EME1_PONAB
ID EME1_PONAB Reviewed; 575 AA.
AC Q5NVA9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Crossover junction endonuclease EME1;
DE EC=3.1.22.-;
GN Name=EME1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interacts with MUS81 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: May self-associate. Interacts with MUS81. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to regions of
CC DNA damage in S-phase cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR EMBL; CR926475; CAI30268.1; -; Transcribed_RNA.
DR RefSeq; XP_009249893.1; XM_009251618.1.
DR AlphaFoldDB; Q5NVA9; -.
DR SMR; Q5NVA9; -.
DR STRING; 9601.ENSPPYP00000009309; -.
DR GeneID; 100458738; -.
DR KEGG; pon:100458738; -.
DR CTD; 146956; -.
DR eggNOG; ENOG502R8ER; Eukaryota.
DR HOGENOM; CLU_034099_2_0_1; -.
DR InParanoid; Q5NVA9; -.
DR OMA; FCVESDW; -.
DR OrthoDB; 1595761at2759; -.
DR TreeFam; TF325310; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.670; -; 1.
DR Gene3D; 3.40.1620.30; -; 1.
DR Gene3D; 4.10.800.30; -; 1.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR043086; EME1_nucdom_sub1.
DR InterPro; IPR043087; Eme1_nucdom_sub2.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033310; Mms4/EME1/EME2.
DR PANTHER; PTHR21077; PTHR21077; 1.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..575
FT /note="Crossover junction endonuclease EME1"
FT /id="PRO_0000223632"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96AY2"
SQ SEQUENCE 575 AA; 63795 MW; EF26A7E82444DF86 CRC64;
MALKKSSPSL DSGDSDSEEL PTFAFLKKEP SSTKRRQPER EEKIVVVDIS DCEASCPPAP
GLLSPPVPDI AETVTQTQPV RLLSSGSEDE EEFIPLAQRL KCKFLTHKQL SPEDSSSPIK
SVLDHQNNEG ASCDWKKQPF PKIPEVPLHD TLERSAADNK DLILDPCRQL PACLSTCPGQ
SSSLAVTKTN SDILPPQKKT KRSQKVQGRG SHGCRQQRQA RQKESTLRRQ ERKNAALVAR
MKAQRPEECL KHIIVVLDPV LLQMEGGGQL LGALQSMECR CVIEAQAVPC SVTWRRRAGP
SEVLWQDGED WVEEPTVLVL LRAEAFVSMI DNGKQGSLDS TMKGKETLQG FVTDITARTA
GKALSLVIVD QEKCFSAQNP PRRGKQGANK QTKEKQQRQP EASIGSMVSR VDAEEALVDL
QLHTEAQAQI VQSWKELADF TCAFTKAVAE VPFKKLRDET TFSFCVESDW AGGVKVDRAG
RGLALVWRRQ IQQLNRVSLE MASAVVNAYP SPQLLVQAYR QCFSEQERQN LLADIQVRRG
EGVTSTSRRV GPELSRRIYL QMTTLQPHLS LDSAD
