ID M3YGI1_MUSPF Unreviewed; 1312 AA.
AC M3YGI1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=DNA repair protein RAD50 isoform X1 {ECO:0000313|RefSeq:XP_004745067.1, ECO:0000313|RefSeq:XP_004745069.1};
DE SubName: Full=RAD50 double strand break repair protein {ECO:0000313|Ensembl:ENSMPUP00000010438.1};
GN Name=RAD50 {ECO:0000313|Ensembl:ENSMPUP00000010438.1,
GN ECO:0000313|RefSeq:XP_004745067.1, ECO:0000313|RefSeq:XP_004745069.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010438.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010438.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004745067.1, ECO:0000313|RefSeq:XP_004745069.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004745067.1,
RC ECO:0000313|RefSeq:XP_004745069.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR EMBL; AEYP01016939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01016940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01016941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01016942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01016943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01016944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01016945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004745067.1; XM_004745010.3.
DR RefSeq; XP_004745069.1; XM_004745012.3.
DR STRING; 9669.ENSMPUP00000010438; -.
DR Ensembl; ENSMPUT00000010606.1; ENSMPUP00000010438.1; ENSMPUG00000010515.1.
DR GeneID; 101688333; -.
DR KEGG; mpuf:101688333; -.
DR CTD; 10111; -.
DR eggNOG; KOG0962; Eukaryota.
DR GeneTree; ENSGT00390000018781; -.
DR HOGENOM; CLU_006184_0_0_1; -.
DR OMA; FSDYYYR; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0070533; C:BRCA1-C complex; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0006310; P:DNA recombination; IEA:Ensembl.
DR GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1904354; P:negative regulation of telomere capping; IEA:Ensembl.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IEA:Ensembl.
DR GO; GO:0000019; P:regulation of mitotic recombination; IEA:Ensembl.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0031860; P:telomeric 3' overhang formation; IEA:Ensembl.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; TIGR00606; rad50; 1.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 635..734
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 241..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 450..662
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..1077
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1312 AA; 153984 MW; EF2D2211301A5AC1 CRC64;
MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
TKGHTFVHDP KVAQETDVRA QIRLQFRDVN GEVIAVQRSM VCTQKSKKTE FKTLEGVITR
TKHGEKVSLS SKCAEIDREM ISSLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
SATRYIKALE TLRQVRQTQG QKVKECQAEL KYLKQNKEKA CEIRDQITSK EAQLTSSKEI
VKSYENELDP LKNRLKEIEQ NLSKIMRLDN EIKALDSRKK QMEKDNSELE KKMEKVFQGT
DEQLNDLYHN HQRTVREKER RLVDCQRELE KLNKESRLLN QEKSELLVEQ GRLQLQADRH
QEHIQARDSL IQSLATQLEL DGFERGPFNE RHIKNFHKLV RERQEREAEI ASQLMNDFAE
KETLKQKQID EIRDKKTGLG RIIELKSEIL TKKQNELRNV KHELQQLEGS SDRILELDQE
LSKAERELSK AEKNNNVEAL KTEVINLQNE KADLDRTLRK LDQEMEQLNY HTTTRTQMEM
LTRDKADKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
LASSEQNKNH VNNELKKKEE RLSSYEDKLF DVCGSQDFES DLERLKEEIE KSSKQRAMLA
GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK
KKEKRRDEML GLVPMRQSII DLKEKEIPEL RNKLQNVNRD IQRLKNDIEE QDTLLGTIMP
EEESAKVCLT DVTIMERLQM ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD
TVSSKMELNR KLIQDQQEQI QHLKSTTNEL KSEKLHISTN LQRRQQLEEQ TVELSTEVQS
LFREIKDAKE QLSPLETTME KFQQEKEEII NKKNKSNKIA QDKMNDIKEK VKNIHGYMKD
IENYIQDGKD DYKKQKENEL NKVVAQLNEY EKHKENINKD MGIMRQDIDT QKIQERWLQD
NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV LQMKNEHQKL EEKIDNIKRN HDLAVGRQKG
YEEEIIHFKR ELREPQYRDA EEKYREMLIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM
EEINKIIRDL WRNTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
NFQLLVITHD EDFVELLGRS EYVDKFYRIK KNIDQCSEIV KCSVSSLGSY VH
//
