(data stored in SCRATCH zone)

SWISSPROT: C4KJH9_SULIK

ID   C4KJH9_SULIK            Unreviewed;       864 AA.
AC   C4KJH9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000256|HAMAP-Rule:MF_00449};
GN   Name=rad50 {ECO:0000256|HAMAP-Rule:MF_00449};
GN   OrderedLocusNames=M164_0063 {ECO:0000313|EMBL:ACR40699.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40699.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40699.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in
CC       the early steps of DNA double-strand break (DSB) repair. The
CC       complex may facilitate opening of the processed DNA ends to aid in
CC       the recruitment of HerA and NurA. Rad50 controls the balance
CC       between DNA end bridging and DNA resection via ATP-dependent
CC       structural rearrangements of the Rad50/Mre11 complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00449}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00449};
CC       Note=Binds 1 zinc ion per homodimer. {ECO:0000256|HAMAP-
CC       Rule:MF_00449};
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11
CC       subunits and two Rad50 subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00449}.
CC   -!- DOMAIN: The two conserved Cys that bind zinc constitute the zinc-
CC       hook, which separates the large intramolecular coiled coil
CC       regions. The 2 Cys residues coordinate one molecule of zinc with
CC       the help of the 2 Cys residues of the zinc-hook of another Rad50
CC       molecule, thereby forming a V-shaped homodimer.
CC       {ECO:0000256|HAMAP-Rule:MF_00449}.
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00449}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00449}.
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DR   EMBL; CP001402; ACR40699.1; -; Genomic_DNA.
DR   RefSeq; WP_012735359.1; NC_012726.1.
DR   EnsemblBacteria; ACR40699; ACR40699; M164_0063.
DR   KEGG; sid:M164_0063; -.
DR   HOGENOM; HOG000107872; -.
DR   KO; K03546; -.
DR   OMA; HTACICG; -.
DR   OrthoDB; POG093Z01RC; -.
DR   BioCyc; SISL426118:GI01-63-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00449; RAD50; 1.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022982; Rad50_ATPase_archaeal.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   Pfam; PF13304; AAA_21; 1.
DR   Pfam; PF04423; Rad50_zn_hook; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   PROSITE; PS51131; ZN_HOOK; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJH9.
DR   SWISS-2DPAGE; C4KJH9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00449};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_00449};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00449};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00449};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00449};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW   ProRule:PRU00471};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00449};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00449, ECO:0000256|PROSITE-
KW   ProRule:PRU00471}.
FT   DOMAIN      380    478       Zinc-hook. {ECO:0000259|PROSITE:PS51131}.
FT   NP_BIND      32     38       ATP. {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      164    240       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      244    281       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      298    325       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      363    400       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      442    531       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      539    602       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      606    633       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   COILED      637    699       {ECO:0000256|HAMAP-Rule:MF_00449}.
FT   METAL       426    426       Zinc. {ECO:0000256|HAMAP-Rule:MF_00449,
FT                                ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   METAL       429    429       Zinc. {ECO:0000256|HAMAP-Rule:MF_00449,
FT                                ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   BINDING     131    131       ATP. {ECO:0000256|HAMAP-Rule:MF_00449}.
SQ   SEQUENCE   864 AA;  101559 MW;  5F4F841A317BD6C9 CRC64;
     MRIDKITLTN FLSHEHSEIH FLGEINVIVG QNGAGKSSII DGIVFSLFRT HSRGNNDNLI
     RKGSNKASVT LHLSNEKDKI EIIRDIRSTT EDRLIRNQIP VARSATVVSN EIEKILGIDK
     DIALSTIIVR QGELDKILEN LQDIMGKILK LESIEKLIDS RGPIVEFKKN LENKLRELDK
     IEQDYNDSKK NLEEKRNRVL ELEKDRKKLE DEIKNLENQI TELKKQFEDY EKKRNQYLEL
     TTILKVKETK LNELNKSIEE LRRQTENMDK LEKEVNELDN LKNFRLKFEK YEVLSRSYIE
     ISNNILNLEK EIEEYEKAIK RKKELEPHYL RYKELERKLE ELQPKHEEYL KSKSNLDSKL
     NLKERLEKDA SEFSKDIDRI SNLEQIMEEK RKRQLDLRAQ LGKVESLISE KNEIINNLSQ
     VKGETCPVCG RPLDEEHKQK IVEEAKSYIS RLELDKNELE EELKKTTDEL NKIEKEYRKL
     SNNKANYDNV IKQLRKLNEE IENLHNRIEA LKDIEEEIKK INVEIKDLKQ YYEEFMRLFK
     YDEKELERKK NRLDEMNKKK VEIEKEMRAL ETELQGLDRK ELENKISDLE RKKKILDEMK
     KKRGVLEDYI GQVELLQEDV KKLREKLNII QFDENKYNEL KTSLDVHNAS LKEKENRKSR
     VEGELDSLGK DIEEISNRIK NYELQLKDKE KIINGINKLE KIRDALGERK LQSYIIMATK
     QLIENNLNDI ISKFDLSIKN VEMEIMPKTS RGKGSGGNIV IYTNNGDTLP IVSLSGGERI
     ALSIALRLAI AKALMSNTNF FILDEPTIHL DDQRKAYLIE IIRAAKESVP QILVVTHDEE
     VVQAADYVIR VEKRGNKSFV REET
//

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