKRTK NLDDTIRYLA RMTFLLRNMY SAPSPPSSRT
SARPSHTLAL LPTRHLALSS SHISALNTLR AENPHVTYGV TFPTFCAIAS KSDALTLRDI
FLKMLMCTKG VSGDKALEIQ RVWPTPQAFI RAFEELTDPK QKENMVADRM AHVMVGRKKI
AKVLSRKIAE VWGGLPG