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Conserved domains on  [gi|1582023753|gb|TAY06473|]
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Ku protein [Rhizobium ruizarguesonis]

Protein Classification

Ku protein( domain architecture ID 11441558)

Ku protein, together with LigD, forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity; binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA; recruits and stimulates the ligase activity of LigD

CATH:  4.10.970.10
Gene Ontology:  GO:0045027|GO:0006303|GO:0006310
PubMed:  11483577|10377944
SCOP:  4000586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YkoV COG1273
Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and ...
6-279 7.45e-118

Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and repair];


:

Pssm-ID: 440884 [Multi-domain]  Cd Length: 279  Bit Score: 339.79  E-value: 7.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYTAAStSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:COG1273     3 RAIWKGAISFGLVNIPVKLYSATE-SHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKGRYVVLEDEELE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:COG1273    82 ALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIARVVLRGRERLAALRPRGDGLVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEkAFEEMP-KLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSK 244
Cdd:COG1273   162 ETLRYPDEVRDAD-EFPDLPeDVKVDPKELDMAKQLIESLTGDFDPEKYKDEYREALLELIEAKIEGKEVVAPPEEEPEG 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1582023753 245 PN--DLLAALRESAGMMKPAADKSKRTAANANTGTGR 279
Cdd:COG1273   241 ANviDLMEALKASLEAAKKKRAAAKAKKAPAKKAARK 277
 
Name Accession Description Interval E-value
YkoV COG1273
Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and ...
6-279 7.45e-118

Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and repair];


Pssm-ID: 440884 [Multi-domain]  Cd Length: 279  Bit Score: 339.79  E-value: 7.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYTAAStSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:COG1273     3 RAIWKGAISFGLVNIPVKLYSATE-SHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKGRYVVLEDEELE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:COG1273    82 ALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIARVVLRGRERLAALRPRGDGLVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEkAFEEMP-KLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSK 244
Cdd:COG1273   162 ETLRYPDEVRDAD-EFPDLPeDVKVDPKELDMAKQLIESLTGDFDPEKYKDEYREALLELIEAKIEGKEVVAPPEEEPEG 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1582023753 245 PN--DLLAALRESAGMMKPAADKSKRTAANANTGTGR 279
Cdd:COG1273   241 ANviDLMEALKASLEAAKKKRAAAKAKKAPAKKAARK 277
KU_like cd00789
Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA ...
6-260 1.34e-112

Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA binding protein Ku. The alignment includes the core domain shared by the prokaryotic YkoV-like proteins and the eukaryotic Ku70 and Ku80. The prokaryotic Ku homologs are predicted to form homodimers. It is proposed that the Ku homologs are functionally associated with ATP-dependent DNA ligase and the eukaryotic-type primase, probably as components of a double-strand break repair system.


Pssm-ID: 238408 [Multi-domain]  Cd Length: 256  Bit Score: 325.65  E-value: 1.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYTAaSTSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:cd00789     1 RAIWKGAISFGLVNIPVKLYSA-TESEDISFHQLHKKDGARIRYQRVCPETGKEVPRDDIVKGYEYEKGEYVILTDEELE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:cd00789    80 ALPPESTRTIEIVDFVPLDEIDPIYFDKPYYLAPDKGGEKAYALLREALRDTGKVAIAKVVLRTRERLAALRPRGKGLVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEKAFEEMPKLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSKP 245
Cdd:cd00789   160 NTLRYPDEVRSPEELFLPIKAVKVDPKELEMAKQLIEQLTGDFDPEKYEDEYREALMELIEAKIEGKAIEAAEPAPAASG 239
                         250
                  ....*....|....*..
gi 1582023753 246 N--DLLAALRESAGMMK 260
Cdd:cd00789   240 NvvDLMEALKKSLEAAK 256
Ku_bact TIGR02772
Ku protein, prokaryotic; Members of this protein family are Ku proteins of non-homologous end ...
6-257 4.37e-97

Ku protein, prokaryotic; Members of this protein family are Ku proteins of non-homologous end joining (NHEJ) DNA repair in bacteria and in at least one member of the archaea (Archaeoglobus fulgidus). Most members are encoded by a gene adjacent to the gene for the DNA ligase that completes the repair. The NHEJ system is broadly but rather sparsely distributed, being present in about one fifth of the first 250 completed prokarytotic genomes. A few species (e.g. Archaeoglobus fulgidus and Bradyrhizobium japonicum) have multiple copies that appear to represent recent paralogous family expansion. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274290  Cd Length: 258  Bit Score: 286.48  E-value: 4.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYtAASTSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:TIGR02772   2 RAIWKGAISFGLVNCPVKLY-PATESEDISFHQLHREDGNRVRYQKVCSETGKEVEREEIVKGYEYDKGKYVIIEDEDIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:TIGR02772  81 SLPPESTKTIEIEAFVDADEIDPIYFDTPYYLAPDKGGEKAYALLREALEDTGKVGIAKVVLRGRERLAALRPVGKGLVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEKAFEEMPKLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSKP 245
Cdd:TIGR02772 161 TTLRYPDEVRSPDEFFGPIKDVEVDPEELELAGQLIDKMTGKFDPEDYHDEYREALLELVDAKLEGGKPPKAEEPAAPAP 240
                         250
                  ....*....|....*
gi 1582023753 246 N---DLLAALRESAG 257
Cdd:TIGR02772 241 GnvvDLMDALKASLR 255
Ku pfam02735
Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
15-196 6.52e-45

Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. This is the central DNA-binding beta-barrel domain. This domain is found in both the Ku70 and Ku80 proteins that form a DNA binding heterodimer.


Pssm-ID: 460669  Cd Length: 197  Bit Score: 151.24  E-value: 6.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  15 FGEVSCGVALYTAASTSERITFNTINKAT--GNRVNRIFIDSETEDPVPKEAQTKGFEIeNGQYIIIDPEEISAAIPESN 92
Cdd:pfam02735   2 GGLVSIPVKLYSATEEEKKPSFKKLDRETndGVRIKYKYVCEDTGKEVEKEDIVKGYEY-GGTYVPLSDEELEELKPEST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  93 KTLEIEAFIPCSDVDDVYF--DKPYYLTPD----RMGGDAFAALRDAMKKSMVAAIARTVLFRR--MRTVLIRPHGK--- 161
Cdd:pfam02735  81 KGLDLLGFVPLDEIDPIYFmgDKSYFLYPDkgdiAGSTKAFSALREALLETDKVAIARFVLRRRehPRLVALRPQEEepd 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1582023753 162 -GLIASTLNYDYEVRSSEKAF-EEMPKLKIQGEMLDL 196
Cdd:pfam02735 161 pGLVLITLPFADDVREEFFPIpSLLEKPKPTEEQLDL 197
Ku78 smart00559
Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single ...
66-176 1.07e-15

Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single stranded DNA- and ATP-depedent helicase that has a role in chromosome translocation. This is a domain of unknown function C-terminal to its von Willebrand factor A domain, that also occurs in bacterial hypothetical proteins.


Pssm-ID: 128831 [Multi-domain]  Cd Length: 140  Bit Score: 72.33  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   66 TKGFEIeNGQYIIIDPEEISAAIPESNKTLEIEAFIPCSDVDDVYFDKP-YYLTPD----RMGGDAFAALRDAMKKSMVA 140
Cdd:smart00559  10 VKGYEY-GGRYVPLSDEELEQLKYKSEPGLELLGFKPLSSLPPYYFLRPsYFLVPDdksvIGSTKAFSALVEALLETDKI 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1582023753  141 AIARTVLFRRM--RTVLIRPH-----GKGLIASTLNYDYEVRS 176
Cdd:smart00559  89 AIARYTLRTKSnpRLVALRPYdeeddGEGLVLVQLPFADDVRK 131
 
Name Accession Description Interval E-value
YkoV COG1273
Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and ...
6-279 7.45e-118

Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and repair];


Pssm-ID: 440884 [Multi-domain]  Cd Length: 279  Bit Score: 339.79  E-value: 7.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYTAAStSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:COG1273     3 RAIWKGAISFGLVNIPVKLYSATE-SHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKGRYVVLEDEELE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:COG1273    82 ALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIARVVLRGRERLAALRPRGDGLVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEkAFEEMP-KLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSK 244
Cdd:COG1273   162 ETLRYPDEVRDAD-EFPDLPeDVKVDPKELDMAKQLIESLTGDFDPEKYKDEYREALLELIEAKIEGKEVVAPPEEEPEG 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1582023753 245 PN--DLLAALRESAGMMKPAADKSKRTAANANTGTGR 279
Cdd:COG1273   241 ANviDLMEALKASLEAAKKKRAAAKAKKAPAKKAARK 277
KU_like cd00789
Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA ...
6-260 1.34e-112

Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA binding protein Ku. The alignment includes the core domain shared by the prokaryotic YkoV-like proteins and the eukaryotic Ku70 and Ku80. The prokaryotic Ku homologs are predicted to form homodimers. It is proposed that the Ku homologs are functionally associated with ATP-dependent DNA ligase and the eukaryotic-type primase, probably as components of a double-strand break repair system.


Pssm-ID: 238408 [Multi-domain]  Cd Length: 256  Bit Score: 325.65  E-value: 1.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYTAaSTSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:cd00789     1 RAIWKGAISFGLVNIPVKLYSA-TESEDISFHQLHKKDGARIRYQRVCPETGKEVPRDDIVKGYEYEKGEYVILTDEELE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:cd00789    80 ALPPESTRTIEIVDFVPLDEIDPIYFDKPYYLAPDKGGEKAYALLREALRDTGKVAIAKVVLRTRERLAALRPRGKGLVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEKAFEEMPKLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSKP 245
Cdd:cd00789   160 NTLRYPDEVRSPEELFLPIKAVKVDPKELEMAKQLIEQLTGDFDPEKYEDEYREALMELIEAKIEGKAIEAAEPAPAASG 239
                         250
                  ....*....|....*..
gi 1582023753 246 N--DLLAALRESAGMMK 260
Cdd:cd00789   240 NvvDLMEALKKSLEAAK 256
Ku_bact TIGR02772
Ku protein, prokaryotic; Members of this protein family are Ku proteins of non-homologous end ...
6-257 4.37e-97

Ku protein, prokaryotic; Members of this protein family are Ku proteins of non-homologous end joining (NHEJ) DNA repair in bacteria and in at least one member of the archaea (Archaeoglobus fulgidus). Most members are encoded by a gene adjacent to the gene for the DNA ligase that completes the repair. The NHEJ system is broadly but rather sparsely distributed, being present in about one fifth of the first 250 completed prokarytotic genomes. A few species (e.g. Archaeoglobus fulgidus and Bradyrhizobium japonicum) have multiple copies that appear to represent recent paralogous family expansion. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274290  Cd Length: 258  Bit Score: 286.48  E-value: 4.37e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFGEVSCGVALYtAASTSERITFNTINKATGNRVNRIFIDSETEDPVPKEAQTKGFEIENGQYIIIDPEEIS 85
Cdd:TIGR02772   2 RAIWKGAISFGLVNCPVKLY-PATESEDISFHQLHREDGNRVRYQKVCSETGKEVEREEIVKGYEYDKGKYVIIEDEDIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  86 AAIPESNKTLEIEAFIPCSDVDDVYFDKPYYLTPDRMGGDAFAALRDAMKKSMVAAIARTVLFRRMRTVLIRPHGKGLIA 165
Cdd:TIGR02772  81 SLPPESTKTIEIEAFVDADEIDPIYFDTPYYLAPDKGGEKAYALLREALEDTGKVGIAKVVLRGRERLAALRPVGKGLVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 166 STLNYDYEVRSSEKAFEEMPKLKIQGEMLDLAKHIISTKKGEFDPATFDDRYEAALADLVKAKLEGKSLPKPKKVEVSKP 245
Cdd:TIGR02772 161 TTLRYPDEVRSPDEFFGPIKDVEVDPEELELAGQLIDKMTGKFDPEDYHDEYREALLELVDAKLEGGKPPKAEEPAAPAP 240
                         250
                  ....*....|....*
gi 1582023753 246 N---DLLAALRESAG 257
Cdd:TIGR02772 241 GnvvDLMDALKASLR 255
KU cd00594
Ku-core domain; includes the central DNA-binding beta-barrels, polypeptide rings, and the ...
6-256 5.12e-60

Ku-core domain; includes the central DNA-binding beta-barrels, polypeptide rings, and the C-terminal arm of Ku proteins. The Ku protein consists of two tightly associated homologous subunits, Ku70 and Ku80, and was originally identified as an autoantigen recognized by the sera of patients with an autoimmunity disease. In eukaryotes, the Ku heterodimer contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by non-homologous end-joining. The bacterial Ku homologs does not contain the conserved N-terminal extension that is present in the eukaryotic Ku protein.


Pssm-ID: 238334 [Multi-domain]  Cd Length: 272  Bit Score: 192.49  E-value: 5.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFG-EVSCGVALYTAASTSERITFNTINKATGNRVNRIFIDSETED-PVPKEAQTKGFEIEnGQYIIIDPEE 83
Cdd:cd00594     1 RAIWKGALSLGlDVSIPVKLYSAATEEKPPSFKQLDRKTGERVKVKRVCKYTGGkEVEKEDIVKGYEYG-GDYVPLTEEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  84 ISAAIPESNKTLEIEAFIPCSDVDDVYFDK-PYYLTPDR---MGGDAFAALRDAMKKSMVAAIARTVLFR--RMRTVLIR 157
Cdd:cd00594    80 LEQLKLETSKGLDILGFVPASEIPPYYFDKeSYYLVPDDsdkGSEKAFSALRRALLEKDKVAIARYVLRRnsRPRLVALR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753 158 PHGK----GLIASTLNYDYEVRSSEKA-FEEMPKLKIQGEMLDLAKHIISTKKG-EFDPATFDDRYEAALADLVKAKLEG 231
Cdd:cd00594   160 PQEEedpeGLVLVTLPFADDVRSYPFPlLLDIKTEKPTDEELELAKQLIDSLDLdDFDPEKFPNPYLQRLYALLEAKALG 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1582023753 232 KSLPKPKKVEVSKP--------NDLLAALRESA 256
Cdd:cd00594   240 EEIPEPPEDLTLPPpeeipkrvIDLLEALKKSL 272
Ku pfam02735
Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
15-196 6.52e-45

Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. This is the central DNA-binding beta-barrel domain. This domain is found in both the Ku70 and Ku80 proteins that form a DNA binding heterodimer.


Pssm-ID: 460669  Cd Length: 197  Bit Score: 151.24  E-value: 6.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  15 FGEVSCGVALYTAASTSERITFNTINKAT--GNRVNRIFIDSETEDPVPKEAQTKGFEIeNGQYIIIDPEEISAAIPESN 92
Cdd:pfam02735   2 GGLVSIPVKLYSATEEEKKPSFKKLDRETndGVRIKYKYVCEDTGKEVEKEDIVKGYEY-GGTYVPLSDEELEELKPEST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  93 KTLEIEAFIPCSDVDDVYF--DKPYYLTPD----RMGGDAFAALRDAMKKSMVAAIARTVLFRR--MRTVLIRPHGK--- 161
Cdd:pfam02735  81 KGLDLLGFVPLDEIDPIYFmgDKSYFLYPDkgdiAGSTKAFSALREALLETDKVAIARFVLRRRehPRLVALRPQEEepd 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1582023753 162 -GLIASTLNYDYEVRSSEKAF-EEMPKLKIQGEMLDL 196
Cdd:pfam02735 161 pGLVLITLPFADDVREEFFPIpSLLEKPKPTEEQLDL 197
Ku78 smart00559
Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single ...
66-176 1.07e-15

Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single stranded DNA- and ATP-depedent helicase that has a role in chromosome translocation. This is a domain of unknown function C-terminal to its von Willebrand factor A domain, that also occurs in bacterial hypothetical proteins.


Pssm-ID: 128831 [Multi-domain]  Cd Length: 140  Bit Score: 72.33  E-value: 1.07e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   66 TKGFEIeNGQYIIIDPEEISAAIPESNKTLEIEAFIPCSDVDDVYFDKP-YYLTPD----RMGGDAFAALRDAMKKSMVA 140
Cdd:smart00559  10 VKGYEY-GGRYVPLSDEELEQLKYKSEPGLELLGFKPLSSLPPYYFLRPsYFLVPDdksvIGSTKAFSALVEALLETDKI 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1582023753  141 AIARTVLFRRM--RTVLIRPH-----GKGLIASTLNYDYEVRS 176
Cdd:smart00559  89 AIARYTLRTKSnpRLVALRPYdeeddGEGLVLVQLPFADDVRK 131
KU80 cd00873
Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in ...
6-146 1.68e-08

Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination. The mechanism underlying the regulation of all the diverse functions of Ku is still unclear, although it seems that Ku is a multifunctional protein that works in nuclei. In mammalian cells, the Ku heterodimer recruits the catalytic subunit of DNA-dependent protein kinase (DNA-PK), which is dependent on its association with the Ku70/80 heterodimer bound to DNA for its protein kinase activity.


Pssm-ID: 238445 [Multi-domain]  Cd Length: 300  Bit Score: 54.60  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753   6 RAQWKGFLKFG-EVSCGVALYTA--------------ASTSERITFNTINKATGNRVNRifiDSETEdpVPKEAQTKGFE 70
Cdd:cd00873     1 VAAFKGQLTLGsPLSIAVELYKKtkeerppklkkvsdAEKTGEDAFEDVKSERSYDVND---DDKTE--VEKEDLIKGYR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  71 iENGQYIIIDPEEISAAIPESNKTLEIEAFIPCSDVDDVYF-DKPYYLTPDRM---GGDAFAALRDAMKKSMVAAIARTV 146
Cdd:cd00873    76 -YGRDIVPLSEEDEEATKLSTSKGLDILGFIKASNVPRYYLmGESSYVVPQQDdeaAALAFSALVRALAELDKYAIARYV 154
KU70 cd00788
Ku-core domain, Ku70 subfamily; Ku70 is a subunit of the Ku protein, which plays a key role in ...
14-213 1.29e-07

Ku-core domain, Ku70 subfamily; Ku70 is a subunit of the Ku protein, which plays a key role in multiple nuclear processes such as DNA repair, chromosome maintenance, transcription regulation, and V(D)J recombination. The mechanism underlying the regulation of all the diverse functions of Ku is still unclear, although it seems that Ku is a multifunctional protein that works in the nuclei. In mammalian cells, the Ku heterodimer recruits the catalytic subunit of DNA-dependent protein kinase (DNA-PK), which is dependent on its association with the Ku70/80 heterodimer bound to DNA for its protein kinase activity.


Pssm-ID: 238407 [Multi-domain]  Cd Length: 287  Bit Score: 51.90  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  14 KFGEVSCGVALYTAASTSERITFNTI--NKATGNRV---NRIFIDSETEDPVPKEAQTKGFEIeNGQYIIIDPEEISAAI 88
Cdd:cd00788    12 PGNKLVISVKGYSLVSHAKKPRKYKLdrEKNEERREvksKRKFFDVESGKTLEKADIKKGYKI-GGEKIIFTKEELKKIK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582023753  89 PESNKTLEIEAFIPCSDVDDVYF-DKPYYLTPD---RMGG-DAFAALRDAMKKSMVAAIARTVLfRR---MRTVLIRP-- 158
Cdd:cd00788    91 SFGEPGLRLIGFKPRSTLKPYHNiKKSYFIYPDesdYKGStRLFAALLRSCLKKNKVAICWYIL-RKnspPRLVALVPqe 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582023753 159 ----------HGKGLIASTLNYDYEVRSSEKAFEE-MPKLKIQGEMLDLAKHIIST-KKGEFDPATF 213
Cdd:cd00788   170 eeldepdgqvLPPGFHLVPLPFADDIRKLPSLLEEnASAESASDELVDKAKQIIKKlRLLSYDPDKF 236
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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