UniProt: E2A7J8

Database: UniProt
Entry: E2A7J8_CAMFO

LinkDB:  E2A7J8_CAMFO 
Original site:  E2A7J8_CAMFO

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Ontology (7)   
   GO (7)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (4)   
   Pfam (3)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   E2A7J8_CAMFO            Unreviewed;      1368 AA.
AC   E2A7J8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:EFN70591.1};
GN   ORFNames=EAG_03182 {ECO:0000313|EMBL:EFN70591.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN70591.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
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DR   EMBL; GL437344; EFN70591.1; -; Genomic_DNA.
DR   RefSeq; XP_011252910.1; XM_011254608.1.
DR   RefSeq; XP_011252911.1; XM_011254609.2.
DR   STRING; 104421.E2A7J8; -.
DR   EnsemblMetazoa; XM_011254608.2; XP_011252910.1; LOC105249281.
DR   EnsemblMetazoa; XM_011254609.3; XP_011252911.1; LOC105249281.
DR   GeneID; 105249281; -.
DR   KEGG; cfo:105249281; -.
DR   InParanoid; E2A7J8; -.
DR   OMA; FSDYYYR; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
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   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS51131; ZN_HOOK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000000311};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          639..738
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   REGION          1320..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          189..275
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          389..427
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          466..500
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          530..604
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          716..771
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          799..879
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          904..945
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          979..1104
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1320..1334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1347..1368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         684
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         687
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   1368 AA;  159261 MW;  589487171BDF4A42 CRC64;
     MSKIRKLSLR GIRNFGDDNE DSLIRFSCPL TLILGPNGTG KTTIIEALKY ATTGEFPPGS
     EKGKFFIHDP SLATTGSVRG VVKAEIIDSM GNTYTVSRTI ESLKAVKKFK TLDSTVTRVS
     KDKKEKASIT NRCADVDAEL SVALGVSKSI LNYVIFCHQE ELNWPFDQGK TLKERFDEIF
     DSTKFNKALE TILKLHKDLQ GDIKSLNAEK QTFKVLVSEV ENKETKLEEH KKRLDITKEK
     INDIDKQLVP LKQKIEEVQQ SHSEYKNIQA EEEKKKMEYG VYKERYQKLK ETINNIFHGT
     TEELNALIES HDTILQEKNN EIAENEIEIK GISEKEARIS NILATRRETV GTFKQQVKDH
     EKRVVRRNEL LNEALQAWNF DTVEQDVTEI EVKALTKRLE QKIRTLEQEI EENRMAMEKK
     EKQSQKEVDI LCSNYLKIES EKTLKEKEIT EIRDEITTIR NQIAQIGAAG NKLKSIEQKL
     QAAKQKIDEL SNALDVDSVK TDIANKIKSR DKIEANLSAI DDEISSLHKL SSLKTEFDLK
     KSTLQAKEEE LENLKRKHGN SIKTLLNTQE LQQTKLKITL DRVHQQLEKE TTSLTQEIQA
     QERKTTAFQT TLQYIESDIG KKKTELHRDK ERISTVCDYK EFDETLLMQS KIVKDLQDKR
     GIYAYQATAY KEYIKKLSVK DPCCPLCHRN FQEQNKVTDL IKEMETDIIR NQPNRLKKCE
     EELKIQQEKY DNMLQLKPIV QKIIQCEETD LKKLEERLEK TKNSVKLSKI AIKDLEVSKA
     EPEKKLLLYK DMIGDIKFWD RCIDEIQQLK KTVNNLQTQM ANAGVKTEKT LEELQVQRES
     LKTSFKETRN HIEALQLKLN KHNERLHEAR ETYNELHEQQ LKIHSDMQKL KHLKDKQEDL
     YVKEVTIGET VEKLQENLAN AENQLDSGKQ QLEKIKLENR QKQDADRKLM MENTRRLTDL
     HKIIDEVDSF ISSNVPKKLA SYELEIETYQ KSLMELINKK KNVEQAINKL KEDVASQEIG
     KRELHDNITL RKTKDTIEAL KEQYKKLNEK LKNMNYSELT KKWEQLESEK QALLRQKNVA
     LGNQEELERV IKQYMQELRK EEYRLARRNY TNKCIELTVQ EDTIANLKAY SKILDTAMIE
     YHEERMSTVN RIMKKLWKHV YKGTDTSSIE ICTEPTKDVG SNRRSYTYKL IQTKHGCKMD
     MKGRCSAGQK VLASIIIRLA LAETFCKDCG ILALDEPTTN LDEENANSLA DTLTKVVELR
     SRYQKNFQLI IISHDEKFLQ KLADLNNHKQ FHELYRKQNG MTAVKISDFN EPASSLVQIK
     SEDESDEEER HPNRASTSGL STNKKRYNWD DFNEHDRPPA KKRYYFAE
//

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