RAD50_ENCCU
ID RAD50_ENCCU Reviewed; 1247 AA.
AC Q8SRK6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DNA repair protein RAD50;
DE EC=3.6.-.-;
GN Name=RAD50; OrderedLocusNames=ECU07_0610i;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). The
CC RAD50/MRE11 complex possesses single-strand endonuclease activity and
CC ATP-dependent double-strand-specific exonuclease activity. RAD50
CC provides ATP-dependent control of MRE11 by unwinding and/or
CC repositioning DNA ends into the MRE11 active site (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Forms a complex with MRE11. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- DOMAIN: The zinc-hook, which separates the large intramolecular coiled
CC coil regions, contains 2 Cys residues that coordinate one molecule of
CC zinc with the help of the 2 Cys residues of the zinc-hook of another
CC RAD50 molecule, thereby forming a V-shaped homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
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DR EMBL; AL590447; CAD25593.1; -; Genomic_DNA.
DR RefSeq; NP_585989.1; NM_001041611.1.
DR AlphaFoldDB; Q8SRK6; -.
DR SMR; Q8SRK6; -.
DR STRING; 284813.Q8SRK6; -.
DR PRIDE; Q8SRK6; -.
DR GeneID; 859418; -.
DR KEGG; ecu:ECU07_0610i; -.
DR VEuPathDB; MicrosporidiaDB:ECU07_0610i; -.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; Q8SRK6; -.
DR OMA; CFGVNCG; -.
DR OrthoDB; 179362at2759; -.
DR Proteomes; UP000000819; Chromosome VII.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd03240; ABC_Rad50; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; DNA damage; DNA repair; Hydrolase; Meiosis;
KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..1247
FT /note="DNA repair protein RAD50"
FT /id="PRO_0000381756"
FT DOMAIN 617..716
FT /note="Zinc-hook"
FT COILED 299..415
FT /evidence="ECO:0000255"
FT COILED 459..545
FT /evidence="ECO:0000255"
FT COILED 787..942
FT /evidence="ECO:0000255"
FT COILED 972..1020
FT /evidence="ECO:0000255"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1247 AA; 144547 MW; A0EE39AB2787C2F6 CRC64;
MASIKKLMIR GVRSFSHKES NTLEFYSPLT LIVGANGTGK TTIIESLKYA TTGSLPPNSR
GGAFIHDPSV AGLAEVQGQV KLLFTNVHGE TMICSRTIQL AQRRDRREQK TLESVIWAER
DGEGVSGRSG DVDAEMPQHF GVSGSILESI IFCHQEESTW PLGEPVVVKK KLDDIFASAK
YGKALDSLKS SRKECSSDVK MKMQELEFLR KMKERKESLE LRIRSGCMSI EKNEIRVEAC
DNEIGRCERV IEEIDLELKG NEEAEKRAHL LRGEHRELME FIDGFREKKL PLEDATDIMS
GKSLQEAEEE YERMKMDAEE SEMRFKDLSE ERSRYIRSKA ELDGVFSEIS VKSSFLDEAR
RQKMEALKSL ESELKVKKDF RETALEVFGK VEDDIKQRKE CIHRLEEEAL RLKKEDRDRT
VALSEKKRIV DEYSGLESDG SIDVSVSYED EVGRLRAEIS RDREMEALEE RLGDYQRRLN
DAYSIAERNF AMNQMRGRKR EIEGMLNGVN VSELKSKLER QKAKLREKES RAKEIEREMS
LRKARAIERS KENDRIRREL RTKSMELGSM GQRSRMAIFE ELGIPMLRNG SRCSVERAKE
VVRSNEGFFA RDDMGFGVEM LDLESLYDGE EVLQRSGASD GIWRERIYRE MLEDGCRSHE
CPVCNKPLSK EEEVEFKRKL EAGIERALDG KENALGSWND RERIAGEIEA LNKEIAGRNK
IREEMAELIL RYEEVEDVSG EEALDEMELD MLDEAEGIKK TEFLIGLVEE LFLIDGKLRG
SEEGESVQEL RSMVDGIRKI YEEKKEEVRR KKERIEYLCR KQEVIRAERE IREKINFREE
AKEAMQRIER SSARIRASDV EEEIRRKKSK LDRILERFAR KRVELEMSME AFYQKEREEA
CLAKEIEELN SKVRKLLQAE FLDEAKDEVK FDDARSDLLE RKNKVLEIGQ KIRRMYEMRS
LAEESMKYYN RERRVREIER ELSETDFEYL AALKEKRRLL EEKKAKLSSQ KSLLLGECKQ
IALGVKSYKQ ELLKDHGRTV ENYNKCFIEV KALELSCMDL DKCIQALDKA IVDFHTSKLE
EVNATLKDLW TNTYRGDDVD WIKIKTESSG QRTYNYKVVF VKGGVELDMR GRSSAGQKMI
ASILIRLALA DSFASSCSVL ALDEPTTNLD RDNIESLAFT LSRVISRHRR DADFQLIVIT
HDEDFVQLLS RGGPEYFYRL SRSESGDSMI VRHSIYGTRE MGPNKVY
