Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA repair protein RAD50

Gene

RAD50

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA double-strand break repair (DSBR). The RAD50/MRE11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. RAD50 provides ATP-dependent control of MRE11 by unwinding and/or repositioning DNA ends into the MRE11 active site (By similarity).By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per homodimer.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi661ZincBy similarity1
Metal bindingi664ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 41ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Meiosis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD50 (EC:3.6.-.-)
Gene namesi
Name:RAD50
Ordered Locus Names:ECU07_0610i
OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Taxonomic identifieri284813 [NCBI]
Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
Proteomesi
  • UP000000819 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU07_0610i.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003817561 – 1247DNA repair protein RAD50Add BLAST1247

Expressioni

Developmental stagei

Expressed in late sporogonial stages.1 Publication

Interactioni

Subunit structurei

Homodimer. Forms a complex with MRE11.By similarity

Protein-protein interaction databases

STRINGi284813.NP_585989.1.

Structurei

3D structure databases

ProteinModelPortaliQ8SRK6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini617 – 716Zinc-hookAdd BLAST100

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili299 – 415Sequence analysisAdd BLAST117
Coiled coili459 – 545Sequence analysisAdd BLAST87
Coiled coili787 – 942Sequence analysisAdd BLAST156
Coiled coili972 – 1020Sequence analysisAdd BLAST49

Domaini

The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. RAD50 subfamily.Curated
Contains 1 zinc-hook domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0962. Eukaryota.
COG0419. LUCA.
HOGENOMiHOG000149364.
InParanoidiQ8SRK6.
KOiK10866.
OMAiVLLCHQE.
OrthoDBiEOG092C0FLY.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
SUPFAMiSSF52540. SSF52540. 5 hits.

Sequencei

Sequence statusi: Complete.

Q8SRK6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIKKLMIR GVRSFSHKES NTLEFYSPLT LIVGANGTGK TTIIESLKYA
60 70 80 90 100
TTGSLPPNSR GGAFIHDPSV AGLAEVQGQV KLLFTNVHGE TMICSRTIQL
110 120 130 140 150
AQRRDRREQK TLESVIWAER DGEGVSGRSG DVDAEMPQHF GVSGSILESI
160 170 180 190 200
IFCHQEESTW PLGEPVVVKK KLDDIFASAK YGKALDSLKS SRKECSSDVK
210 220 230 240 250
MKMQELEFLR KMKERKESLE LRIRSGCMSI EKNEIRVEAC DNEIGRCERV
260 270 280 290 300
IEEIDLELKG NEEAEKRAHL LRGEHRELME FIDGFREKKL PLEDATDIMS
310 320 330 340 350
GKSLQEAEEE YERMKMDAEE SEMRFKDLSE ERSRYIRSKA ELDGVFSEIS
360 370 380 390 400
VKSSFLDEAR RQKMEALKSL ESELKVKKDF RETALEVFGK VEDDIKQRKE
410 420 430 440 450
CIHRLEEEAL RLKKEDRDRT VALSEKKRIV DEYSGLESDG SIDVSVSYED
460 470 480 490 500
EVGRLRAEIS RDREMEALEE RLGDYQRRLN DAYSIAERNF AMNQMRGRKR
510 520 530 540 550
EIEGMLNGVN VSELKSKLER QKAKLREKES RAKEIEREMS LRKARAIERS
560 570 580 590 600
KENDRIRREL RTKSMELGSM GQRSRMAIFE ELGIPMLRNG SRCSVERAKE
610 620 630 640 650
VVRSNEGFFA RDDMGFGVEM LDLESLYDGE EVLQRSGASD GIWRERIYRE
660 670 680 690 700
MLEDGCRSHE CPVCNKPLSK EEEVEFKRKL EAGIERALDG KENALGSWND
710 720 730 740 750
RERIAGEIEA LNKEIAGRNK IREEMAELIL RYEEVEDVSG EEALDEMELD
760 770 780 790 800
MLDEAEGIKK TEFLIGLVEE LFLIDGKLRG SEEGESVQEL RSMVDGIRKI
810 820 830 840 850
YEEKKEEVRR KKERIEYLCR KQEVIRAERE IREKINFREE AKEAMQRIER
860 870 880 890 900
SSARIRASDV EEEIRRKKSK LDRILERFAR KRVELEMSME AFYQKEREEA
910 920 930 940 950
CLAKEIEELN SKVRKLLQAE FLDEAKDEVK FDDARSDLLE RKNKVLEIGQ
960 970 980 990 1000
KIRRMYEMRS LAEESMKYYN RERRVREIER ELSETDFEYL AALKEKRRLL
1010 1020 1030 1040 1050
EEKKAKLSSQ KSLLLGECKQ IALGVKSYKQ ELLKDHGRTV ENYNKCFIEV
1060 1070 1080 1090 1100
KALELSCMDL DKCIQALDKA IVDFHTSKLE EVNATLKDLW TNTYRGDDVD
1110 1120 1130 1140 1150
WIKIKTESSG QRTYNYKVVF VKGGVELDMR GRSSAGQKMI ASILIRLALA
1160 1170 1180 1190 1200
DSFASSCSVL ALDEPTTNLD RDNIESLAFT LSRVISRHRR DADFQLIVIT
1210 1220 1230 1240
HDEDFVQLLS RGGPEYFYRL SRSESGDSMI VRHSIYGTRE MGPNKVY
Length:1,247
Mass (Da):144,547
Last modified:June 1, 2002 - v1
Checksum:iA0EE39AB2787C2F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590447 Genomic DNA. Translation: CAD25593.1.
RefSeqiNP_585989.1. NM_001041611.1.

Genome annotation databases

EnsemblFungiiCAD25593; CAD25593; CAD25593.
GeneIDi859418.
KEGGiecu:ECU07_0610i.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590447 Genomic DNA. Translation: CAD25593.1.
RefSeqiNP_585989.1. NM_001041611.1.

3D structure databases

ProteinModelPortaliQ8SRK6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284813.NP_585989.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAD25593; CAD25593; CAD25593.
GeneIDi859418.
KEGGiecu:ECU07_0610i.

Organism-specific databases

EuPathDBiMicrosporidiaDB:ECU07_0610i.

Phylogenomic databases

eggNOGiKOG0962. Eukaryota.
COG0419. LUCA.
HOGENOMiHOG000149364.
InParanoidiQ8SRK6.
KOiK10866.
OMAiVLLCHQE.
OrthoDBiEOG092C0FLY.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
SUPFAMiSSF52540. SSF52540. 5 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRAD50_ENCCU
AccessioniPrimary (citable) accession number: Q8SRK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.