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Conserved domains on  [gi|17985997|ref|NP_536773|]
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inverted repeat-binding protein, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KU70 cd00788
Ku-core domain, Ku70 subfamily; Ku70 is a subunit of the Ku protein, which plays a key role in ...
255-546 6.71e-87

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: 272.62  E-value: 6.71e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 255 RCLGHFSFYLGP--NLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRtkRVITVQKQKDDGS-QDIEHEYQIKVTggwytc 331
Cdd:cd00788   1 RALFRLPLELGPgnKLVISVKGYSLVSHAKKPRKYKLDREKNEERR--EVKSKRKFFDVESgKTLEKADIKKGY------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 332 NVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKIAICLF 411
Cdd:cd00788  73 KIGGEKIIFTKEELKKIKSFGEPGLRLIGFKPRSTLKPYHNIKKSYFIYPDESDYKGSTRLFAALLRSCLKKNKVAICWY 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 412 MCKRKSIPRYVALVPVEAPDNGEDknyrSLLCGDGFKIVYLPEAKHIRHL-DLQDWNNTENTADEQKVEFFQKIIKKLRV 490
Cdd:cd00788 153 ILRKNSPPRLVALVPQEEELDEPD----GQVLPPGFHLVPLPFADDIRKLpSLLEENASAESASDELVDKAKQIIKKLRL 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17985997 491 -DYQPNLINDPSLDALQANLLALSLDFSTDTKGLDNLL-DTSQQDKRIEKLLPDYEMF 546
Cdd:cd00788 229 lSYDPDKFPNPSLQKHYKILEALALDEEDPEKPDDLTLpDTEGIDKRLGDLIEEFKKL 286
Ku_N pfam03731
Ku70/Ku80 N-terminal alpha/beta domain; The Ku heterodimer (composed of Ku70 and Ku80) ...
33-256 2.55e-60

Ku70/Ku80 N-terminal alpha/beta 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 amino terminal alpha/beta domain. This domain only makes a small contribution to the dimer interface. The domain comprises a six stranded beta sheet of the Rossman fold.


:

Pssm-ID: 427470  Cd Length: 220  Bit Score: 200.66  E-value: 2.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    33 AILFVVDANLQTAGVERLLE-----ALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPpleASALDNIVMpdncavflpL 107
Cdd:pfam03731   1 AILFVIDVSPAMFESSKLLEapfdmALKCIRELLKSKIISRDKDLIGVVLYGTDNSEN---SEGLPNITV---------L 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   108 RQLTKPIVEHYLEFMGGVETQFADVYGLAEPDGRGRFDLMIRLCIEMLEKCGKKLNNAKIAYVTDVREPHPsNSNHFQAA 187
Cdd:pfam03731  69 RDLDLPGAELILELDQFVESFGRDVRGFSGDSSDGSLLSALWVCLELLQKTGKKLSHKRIFLFTDLDDPFE-DQDKLDIA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17985997   188 LQK--ASDLEGKEFEFHVIPM--VDDFDYEPFYKEFITLSRAIELDAFQVPDAQMLREILSDRKLKQDFLRRC 256
Cdd:pfam03731 148 LQRllAEDLRDTRGEFDLIHLpnADGFDPNLFYKDIIKLGSDEVLNVMLDLEGQKLEDLLAKIRAKKTAKRAH 220
HeH super family cl15188
HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) ...
593-624 7.17e-03

HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) structures. It was demonstrated that the DNA-binding activity of the HEH/LEM domain assists the association of proteins with the centromeric region. This domain is closely related to pfam03020 and pfam02037.


The actual alignment was detected with superfamily member pfam12949:

Pssm-ID: 403988  Cd Length: 35  Bit Score: 34.69  E-value: 7.17e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17985997   593 LTSCTAAQLHFILQHHfDVTMPKSSKKAKLVA 624
Cdd:pfam12949   1 PKSLTVAQLRRILVEH-GIEYPSNAKKADLVR 31
 
Name Accession Description Interval E-value
KU70 cd00788
Ku-core domain, Ku70 subfamily; Ku70 is a subunit of the Ku protein, which plays a key role in ...
255-546 6.71e-87

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: 272.62  E-value: 6.71e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 255 RCLGHFSFYLGP--NLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRtkRVITVQKQKDDGS-QDIEHEYQIKVTggwytc 331
Cdd:cd00788   1 RALFRLPLELGPgnKLVISVKGYSLVSHAKKPRKYKLDREKNEERR--EVKSKRKFFDVESgKTLEKADIKKGY------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 332 NVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKIAICLF 411
Cdd:cd00788  73 KIGGEKIIFTKEELKKIKSFGEPGLRLIGFKPRSTLKPYHNIKKSYFIYPDESDYKGSTRLFAALLRSCLKKNKVAICWY 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 412 MCKRKSIPRYVALVPVEAPDNGEDknyrSLLCGDGFKIVYLPEAKHIRHL-DLQDWNNTENTADEQKVEFFQKIIKKLRV 490
Cdd:cd00788 153 ILRKNSPPRLVALVPQEEELDEPD----GQVLPPGFHLVPLPFADDIRKLpSLLEENASAESASDELVDKAKQIIKKLRL 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17985997 491 -DYQPNLINDPSLDALQANLLALSLDFSTDTKGLDNLL-DTSQQDKRIEKLLPDYEMF 546
Cdd:cd00788 229 lSYDPDKFPNPSLQKHYKILEALALDEEDPEKPDDLTLpDTEGIDKRLGDLIEEFKKL 286
Ku_N pfam03731
Ku70/Ku80 N-terminal alpha/beta domain; The Ku heterodimer (composed of Ku70 and Ku80) ...
33-256 2.55e-60

Ku70/Ku80 N-terminal alpha/beta 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 amino terminal alpha/beta domain. This domain only makes a small contribution to the dimer interface. The domain comprises a six stranded beta sheet of the Rossman fold.


Pssm-ID: 427470  Cd Length: 220  Bit Score: 200.66  E-value: 2.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    33 AILFVVDANLQTAGVERLLE-----ALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPpleASALDNIVMpdncavflpL 107
Cdd:pfam03731   1 AILFVIDVSPAMFESSKLLEapfdmALKCIRELLKSKIISRDKDLIGVVLYGTDNSEN---SEGLPNITV---------L 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   108 RQLTKPIVEHYLEFMGGVETQFADVYGLAEPDGRGRFDLMIRLCIEMLEKCGKKLNNAKIAYVTDVREPHPsNSNHFQAA 187
Cdd:pfam03731  69 RDLDLPGAELILELDQFVESFGRDVRGFSGDSSDGSLLSALWVCLELLQKTGKKLSHKRIFLFTDLDDPFE-DQDKLDIA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17985997   188 LQK--ASDLEGKEFEFHVIPM--VDDFDYEPFYKEFITLSRAIELDAFQVPDAQMLREILSDRKLKQDFLRRC 256
Cdd:pfam03731 148 LQRllAEDLRDTRGEFDLIHLpnADGFDPNLFYKDIIKLGSDEVLNVMLDLEGQKLEDLLAKIRAKKTAKRAH 220
vWA_ku cd01458
Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to ...
31-246 4.74e-52

Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks (DSB) in a preferred orientation. DSB's are repaired by either homologues recombination or non-homologues end joining and facilitate repair by the non-homologous end-joining pathway (NHEJ). The Ku heterodimer is required for accurate process that tends to preserve the sequence at the junction. Ku78 is found in all three kingdoms of life. However, only the eukaryotic proteins have a vWA domain fused to them at their N-termini. The vWA domain is not involved in DNA binding but may very likey mediate Ku78's interactions with other proteins. Members of this subgroup lack the conserved MIDAS motif.


Pssm-ID: 238735  Cd Length: 218  Bit Score: 178.33  E-value: 4.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997  31 REAILFVVDAN----LQTAG--VERLLEALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPPleasaldniVMPDNCAVF 104
Cdd:cd01458   1 KESVVFLVDVSpsmfESKDGeyESPFEEALKCIRQLMKSKIISSPKDLVGVVFYGTEESKNP---------VGYENIYVL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 105 LPLRQLTKPIVEHYLEFMGGVETQFADVYGlaePDGRGRFDLMIRLCIEMLEKCGKKLNNAKIAYVTDVREPHPSNSNHF 184
Cdd:cd01458  72 LDLDTPGAERVEDLKELIEPGGLSFAGQVG---DSGQVSLSDALWVCLDLFSKGKKKKSHKRIFLFTNNDDPHGGDSIKD 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 185 QAALQKASDLEGKEFEFHVIPMVDD---FDYEPFYKEFITLSRA---IELDAFQVP--DAQMLREILSDR 246
Cdd:cd01458 149 SQAAVKAEDLKDKGIELELFPLSSPgkkFDVSKFYKDIIALVEDaneELLDEFTEPskDLEDLLKRLRAK 218
ku70 TIGR00578
ATP-dependent DNA helicase II, 70 kDa subunit (ku70); Proteins in this family are involved in ...
20-628 1.21e-48

ATP-dependent DNA helicase II, 70 kDa subunit (ku70); Proteins in this family are involved in non-homologous end joining, a process used for the repair of double stranded DNA breaks. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Cutoff does not detect the putative ku70 homologs in yeast. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273151 [Multi-domain]  Cd Length: 586  Bit Score: 179.32  E-value: 1.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    20 EDVSMKRDYHGREAILFVVDANL----QTAGVERL---LEALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPPLEasaL 92
Cdd:TIGR00578   1 PEATGDYKYSGRDSLIFLVDASKamfeESQGEDELtpfDMSIQCIQSVYTSKIISSDKDLLAVVFYGTEKDKNSVN---F 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    93 DNIVMpdncavflpLRQLTKPIVEHYLE---FMGGV-ETQFADVYGLAEPDGRGRfdlMIRLCIEMLEKCGKKLNNAKIA 168
Cdd:TIGR00578  78 KNIYV---------LQDLDNPGAKRVLEldqFKGDQgPKKFRDTYGHGSDYSLSE---VLWVCANLFSDVQVRMSHKRIM 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   169 YVTDVREPHPSNSNHFQAALQKASDL--EGKEFEFHVIPMVDDFDYEPFYKEFITLSRAIELDAFqvPDAQMLREILSDR 246
Cdd:TIGR00578 146 LFTNEDDPHGNDSAKASRARTKAGDLrdTGIFLDLMHLKKPGGFDISLFYRDIITDAEDEDLGVH--PEESSKLEDLLRK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   247 KLKQDFLRRCLGHFSFYLGPNLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRTKRVITvqkQKDDGSQDIEHEYQIKVTg 326
Cdd:TIGR00578 224 VRAKETKKRALSRLKFKLGKDVVMSVGIYNLVQKAGKPAPVRLYRETNEPVKTKTRTF---NMDTGSLLLPSDTKRSQT- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   327 gwytcnVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKI 406
Cdd:TIGR00578 300 ------YGGRQIYLEKEETEELKRFDPPGLQLMGFKPLSMLKKQHHLRPSLFVYPEESLVRGSTTLFSALLQKCLEKEVA 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   407 AICLFMCKRKSIPRYVALVPVEApdngEDKNYRSLLCGDGFKIVYLPEAKHIRHLDLQDwnntENTADEQKVEFFQKIIK 486
Cdd:TIGR00578 374 ALCRYISRRNQPPYFVALVPQEE----ELDDQKIQVTPPGFHLVFLPFADDKRKVPFTE----KVKATPEQVDKMKAIVE 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   487 KLRVDYQPNLINDPSLDALQANLLALSLDFSTDTKGLD-NLLDTSQQDKRIEKLLPDYE--MFAPEAEPHKKRAAKSTTA 563
Cdd:TIGR00578 446 KLRFTYRSDSFENPVLQQHFRNLEALALDMMEPEQAVDlTLPKVEAMKKRLGSLVDEFKelVYPPGYNPEGKVAKRKQAG 525
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17985997   564 GASGPKMAKIDDDQlkefEFVKSLNKDEALTSCTAAQLHFILQHHfdvTMPKSSKKAKLVAKIEE 628
Cdd:TIGR00578 526 EGSQSKKPKVENSE----EELREHAKKGTLGKLTVSVLKDFCKAY---GLRSGSKKQELLDALTK 583
Ku78 smart00559
Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single ...
319-469 4.90e-46

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: 159.38  E-value: 4.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    319 EYQIKVTGGWYTCNVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWE 398
Cdd:smart00559   1 GKEVKPEDIVKGYEYGGRYVPLSDEELEQLKYKSEPGLELLGFKPLSSLPPYYFLRPSYFLVPDDKSVIGSTKAFSALVE 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17985997    399 RCLVRDKIAICLFMCKRKSIPRYVALVPVEAPDNGEdknyrsllcgdGFKIVYLPEAKHIRHLDLQDWNNT 469
Cdd:smart00559  81 ALLETDKIAIARYTLRTKSNPRLVALRPYDEEDDGE-----------GLVLVQLPFADDVRKLDFPELNTT 140
Ku pfam02735
Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
264-479 2.07e-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: 146.24  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   264 LGPNLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRTKRVITVQ-KQKDDGSQDIEHEYQIkvtggwytcnvGERDLRISM 342
Cdd:pfam02735   1 IGGLVSIPVKLYSATEEEKKPSFKKLDRETNDGVRIKYKYVCEdTGKEVEKEDIVKGYEY-----------GGTYVPLSD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   343 DQLNRVRNLHKPQMMLLGFKHRSS-LPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKIAICLFMCKRKSIPRY 421
Cdd:pfam02735  70 EELEELKPESTKGLDLLGFVPLDEiDPIYFMGDKSYFLYPDKGDIAGSTKAFSALREALLETDKVAIARFVLRRREHPRL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17985997   422 VALVPVEAPDngedknyrsllcGDGFKIVYLPEAKHIRHLDLQDWNNTE-NTADEQKVE 479
Cdd:pfam02735 150 VALRPQEEEP------------DPGLVLITLPFADDVREEFFPIPSLLEkPKPTEEQLD 196
HeH pfam12949
HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) ...
593-624 7.17e-03

HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) structures. It was demonstrated that the DNA-binding activity of the HEH/LEM domain assists the association of proteins with the centromeric region. This domain is closely related to pfam03020 and pfam02037.


Pssm-ID: 403988  Cd Length: 35  Bit Score: 34.69  E-value: 7.17e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17985997   593 LTSCTAAQLHFILQHHfDVTMPKSSKKAKLVA 624
Cdd:pfam12949   1 PKSLTVAQLRRILVEH-GIEYPSNAKKADLVR 31
 
Name Accession Description Interval E-value
KU70 cd00788
Ku-core domain, Ku70 subfamily; Ku70 is a subunit of the Ku protein, which plays a key role in ...
255-546 6.71e-87

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: 272.62  E-value: 6.71e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 255 RCLGHFSFYLGP--NLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRtkRVITVQKQKDDGS-QDIEHEYQIKVTggwytc 331
Cdd:cd00788   1 RALFRLPLELGPgnKLVISVKGYSLVSHAKKPRKYKLDREKNEERR--EVKSKRKFFDVESgKTLEKADIKKGY------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 332 NVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKIAICLF 411
Cdd:cd00788  73 KIGGEKIIFTKEELKKIKSFGEPGLRLIGFKPRSTLKPYHNIKKSYFIYPDESDYKGSTRLFAALLRSCLKKNKVAICWY 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 412 MCKRKSIPRYVALVPVEAPDNGEDknyrSLLCGDGFKIVYLPEAKHIRHL-DLQDWNNTENTADEQKVEFFQKIIKKLRV 490
Cdd:cd00788 153 ILRKNSPPRLVALVPQEEELDEPD----GQVLPPGFHLVPLPFADDIRKLpSLLEENASAESASDELVDKAKQIIKKLRL 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17985997 491 -DYQPNLINDPSLDALQANLLALSLDFSTDTKGLDNLL-DTSQQDKRIEKLLPDYEMF 546
Cdd:cd00788 229 lSYDPDKFPNPSLQKHYKILEALALDEEDPEKPDDLTLpDTEGIDKRLGDLIEEFKKL 286
Ku_N pfam03731
Ku70/Ku80 N-terminal alpha/beta domain; The Ku heterodimer (composed of Ku70 and Ku80) ...
33-256 2.55e-60

Ku70/Ku80 N-terminal alpha/beta 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 amino terminal alpha/beta domain. This domain only makes a small contribution to the dimer interface. The domain comprises a six stranded beta sheet of the Rossman fold.


Pssm-ID: 427470  Cd Length: 220  Bit Score: 200.66  E-value: 2.55e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    33 AILFVVDANLQTAGVERLLE-----ALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPpleASALDNIVMpdncavflpL 107
Cdd:pfam03731   1 AILFVIDVSPAMFESSKLLEapfdmALKCIRELLKSKIISRDKDLIGVVLYGTDNSEN---SEGLPNITV---------L 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   108 RQLTKPIVEHYLEFMGGVETQFADVYGLAEPDGRGRFDLMIRLCIEMLEKCGKKLNNAKIAYVTDVREPHPsNSNHFQAA 187
Cdd:pfam03731  69 RDLDLPGAELILELDQFVESFGRDVRGFSGDSSDGSLLSALWVCLELLQKTGKKLSHKRIFLFTDLDDPFE-DQDKLDIA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17985997   188 LQK--ASDLEGKEFEFHVIPM--VDDFDYEPFYKEFITLSRAIELDAFQVPDAQMLREILSDRKLKQDFLRRC 256
Cdd:pfam03731 148 LQRllAEDLRDTRGEFDLIHLpnADGFDPNLFYKDIIKLGSDEVLNVMLDLEGQKLEDLLAKIRAKKTAKRAH 220
vWA_ku cd01458
Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to ...
31-246 4.74e-52

Ku70/Ku80 N-terminal domain. The Ku78 heterodimer (composed of Ku70 and Ku80) contributes to genomic integrity through its ability to bind DNA double-strand breaks (DSB) in a preferred orientation. DSB's are repaired by either homologues recombination or non-homologues end joining and facilitate repair by the non-homologous end-joining pathway (NHEJ). The Ku heterodimer is required for accurate process that tends to preserve the sequence at the junction. Ku78 is found in all three kingdoms of life. However, only the eukaryotic proteins have a vWA domain fused to them at their N-termini. The vWA domain is not involved in DNA binding but may very likey mediate Ku78's interactions with other proteins. Members of this subgroup lack the conserved MIDAS motif.


Pssm-ID: 238735  Cd Length: 218  Bit Score: 178.33  E-value: 4.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997  31 REAILFVVDAN----LQTAG--VERLLEALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPPleasaldniVMPDNCAVF 104
Cdd:cd01458   1 KESVVFLVDVSpsmfESKDGeyESPFEEALKCIRQLMKSKIISSPKDLVGVVFYGTEESKNP---------VGYENIYVL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 105 LPLRQLTKPIVEHYLEFMGGVETQFADVYGlaePDGRGRFDLMIRLCIEMLEKCGKKLNNAKIAYVTDVREPHPSNSNHF 184
Cdd:cd01458  72 LDLDTPGAERVEDLKELIEPGGLSFAGQVG---DSGQVSLSDALWVCLDLFSKGKKKKSHKRIFLFTNNDDPHGGDSIKD 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 185 QAALQKASDLEGKEFEFHVIPMVDD---FDYEPFYKEFITLSRA---IELDAFQVP--DAQMLREILSDR 246
Cdd:cd01458 149 SQAAVKAEDLKDKGIELELFPLSSPgkkFDVSKFYKDIIALVEDaneELLDEFTEPskDLEDLLKRLRAK 218
ku70 TIGR00578
ATP-dependent DNA helicase II, 70 kDa subunit (ku70); Proteins in this family are involved in ...
20-628 1.21e-48

ATP-dependent DNA helicase II, 70 kDa subunit (ku70); Proteins in this family are involved in non-homologous end joining, a process used for the repair of double stranded DNA breaks. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Cutoff does not detect the putative ku70 homologs in yeast. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273151 [Multi-domain]  Cd Length: 586  Bit Score: 179.32  E-value: 1.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    20 EDVSMKRDYHGREAILFVVDANL----QTAGVERL---LEALNIIRTAFISGLLVNDKDLIGLIFANTKHSPPPLEasaL 92
Cdd:TIGR00578   1 PEATGDYKYSGRDSLIFLVDASKamfeESQGEDELtpfDMSIQCIQSVYTSKIISSDKDLLAVVFYGTEKDKNSVN---F 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    93 DNIVMpdncavflpLRQLTKPIVEHYLE---FMGGV-ETQFADVYGLAEPDGRGRfdlMIRLCIEMLEKCGKKLNNAKIA 168
Cdd:TIGR00578  78 KNIYV---------LQDLDNPGAKRVLEldqFKGDQgPKKFRDTYGHGSDYSLSE---VLWVCANLFSDVQVRMSHKRIM 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   169 YVTDVREPHPSNSNHFQAALQKASDL--EGKEFEFHVIPMVDDFDYEPFYKEFITLSRAIELDAFqvPDAQMLREILSDR 246
Cdd:TIGR00578 146 LFTNEDDPHGNDSAKASRARTKAGDLrdTGIFLDLMHLKKPGGFDISLFYRDIITDAEDEDLGVH--PEESSKLEDLLRK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   247 KLKQDFLRRCLGHFSFYLGPNLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRTKRVITvqkQKDDGSQDIEHEYQIKVTg 326
Cdd:TIGR00578 224 VRAKETKKRALSRLKFKLGKDVVMSVGIYNLVQKAGKPAPVRLYRETNEPVKTKTRTF---NMDTGSLLLPSDTKRSQT- 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   327 gwytcnVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKI 406
Cdd:TIGR00578 300 ------YGGRQIYLEKEETEELKRFDPPGLQLMGFKPLSMLKKQHHLRPSLFVYPEESLVRGSTTLFSALLQKCLEKEVA 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   407 AICLFMCKRKSIPRYVALVPVEApdngEDKNYRSLLCGDGFKIVYLPEAKHIRHLDLQDwnntENTADEQKVEFFQKIIK 486
Cdd:TIGR00578 374 ALCRYISRRNQPPYFVALVPQEE----ELDDQKIQVTPPGFHLVFLPFADDKRKVPFTE----KVKATPEQVDKMKAIVE 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   487 KLRVDYQPNLINDPSLDALQANLLALSLDFSTDTKGLD-NLLDTSQQDKRIEKLLPDYE--MFAPEAEPHKKRAAKSTTA 563
Cdd:TIGR00578 446 KLRFTYRSDSFENPVLQQHFRNLEALALDMMEPEQAVDlTLPKVEAMKKRLGSLVDEFKelVYPPGYNPEGKVAKRKQAG 525
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17985997   564 GASGPKMAKIDDDQlkefEFVKSLNKDEALTSCTAAQLHFILQHHfdvTMPKSSKKAKLVAKIEE 628
Cdd:TIGR00578 526 EGSQSKKPKVENSE----EELREHAKKGTLGKLTVSVLKDFCKAY---GLRSGSKKQELLDALTK 583
KU cd00594
Ku-core domain; includes the central DNA-binding beta-barrels, polypeptide rings, and the ...
255-545 2.02e-48

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: 170.53  E-value: 2.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 255 RCLGHFSFYLGPNLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRTKRVItvqkqKDDGSQDIEHEYQIKVtggwytCNVG 334
Cdd:cd00594   1 RAIWKGALSLGLDVSIPVKLYSAATEEKPPSFKQLDRKTGERVKVKRVC-----KYTGGKEVEKEDIVKG------YEYG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 335 ERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDqSIIGSKRLFRALWERCLVRDKIAICLFMCK 414
Cdd:cd00594  70 GDYVPLTEEELEQLKLETSKGLDILGFVPASEIPPYYFDKESYYLVPDD-SDKGSEKAFSALRRALLEKDKVAIARYVLR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 415 RKSIPRYVALVPVEAPDNgedknyrsllcgDGFKIVYLPEAKHIRHL-DLQDWNNTENTADEQKVEFFQKIIKKLRVD-Y 492
Cdd:cd00594 149 RNSRPRLVALRPQEEEDP------------EGLVLVTLPFADDVRSYpFPLLLDIKTEKPTDEELELAKQLIDSLDLDdF 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 17985997 493 QPNLINDPSLDALQANLLALSLDFSTDTKGLD-NLLDTSQQDKRIEKLLPDYEM 545
Cdd:cd00594 217 DPEKFPNPYLQRLYALLEAKALGEEIPEPPEDlTLPPPEEIPKRVIDLLEALKK 270
Ku78 smart00559
Ku70 and Ku80 are 70kDa and 80kDa subunits of the Lupus Ku autoantigen; This is a single ...
319-469 4.90e-46

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: 159.38  E-value: 4.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997    319 EYQIKVTGGWYTCNVGERDLRISMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIIGSKRLFRALWE 398
Cdd:smart00559   1 GKEVKPEDIVKGYEYGGRYVPLSDEELEQLKYKSEPGLELLGFKPLSSLPPYYFLRPSYFLVPDDKSVIGSTKAFSALVE 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17985997    399 RCLVRDKIAICLFMCKRKSIPRYVALVPVEAPDNGEdknyrsllcgdGFKIVYLPEAKHIRHLDLQDWNNT 469
Cdd:smart00559  81 ALLETDKIAIARYTLRTKSNPRLVALRPYDEEDDGE-----------GLVLVQLPFADDVRKLDFPELNTT 140
Ku pfam02735
Ku70/Ku80 beta-barrel domain; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
264-479 2.07e-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: 146.24  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   264 LGPNLSMSVQYYNYFQRRAYPRKVQILRRDNSVVRTKRVITVQ-KQKDDGSQDIEHEYQIkvtggwytcnvGERDLRISM 342
Cdd:pfam02735   1 IGGLVSIPVKLYSATEEEKKPSFKKLDRETNDGVRIKYKYVCEdTGKEVEKEDIVKGYEY-----------GGTYVPLSD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   343 DQLNRVRNLHKPQMMLLGFKHRSS-LPEVSYIKPANFMYPDDQSIIGSKRLFRALWERCLVRDKIAICLFMCKRKSIPRY 421
Cdd:pfam02735  70 EELEELKPESTKGLDLLGFVPLDEiDPIYFMGDKSYFLYPDKGDIAGSTKAFSALREALLETDKVAIARFVLRRREHPRL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17985997   422 VALVPVEAPDngedknyrsllcGDGFKIVYLPEAKHIRHLDLQDWNNTE-NTADEQKVE 479
Cdd:pfam02735 150 VALRPQEEEP------------DPGLVLITLPFADDVREEFFPIPSLLEkPKPTEEQLD 196
Ku_C pfam03730
Ku70/Ku80 C-terminal arm; The Ku heterodimer (composed of Ku70 and Ku80) contributes to ...
491-573 5.51e-11

Ku70/Ku80 C-terminal arm; 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 C terminal arm. This alpha helical region embraces the beta-barrel domain pfam02735 of the opposite subunit.


Pssm-ID: 461029  Cd Length: 79  Bit Score: 58.82  E-value: 5.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997   491 DYQPNLINDPSLDALQANLLALSLDFSTDTKGLDN-LLDTSQQDKRIEKLLPDY-EMFAPEAEPhkkraaKSTTAGASGP 568
Cdd:pfam03730   1 SYNPDKFPNPSLQRHYQNLQALALDEDEPEEPEDLtLPKYEAIDKRIGKLLEEFkELFELEDYK------PDEDEEGPAA 74

                  ....*
gi 17985997   569 KMAKI 573
Cdd:pfam03730  75 KKAKI 79
KU80 cd00873
Ku-core domain, Ku80 subfamily; Ku80 is a subunit of the Ku protein, which plays a key role in ...
264-503 2.87e-03

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: 39.97  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 264 LGPNLSMSVQYYnYFQRRAYPRKvqilrrdnsvvrTKRVITVQKQKDDGSQDIEHEYQIKVTGGwYTCNVgERDLRI--- 340
Cdd:cd00873  10 LGSPLSIAVELY-KKTKEERPPK------------LKKVSDAEKTGEDAFEDVKSERSYDVNDD-DKTEV-EKEDLIkgy 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 341 ---------SMDQLNRVRNLHKPQMMLLGFKHRSSLPEVSYIKPANFMYPDDQSIiGSKRLFRALWERCLVRDKIAICLF 411
Cdd:cd00873  75 rygrdivplSEEDEEATKLSTSKGLDILGFIKASNVPRYYLMGESSYVVPQQDDE-AAALAFSALVRALAELDKYAIARY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17985997 412 MCKRKSIPRYVALVPVeapdngEDKNYRSLLcgdgfkIVYLPEAKHIRHLD---LQDwNNTENTADEQKVEFFQKIIKKL 488
Cdd:cd00873 154 VYKDNSEPQLGVLFPR------IKEDYECLV------LVRLPFAEDVRQYRfpsLDK-LKTPNLPTEEQLEAMDDLVDSM 220
                       250
                ....*....|....*
gi 17985997 489 RVDYQPNLINDPSLD 503
Cdd:cd00873 221 DLDDDEEDDPEEALK 235
HeH pfam12949
HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) ...
593-624 7.17e-03

HeH/LEM domain; This is a HeH domain. HeH domains form helix-extended loop-helix (HeH) structures. It was demonstrated that the DNA-binding activity of the HEH/LEM domain assists the association of proteins with the centromeric region. This domain is closely related to pfam03020 and pfam02037.


Pssm-ID: 403988  Cd Length: 35  Bit Score: 34.69  E-value: 7.17e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17985997   593 LTSCTAAQLHFILQHHfDVTMPKSSKKAKLVA 624
Cdd:pfam12949   1 PKSLTVAQLRRILVEH-GIEYPSNAKKADLVR 31
 
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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