ID S7PB68_MYOBR Unreviewed; 1327 AA.
AC S7PB68;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:EPQ07358.1};
GN ORFNames=D623_10032558 {ECO:0000313|EMBL:EPQ07358.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07358.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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; KE162186; EPQ07358.1; -; Genomic_DNA.
DR eggNOG; KOG0962; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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 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:UP000052978};
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..363
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 450..655
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..925
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1024..1070
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 1327 AA; 155329 MW; CE5C8F2105D0E88D CRC64;
MSRIEKMSIM GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELVAVQRSM VCTQKSKKTE FKTLEGVITR
TKHGEKVSLS SKCAEIDREM ISSLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
SATRYIKALE TLRQVRQTQG QKVKECQTEL KYLKQNKEKA CEIRDQITSK EAQLTSSKEI
VKSYENELDP LKNRLKEIEH NLSKIMKLDN EIKALESRKK QMEKDNSELE QKMEKVFQGT
DEQLNDLYLN HQRTIREKER KLVDCQRELE KLNKESRLLN QEKSELLVEQ GRLQQQADRH
QENIRARDSL IQSLASQLEL DGFEHGPFSE RQIKNFHKLV RERQEKEEET ASQLMNDFAE
KETLKQKQID EIRDKKIGLG RIIELKSEIL SKKQNELKNV KYELQQLEGS SDRIHELDQE
LTKAEHELSK AEKNSNVETL KTEVISLQNE KTDLDRTLRK LDQEMEQLNH HTATRTQMEM
LTKDKADKDE QIRKIKSRHS DELNSLLGYF PNKKQLEDWL HSKSREINQT RDRLAKLNKE
LASAEQNKNH INIELKRREE QLSSYEDKLF DVCGSQDFES DLGRLKEEIE KSSKQRAMLA
GATAVYSQFI TQLTDESQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLRSTESELK
KKEKRRDEML GLVPMRQSII DLKEKEIPEL RNKLQNVNRD IQRLKNDIEE QETLLGTIMP
EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGLD LDRTLQQVNQ EKQEKQHKLD
TVSSKIELNR KLIQDQQEQI QHLRGVTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS
LYREIKDAKE QISPLEITLE KFQQEKEELI FKKNTSHKIT QDKMNDIKEK VKNIHGYVKN
IENYIQDGKD DYKKQKETEL NKVIAQLSES EKHKEKINTD MGIMRQDIDT QKIQERWLQD
NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV LQLKNEHQNL EEKIENIKRS HSLAIGRQKG
YEEEIIHFKK ELRSPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
CSAGQKAVPG SPKQKSSDLP QVLASLIIRL ALAETFCLNC GILALDEPTT NLDRENIESL
AHSLVEIIKS RSQQRNFQLL VITHDEDFVE LLGRSEYVEK FYRIKKNIDQ CSEIVKCNIS
SLESYVH
//
