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Conserved domains on  [gi|1691287737|gb|QDE40829|]
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Ku protein [Luteibacter pinisoli]

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 ...
1-268 4.18e-119

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


:

Pssm-ID: 440884 [Multi-domain]  Cd Length: 279  Bit Score: 343.64  E-value: 4.18e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   1 MARPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDI 80
Cdd:COG1273     1 MMRAIWKGAISFGLVNIPVKLYSATESHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKGRYVVLEDEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  81 RSAASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALL 160
Cdd:COG1273    81 EALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIARVVLRGRERLAALRPRGDGLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 161 LNILRYQAELVDAEEY-GLPGkavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDD 239
Cdd:COG1273   161 LETLRYPDEVRDADEFpDLPE----DVKVDPKELDMAKQLIESLTGDFDPEKYKDEYREALLELIEAKIEGKEVVAPPEE 236
                         250       260
                  ....*....|....*....|....*....
gi 1691287737 240 DDEHvpehatTNVVDFMELLKKSIGAKKR 268
Cdd:COG1273   237 EPEG------ANVIDLMEALKASLEAAKK 259
 
Name Accession Description Interval E-value
YkoV COG1273
Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and ...
1-268 4.18e-119

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


Pssm-ID: 440884 [Multi-domain]  Cd Length: 279  Bit Score: 343.64  E-value: 4.18e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   1 MARPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDI 80
Cdd:COG1273     1 MMRAIWKGAISFGLVNIPVKLYSATESHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKGRYVVLEDEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  81 RSAASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALL 160
Cdd:COG1273    81 EALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIARVVLRGRERLAALRPRGDGLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 161 LNILRYQAELVDAEEY-GLPGkavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDD 239
Cdd:COG1273   161 LETLRYPDEVRDADEFpDLPE----DVKVDPKELDMAKQLIESLTGDFDPEKYKDEYREALLELIEAKIEGKEVVAPPEE 236
                         250       260
                  ....*....|....*....|....*....
gi 1691287737 240 DDEHvpehatTNVVDFMELLKKSIGAKKR 268
Cdd:COG1273   237 EPEG------ANVIDLMEALKASLEAAKK 259
KU_like cd00789
Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA ...
3-267 3.92e-115

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: 332.58  E-value: 3.92e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   3 RPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDIRS 82
Cdd:cd00789     1 RAIWKGAISFGLVNIPVKLYSATESEDISFHQLHKKDGARIRYQRVCPETGKEVPRDDIVKGYEYEKGEYVILTDEELEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  83 AASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALLLN 162
Cdd:cd00789    81 LPPESTRTIEIVDFVPLDEIDPIYFDKPYYLAPDKGGEKAYALLREALRDTGKVAIAKVVLRTRERLAALRPRGKGLVLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 163 ILRYQAELVDAEEYGLPGKavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDddde 242
Cdd:cd00789   161 TLRYPDEVRSPEELFLPIK---AVKVDPKELEMAKQLIEQLTGDFDPEKYEDEYREALMELIEAKIEGKAIEAAEP---- 233
                         250       260
                  ....*....|....*....|....*
gi 1691287737 243 hvPEHATTNVVDFMELLKKSIGAKK 267
Cdd:cd00789   234 --APAASGNVVDLMEALKKSLEAAK 256
Ku_bact TIGR02772
Ku protein, prokaryotic; Members of this protein family are Ku proteins of non-homologous end ...
2-267 3.30e-107

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: 312.68  E-value: 3.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   2 ARPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDIR 81
Cdd:TIGR02772   1 ARAIWKGAISFGLVNCPVKLYPATESEDISFHQLHREDGNRVRYQKVCSETGKEVEREEIVKGYEYDKGKYVIIEDEDIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  82 SAASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALLL 161
Cdd:TIGR02772  81 SLPPESTKTIEIEAFVDADEIDPIYFDTPYYLAPDKGGEKAYALLREALEDTGKVGIAKVVLRGRERLAALRPVGKGLVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 162 NILRYQAELVDAEEYGLPGKavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDDdd 241
Cdd:TIGR02772 161 TTLRYPDEVRSPDEFFGPIK---DVEVDPEELELAGQLIDKMTGKFDPEDYHDEYREALLELVDAKLEGGKPPKAEEP-- 235
                         250       260
                  ....*....|....*....|....*.
gi 1691287737 242 ehvPEHATTNVVDFMELLKKSIGAKK 267
Cdd:TIGR02772 236 ---AAPAPGNVVDLMDALKASLRAAK 258
Ku pfam02735
Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
12-195 4.24e-40

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: 138.92  E-value: 4.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  12 FGLLNVPIRLMTG-ERRTDIHFRMLDQRNNTPVR--YERVNAETGEEVPWKDIVKAFEYqKGNYVVLEEEDIRSAASEVH 88
Cdd:pfam02735   2 GGLVSIPVKLYSAtEEEKKPSFKKLDRETNDGVRikYKYVCEDTGKEVEKEDIVKGYEY-GGTYVPLSDEELEELKPEST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  89 ETVEIDSFVDAAEIAPAYF--EKPYVLAPAKKAEKG----YVLLRETLKKTGKVGIARVVIRTREY--LAAVIPS----G 156
Cdd:pfam02735  81 KGLDLLGFVPLDEIDPIYFmgDKSYFLYPDKGDIAGstkaFSALREALLETDKVAIARFVLRRREHprLVALRPQeeepD 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1691287737 157 DALLLNILRYQAELVDAEEYGLPGKAVadYRITPKEIEM 195
Cdd:pfam02735 161 PGLVLITLPFADDVREEFFPIPSLLEK--PKPTEEQLDL 197
Ku78 smart00559
Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single ...
53-166 2.03e-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: 71.94  E-value: 2.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   53 GEEVPWKDIVKAFEYqKGNYVVLEEEDIRSAASEVHETVEIDSFVDAAEIAPAYFEKP-YVLAPAKK----AEKGYVLLR 127
Cdd:smart00559   1 GKEVKPEDIVKGYEY-GGRYVPLSDEELEQLKYKSEPGLELLGFKPLSSLPPYYFLRPsYFLVPDDKsvigSTKAFSALV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1691287737  128 ETLKKTGKVGIARVVIRTR--EYLAAVIP-----SGDALLLNILRY 166
Cdd:smart00559  80 EALLETDKIAIARYTLRTKsnPRLVALRPydeedDGEGLVLVQLPF 125
 
Name Accession Description Interval E-value
YkoV COG1273
Non-homologous end joining protein Ku, dsDNA break repair [Replication, recombination and ...
1-268 4.18e-119

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


Pssm-ID: 440884 [Multi-domain]  Cd Length: 279  Bit Score: 343.64  E-value: 4.18e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   1 MARPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDI 80
Cdd:COG1273     1 MMRAIWKGAISFGLVNIPVKLYSATESHDISFHQLHRKDGGRIRYKRVCEVTGKEVEYEDIVKGYEYEKGRYVVLEDEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  81 RSAASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALL 160
Cdd:COG1273    81 EALPPESTKTIDIEQFVPADEIDPIYFDKPYYLAPDKGGEKAYALLREALRKTGKVAIARVVLRGRERLAALRPRGDGLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 161 LNILRYQAELVDAEEY-GLPGkavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDD 239
Cdd:COG1273   161 LETLRYPDEVRDADEFpDLPE----DVKVDPKELDMAKQLIESLTGDFDPEKYKDEYREALLELIEAKIEGKEVVAPPEE 236
                         250       260
                  ....*....|....*....|....*....
gi 1691287737 240 DDEHvpehatTNVVDFMELLKKSIGAKKR 268
Cdd:COG1273   237 EPEG------ANVIDLMEALKASLEAAKK 259
KU_like cd00789
Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA ...
3-267 3.92e-115

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: 332.58  E-value: 3.92e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   3 RPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDIRS 82
Cdd:cd00789     1 RAIWKGAISFGLVNIPVKLYSATESEDISFHQLHKKDGARIRYQRVCPETGKEVPRDDIVKGYEYEKGEYVILTDEELEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  83 AASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALLLN 162
Cdd:cd00789    81 LPPESTRTIEIVDFVPLDEIDPIYFDKPYYLAPDKGGEKAYALLREALRDTGKVAIAKVVLRTRERLAALRPRGKGLVLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 163 ILRYQAELVDAEEYGLPGKavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDddde 242
Cdd:cd00789   161 TLRYPDEVRSPEELFLPIK---AVKVDPKELEMAKQLIEQLTGDFDPEKYEDEYREALMELIEAKIEGKAIEAAEP---- 233
                         250       260
                  ....*....|....*....|....*
gi 1691287737 243 hvPEHATTNVVDFMELLKKSIGAKK 267
Cdd:cd00789   234 --APAASGNVVDLMEALKKSLEAAK 256
Ku_bact TIGR02772
Ku protein, prokaryotic; Members of this protein family are Ku proteins of non-homologous end ...
2-267 3.30e-107

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: 312.68  E-value: 3.30e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   2 ARPIWTGTLTFGLLNVPIRLMTGERRTDIHFRMLDQRNNTPVRYERVNAETGEEVPWKDIVKAFEYQKGNYVVLEEEDIR 81
Cdd:TIGR02772   1 ARAIWKGAISFGLVNCPVKLYPATESEDISFHQLHREDGNRVRYQKVCSETGKEVEREEIVKGYEYDKGKYVIIEDEDIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  82 SAASEVHETVEIDSFVDAAEIAPAYFEKPYVLAPAKKAEKGYVLLRETLKKTGKVGIARVVIRTREYLAAVIPSGDALLL 161
Cdd:TIGR02772  81 SLPPESTKTIEIEAFVDADEIDPIYFDTPYYLAPDKGGEKAYALLREALEDTGKVGIAKVVLRGRERLAALRPVGKGLVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 162 NILRYQAELVDAEEYGLPGKavaDYRITPKEIEMATDLVKSMAGDWKPEAYRDDFRDKLRKAIEKRLKTKGVTTAVDDdd 241
Cdd:TIGR02772 161 TTLRYPDEVRSPDEFFGPIK---DVEVDPEELELAGQLIDKMTGKFDPEDYHDEYREALLELVDAKLEGGKPPKAEEP-- 235
                         250       260
                  ....*....|....*....|....*.
gi 1691287737 242 ehvPEHATTNVVDFMELLKKSIGAKK 267
Cdd:TIGR02772 236 ---AAPAPGNVVDLMDALKASLRAAK 258
KU cd00594
Ku-core domain; includes the central DNA-binding beta-barrels, polypeptide rings, and the ...
3-263 2.54e-59

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: 190.95  E-value: 2.54e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   3 RPIWTGTLTFGL-LNVPIRLMTGERR-TDIHFRMLDQRNNTPVRYERVNAETG-EEVPWKDIVKAFEYqKGNYVVLEEED 79
Cdd:cd00594     1 RAIWKGALSLGLdVSIPVKLYSAATEeKPPSFKQLDRKTGERVKVKRVCKYTGgKEVEKEDIVKGYEY-GGDYVPLTEEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  80 IRSAASEVHETVEIDSFVDAAEIAPAYFEK-PYVLAPA---KKAEKGYVLLRETLKKTGKVGIARVVIRT--REYLAAVI 153
Cdd:cd00594    80 LEQLKLETSKGLDILGFVPASEIPPYYFDKeSYYLVPDdsdKGSEKAFSALRRALLEKDKVAIARYVLRRnsRPRLVALR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737 154 PSG----DALLLNILRYQAELVDAEEygLPGKAVADYRITPKEIEMATDLVKSMAGD-WKPEAYRDDFRDKLRKAIEKRL 228
Cdd:cd00594   160 PQEeedpEGLVLVTLPFADDVRSYPF--PLLLDIKTEKPTDEELELAKQLIDSLDLDdFDPEKFPNPYLQRLYALLEAKA 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1691287737 229 KTKGVTTAVDDDDEHVPEHATTNVVDFMELLKKSI 263
Cdd:cd00594   238 LGEEIPEPPEDLTLPPPEEIPKRVIDLLEALKKSL 272
Ku pfam02735
Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
12-195 4.24e-40

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: 138.92  E-value: 4.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  12 FGLLNVPIRLMTG-ERRTDIHFRMLDQRNNTPVR--YERVNAETGEEVPWKDIVKAFEYqKGNYVVLEEEDIRSAASEVH 88
Cdd:pfam02735   2 GGLVSIPVKLYSAtEEEKKPSFKKLDRETNDGVRikYKYVCEDTGKEVEKEDIVKGYEY-GGTYVPLSDEELEELKPEST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737  89 ETVEIDSFVDAAEIAPAYF--EKPYVLAPAKKAEKG----YVLLRETLKKTGKVGIARVVIRTREY--LAAVIPS----G 156
Cdd:pfam02735  81 KGLDLLGFVPLDEIDPIYFmgDKSYFLYPDKGDIAGstkaFSALREALLETDKVAIARFVLRRREHprLVALRPQeeepD 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1691287737 157 DALLLNILRYQAELVDAEEYGLPGKAVadYRITPKEIEM 195
Cdd:pfam02735 161 PGLVLITLPFADDVREEFFPIPSLLEK--PKPTEEQLDL 197
Ku78 smart00559
Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single ...
53-166 2.03e-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: 71.94  E-value: 2.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   53 GEEVPWKDIVKAFEYqKGNYVVLEEEDIRSAASEVHETVEIDSFVDAAEIAPAYFEKP-YVLAPAKK----AEKGYVLLR 127
Cdd:smart00559   1 GKEVKPEDIVKGYEY-GGRYVPLSDEELEQLKYKSEPGLELLGFKPLSSLPPYYFLRPsYFLVPDDKsvigSTKAFSALV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1691287737  128 ETLKKTGKVGIARVVIRTR--EYLAAVIP-----SGDALLLNILRY 166
Cdd:smart00559  80 EALLETDKIAIARYTLRTKsnPRLVALRPydeedDGEGLVLVQLPF 125
KU80 cd00873
Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in ...
3-146 7.47e-05

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: 43.82  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1691287737   3 RPIWTGTLTFG-LLNVPIRLMTGER-------RTDIHFRMLDQRNNTPVRYER---VNAETGEEVPWKDIVKAFEYQKgN 71
Cdd:cd00873     1 VAAFKGQLTLGsPLSIAVELYKKTKeerppklKKVSDAEKTGEDAFEDVKSERsydVNDDDKTEVEKEDLIKGYRYGR-D 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1691287737  72 YVVLEEEDIRSAASEVHETVEIDSFVDAAEIAPAYF--EKPYVLAPA--KKAEKGYVLLRETLKKTGKVGIARVVIRTR 146
Cdd:cd00873    80 IVPLSEEDEEATKLSTSKGLDILGFIKASNVPRYYLmgESSYVVPQQddEAAALAFSALVRALAELDKYAIARYVYKDN 158
 
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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