ID G9KJY1_MUSPF Unreviewed; 1311 AA.
AC G9KJY1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=RAD50-like protein {ECO:0000313|EMBL:AES05210.1};
DE Flags: Fragment;
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|EMBL:AES05210.1};
RN [1] {ECO:0000313|EMBL:AES05210.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES05210.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(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}.
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; JP016612; AES05210.1; -; mRNA.
DR HOGENOM; CLU_006184_0_0_1; -.
DR OMA; FSDYYYR; -.
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: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 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 2: Evidence at transcript level;
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 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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES05210.1"
FT NON_TER 1311
FT /evidence="ECO:0000313|EMBL:AES05210.1"
SQ SEQUENCE 1311 AA; 153847 MW; 9D2211301A5AC1E9 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 V
//