|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
106-311 |
1.61e-88 |
|
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51D, together with the other RAD51 paralogs, RAD51B, RAD51C, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410897 [Multi-domain] Cd Length: 209 Bit Score: 264.50 E-value: 1.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 106 DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSF 185
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 186 DIFRMLDMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQQR-EGLALMMQLARELKILARDLGVAVVVTNHLT 264
Cdd:cd19489 81 DPYELLDLLEELRNTLSQQQENLYSRLKLVIIDSLSALISPLLGGSKHsEGHALLASLARLLKKLAAEYQIAVLVTNLTV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907080609 265 RDWDGRRF---KPALGRSWSFVPSTRILLDVTEGAGTlGSSQRTVCLTKS 311
Cdd:cd19489 161 RGGDGGQQgstKPALGEYWESVPSTRLLLSRDENDPE-ESGVCTATLLKS 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
112-291 |
1.67e-46 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 155.97 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 112 GEVTEIVGGPGSGKTQVCLCVAANVAHsLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSFDifrml 191
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALL-LGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYFRPPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 192 DMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQ------QREGLALMMQLARELKILARDLGVAVVVTNHLTR 265
Cdd:cd01393 75 TLAHLLALDSLPESLFPPPNTSLVVVDSVSALFRKAFPRGgdgdssSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTT 154
|
170 180 190
....*....|....*....|....*....|
gi 1907080609 266 DWDGR----RFKPALGRSWSFVPSTRILLD 291
Cdd:cd01393 155 KIRGGsgasLVPPALGNTWEHSVSTRLLLY 184
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
102-312 |
3.49e-29 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 111.64 E-value: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 102 DKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----HSLQQNVLYVDSNGGMTASRLLQLLQART--------QD 168
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkGGLDGGVLYIDTESKFSAERLAEIAEARFpeafsgfmEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEKQASALQRIQVVRSFDIFRMLDMLQDLRgtiaqqEATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARE--- 245
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLE------EHILSSGVRLVVIDSIAALVRREFGGSDGEVTERHNALAREass 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907080609 246 LKILARDLGVAVVVTNHL-TRDWDGRRF----KPALGRSWSFVPSTRILLDVtegagTLGSSQRTVCLTKSP 312
Cdd:cd19493 155 LKRLAEEFRIAVLVTNQAtTHFGDAGDGssgvTAALGDAWAHAVNTRLRLER-----CLLQLRRVLEIVKSP 221
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
112-312 |
4.61e-25 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 99.22 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 112 GEVTEIVGGPGSGKTQVCLCVAANV-----AHSLQQNVLYVDSNGgmtasrllqllqartqdeekqasalqriqvvrSFD 186
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVqipkcFGGLAGEAIYIDTEG--------------------------------SFN 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 187 I--FRMLDMLQdLRGTIAQQEA--TSSGAVKVVIVDSVTAvvaPLLGGQQREGL--ALMMQLARELKILARDLGVAVVVT 260
Cdd:cd19492 49 IhyFRVHDYVE-LLALINSLPKflEDHPKVKLIVVDSIAF---PFRHDFDDLAQrtRLLNGLAQLLHSLARQHNLAVVLT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907080609 261 NHLT---RDWDGRRFKPALGRSWSFVPSTRILLdvtegagTLGSSQRTVCLTKSP 312
Cdd:cd19492 125 NQVTtkiSEDGQSQLVPALGESWSHACTTRLFL-------TWDEKQRFAHLYKSP 172
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
94-324 |
1.23e-22 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 93.92 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDSNgGMTASRLLQLLQARTQdeekqa 173
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAA-KQGKKVVYIDTE-GLSPERFQQIAGERFE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 174 SALQRIQVVRSFDIFRMLDMLQDLRGTIaqqeatSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARELKIlARDL 253
Cdd:cd01394 73 SIASNIIVFEPYSFDEQGVAIQEAEKLL------KSDKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLSI-ARKY 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907080609 254 GVAVVVTNHLTRDWDGRRFKPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTGLQEMIDI 324
Cdd:cd01394 146 DIPVVITNQVYSDIDDDRLKPVGGTLLEHWSKAIIRLEKSPP------GLRRATLEKHRSRPEGQSAGFRI 210
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
26-317 |
1.46e-22 |
|
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239), and archaeal RadB (TIGR02237). This protein is involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 131290 [Multi-domain] Cd Length: 310 Bit Score: 95.97 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 26 GGGPRAPRVLR---VGKVADLAAADLEEVAQKCGLS----YKALVALRRvlLAQFSAFPlNGADLYEELKTSTAIlSTGI 98
Cdd:TIGR02236 6 GVGPATAEKLReagYDTFEAIAVASPKELSEIAGISegtaAKIIQAARK--AADLGGFE-TADDVLERRKTIGKI-TTGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 99 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAH-----SLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKqa 173
Cdd:TIGR02236 82 KELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLpeekgGLGGKAVYIDTENTFRPERIMQMAEARGLDPDE-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 174 sALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssGAVKVVIVDSVTAVV-APLLGgqqREGLALMMQ-LARELKILAR 251
Cdd:TIGR02236 160 -VLKNIYVARAYNSNHQMLLVEKAEDLIKELN----NPVKLLIVDSLTSHFrAEYVG---RGALAERQQkLNKHLHDLLR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907080609 252 --DL-GVAVVVTNHLTRDWD---GRRFKPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTG 317
Cdd:TIGR02236 232 laDLyNAAVVVTNQVMARPDaffGDPTRPIGGHILGHAATFRVYLRKGKG------DKRIARLVDSPHLPEG 297
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
94-281 |
1.87e-22 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 93.77 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDSNgGMTASRLLQLLqartqdEEKQA 173
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAA-KNGKKVIYIDTE-GLSPERFKQIA------GEDFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 174 SALQRIQVVRSFDiFRMLDM-LQDLRGTIAQQeatssgaVKVVIVDSVTAVVApLLGGQQREGLALMMQLARELKIL--- 249
Cdd:PRK09361 77 ELLSNIIIFEPSS-FEEQSEaIRKAEKLAKEN-------VGLIVLDSATSLYR-LELEDEEDNSKLNRELGRQLTHLlkl 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1907080609 250 ARDLGVAVVVTNHLTRDWDGRRFKPALGRS---WS 281
Cdd:PRK09361 148 ARKHDLAVVITNQVYSDIDSDGLRPLGGHTlehWS 182
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
94-290 |
1.47e-21 |
|
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ATPase RecA protein.
Pssm-ID: 462471 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:pfam08423 19 ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLChtLCVTCQLPLEMgggEGKALYIDTEGTFRPERLVAIAERYGLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGqqREGLAL-MMQLARELK 247
Cdd:pfam08423 99 PE---DVLDNVAYARAYNSEHQMQLLQQAAAMMSESR------FALLIVDSATALYRTDFSG--RGELAErQQHLAKFLR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907080609 248 ILAR---DLGVAVVVTNHLTRDWDGRR--F-----KPALGRSWSFVPSTRILL 290
Cdd:pfam08423 168 TLQRladEFGVAVVITNQVVAQVDGAAgmFsgdpkKPIGGHIMAHASTTRLSL 220
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
101-312 |
6.69e-21 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 90.04 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 101 LDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHS---LQQNVLYVDSNGGMTASRLLQLLQ--ARTQDEEKQA 173
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLClqLALTVQLPRElggLGGGAVYICTESSFPSKRLQQLASslPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 174 SALQRIQVVRSFDifrmldmLQDLRGTIAQQ--EATSSGAVKVVIVDSVTAVV-----APLLGGQQREglALMMQLAREL 246
Cdd:cd19491 81 NFLDNIFVEHVAD-------LETLEHCLNYQlpALLERGPIRLVVIDSIAALFrsefdTSRSDLVERA--KYLRRLADHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 247 KILARDLGVAVVVTNHLTRDWD-------------------------GRRFKPALGRSWSFVPSTRILLDVTEGAGTLGS 301
Cdd:cd19491 152 KRLADKYNLAVVVVNQVTDRFDsssdasglgvldylsqfssfsggvsGNRKVPALGLTWANLVNTRLMLSRTPKRITDSS 231
|
250
....*....|....*
gi 1907080609 302 SQ----RTVCLTKSP 312
Cdd:cd19491 232 AAsisvRRLEVVFSP 246
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
94-317 |
5.68e-20 |
|
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a homolog of Rad51. RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR)
Pssm-ID: 410923 [Multi-domain] Cd Length: 233 Bit Score: 87.03 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----HSLQQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQlppeeGGLNGKAVYIDTENTFRPERIMQMAKALGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEKqasALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgAVKVVIVDSVTAVV-APLLGgqqREGLALMMQ-LAREL 246
Cdd:cd19515 81 PDE---VLDNIYVARAYNSNHQMLLVEKAEDLIKEGN-----NIKLLIVDSLTSHFrAEYVG---RGTLAERQQkLNKHL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080609 247 KILAR--DL-GVAVVVTNHLTRDWD---GRRFKPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTG 317
Cdd:cd19515 150 HDLHRlaDLyNIAVLVTNQVMAKPDaffGDPTQAIGGHILGHAATFRVYLRKGKG------GKRIARLVDSPHLPEG 220
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
40-261 |
7.43e-20 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 88.40 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 40 VADLAAADLEEVAQKCGLSYKA----LVALRRVL-LAQFSAfplnGADLYEELKtSTAILSTGIGSLDKLLDAGLYTGEV 114
Cdd:PRK04301 30 VEAIAVASPKELSEAAGIGESTaakiIEAAREAAdIGGFET----ALEVLERRK-NVGKITTGSKELDELLGGGIETQSI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 115 TEIVGGPGSGKTQVCLCVAANV-----AHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKqasALQRIQVVRSFDI-- 187
Cdd:PRK04301 105 TEFYGEFGSGKTQICHQLAVNVqlpeeKGGLEGKAVYIDTEGTFRPERIEQMAEALGLDPDE---VLDNIHVARAYNSdh 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 188 -FRMLDMLQDLrgtIAQQEatssgAVKVVIVDSVTAVV-APLLGgqqREGLA-----LMMQLARELKiLARDLGVAVVVT 260
Cdd:PRK04301 182 qMLLAEKAEEL---IKEGE-----NIKLVIVDSLTAHFrAEYVG---RGNLAerqqkLNKHLHDLLR-LADLYNAAVVVT 249
|
.
gi 1907080609 261 N 261
Cdd:PRK04301 250 N 250
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
94-317 |
4.01e-18 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 82.19 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHS---LQQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLChtLAVTCQLPIDrggGEGKAIYIDTEGTFRPERLRAIAQRFGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGQQrEGLALMMQLARELKI 248
Cdd:cd01123 81 PD---DVLDNVAYARAFNSDHQTQLLDQAAAMMVESR------FKLLIVDSATALYRTDYSGRG-ELSARQMHLAKFLRM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080609 249 LAR---DLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILLDVTEGagtlgsSQRTVCLTKSPRQPTG 317
Cdd:cd01123 151 LQRladEFGVAVVVTNQVVAQVDGAMMfaadpkKPIGGNILAHASTTRLYLRKGRG------ETRICKIYDSPCLPEA 222
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
40-290 |
3.98e-17 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 80.93 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 40 VADLAAADLEEVAQKCGLS-YKALvalrRVLLAQFSAFPL---NGADLYEElKTSTAILSTGIGSLDKLLDAGLYTGEVT 115
Cdd:PLN03186 52 VESLAYAPKKDLLQIKGISeAKVE----KILEAASKLVPLgftTASQLHAQ-RQEIIQITTGSRELDKILEGGIETGSIT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 116 EIVGGPGSGKTQVC--LCVAANVahSLQQ-----NVLYVDSNGGMTASRLLQLLQARTQDeekQASALQRIQVVRSFDIF 188
Cdd:PLN03186 127 EIYGEFRTGKTQLChtLCVTCQL--PLDQgggegKAMYIDTEGTFRPQRLIQIAERFGLN---GADVLENVAYARAYNTD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 189 RMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGQQrEGLALMMQLARELKILAR---DLGVAVVVTNHLTR 265
Cdd:PLN03186 202 HQSELLLEAASMMAETR------FALMIVDSATALYRTEFSGRG-ELSARQMHLGKFLRSLQRladEFGVAVVITNQVVA 274
|
250 260 270
....*....|....*....|....*....|.
gi 1907080609 266 DWDGRRF------KPALGRSWSFVPSTRILL 290
Cdd:PLN03186 275 QVDGSAFfagpqlKPIGGNIMAHASTTRLAL 305
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
94-269 |
1.12e-16 |
|
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.
Pssm-ID: 410921 [Multi-domain] Cd Length: 235 Bit Score: 78.13 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLPIDQgggEGKALYIDTEGTFRPERLLAIAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGQQrEGLALMMQLARELKI 248
Cdd:cd19513 81 GE---DVLDNVAYARAYNTDHQMQLLIQASAMMAESR------YALLIVDSATALYRTDYSGRG-ELSARQMHLAKFLRM 150
|
170 180
....*....|....*....|....
gi 1907080609 249 LAR---DLGVAVVVTNHLTRDWDG 269
Cdd:cd19513 151 LQRladEFGVAVVITNQVVAQVDG 174
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
112-290 |
4.83e-16 |
|
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.
Pssm-ID: 410898 [Multi-domain] Cd Length: 226 Bit Score: 76.23 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 112 GEVTEIVGGPGSGKTQVCLCVAAN----------VAHSLQQNVLYVDSNGGMTASRLLQLLQAR--------------TQ 167
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARcilpsswggvPLGGLEAAVVFIDTDGRFDILRLRSILEARiraaiqaanssddeED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 168 DEEKQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEAtsSGAVKVVIVDSVTA------VVAPLLGGQQREGLALMMQ 241
Cdd:cd19490 81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSLSA--NPELGLLLIDSISAfywqdrFSAELARAAPLLQEAALRA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907080609 242 LARELKILARDLGVAVVVTNHL---TRDWDGRR--------------FKPALGRSWSFVPSTRILL 290
Cdd:cd19490 159 ILRELRRLRRRFQLVVIATKQAlfpGKSASTDNpaannavskasapsHREYLPRPWQRLVTHRLVL 224
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
94-269 |
1.07e-15 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 76.69 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:TIGR02239 78 LTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLChtLAVTCQLPIDQgggEGKALYIDTEGTFRPERLLAIAERYGLN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEKqasALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEATssgavkVVIVDSVTAVVAPLLGGQQrEGLALMMQLA---RE 245
Cdd:TIGR02239 158 PED---VLDNVAYARAYNTDHQLQLLQQAAAMMSESRFA------LLIVDSATALYRTDFSGRG-ELSARQMHLArflRS 227
|
170 180
....*....|....*....|....
gi 1907080609 246 LKILARDLGVAVVVTNHLTRDWDG 269
Cdd:TIGR02239 228 LQRLADEFGVAVVITNQVVAQVDG 251
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
79-269 |
2.09e-15 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 75.80 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 79 NGADLYEeLKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSLQQN---VLYVDSNGGM 153
Cdd:PTZ00035 86 SATEYLE-ARKNIIRITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLChtLCVTCQLPIEQGGGegkVLYIDTEGTF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 154 TASRLLQLLQARTQDEEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVV-------AP 226
Cdd:PTZ00035 165 RPERIVQIAERFGLDPE---DVLDNIAYARAYNHEHQMQLLSQAAAKMAEER------FALLIVDSATALFrvdysgrGE 235
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907080609 227 LLGGQQRegLALMMqlaRELKILARDLGVAVVVTNHLTRDWDG 269
Cdd:PTZ00035 236 LAERQQH--LGKFL---RALQKLADEFNVAVVITNQVMADVDG 273
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
94-315 |
5.42e-13 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 67.38 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLShtLCVTAQLPGSMgggGGKVAYIDTEGTFRPDRIRPIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 eekQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQqeatsSGAVKVVIVDSVTAVVAPLLGG-------QQRegLALMMq 241
Cdd:cd19514 81 ---HDAVLDNILYARAYTSEHQMELLDYVAAKFHE-----EAVFRLLIIDSIMALFRVDFSGrgelaerQQK--LAQML- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 242 lARELKIlARDLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILLdvTEGAGtlgsSQRTVCLTKSPRQP 315
Cdd:cd19514 150 -SRLQKI-SEEYNVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISL--RKGRG----EERIAKIYDSPDLP 221
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
80-290 |
3.55e-11 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 63.26 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 80 GADLYEELKTSTAIlSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSLQ---QNVLYVDSNGGMT 154
Cdd:PLN03187 95 GSDALLKRKSVVRI-TTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAhtLCVTTQLPTEMGggnGKVAYIDTEGTFR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 155 ASRLLQLLQARTQDEEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQeatssgAVKVVIVDSVTAVV-------APL 227
Cdd:PLN03187 174 PDRIVPIAERFGMDAD---AVLDNIIYARAYTYEHQYNLLLGLAAKMAEE------PFRLLIVDSVIALFrvdftgrGEL 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080609 228 LGGQQRegLALMmqLARELKIlARDLGVAVVVTNHLTRDWDGRRF-----KPALGRSWSFVPSTRILL 290
Cdd:PLN03187 245 AERQQK--LAQM--LSRLTKI-AEEFNVAVYMTNQVIADPGGGMFisdpkKPAGGHVLAHAATIRLML 307
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
94-264 |
4.75e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 61.86 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSlQQNVLYVDSNggMTASRLLQLLQARTQDEEKQA 173
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRR-GEKGLYVSFE--ESPEQLLRRAESLGLDLEEYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 174 SAlQRIQVVRSFDIFRMLD---MLQDLRGTIAQQEAtssgavKVVIVDSVTAVVapLLGGQQREGLALMMQLARELKila 250
Cdd:COG0467 79 ES-GLLRIIDLSPEELGLDleeLLARLREAVEEFGA------KRVVIDSLSGLL--LALPDPERLREFLHRLLRYLK--- 146
|
170
....*....|....
gi 1907080609 251 rDLGVAVVVTNHLT 264
Cdd:COG0467 147 -KRGVTTLLTSETG 159
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
94-315 |
2.86e-10 |
|
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.
Pssm-ID: 131292 [Multi-domain] Cd Length: 313 Bit Score: 60.56 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 168
Cdd:TIGR02238 78 ITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLShtLCVTAQLPREMgggNGKVAYIDTEGTFRPDRIRAIAERFGVD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 EEkqaSALQRIQVVRSFDIFRMLDMLQDLrgtiaqQEATSSGAVKVVIVDSVTAVVAPLLGG-----QQREGLALMMQla 243
Cdd:TIGR02238 158 PD---AVLDNILYARAYTSEHQMELLDYL------AAKFSEEPFRLLIVDSIMALFRVDFSGrgelsERQQKLAQMLS-- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 244 rELKILARDLGVAVVVTNHLTRD--------WDGRrfKPALGRSWSFVPSTRILLdvTEGAGtlgsSQRTVCLTKSPRQP 315
Cdd:TIGR02238 227 -RLNKISEEFNVAVFVTNQVQADpgatmtfiADPK--KPIGGHVLAHASTTRILL--RKGRG----EERVAKLYDSPDMP 297
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
94-266 |
4.23e-09 |
|
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.
Pssm-ID: 410866 [Multi-domain] Cd Length: 268 Bit Score: 56.39 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYV---DSNG--GMTASRllqlLQARTQD 168
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLA-QRGGKVLYVsgeESLSqiKLRAER----LGLGSDN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 169 eekqasalqrIQVVRSFDIFRMLDMLQDLRgtiaqqeatssgaVKVVIVDSVTAVVAPLLGG------QQREGLALMMQL 242
Cdd:cd01121 139 ----------LYLLAETNLEAILAEIEELK-------------PSLVVIDSIQTVYSPELTSspgsvsQVRECAAELLRL 195
|
170 180
....*....|....*....|....
gi 1907080609 243 ARElkilardLGVAVVVTNHLTRD 266
Cdd:cd01121 196 AKE-------TGIPVFLVGHVTKD 212
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
95-263 |
6.41e-08 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 53.64 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 95 STGIGSLDKLL-DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVahslQQN---VLYVDSNG----------GMTASRLLq 160
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEA----QKAggiAAFIDAEHaldpeyakklGVDIDNLL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 161 LLQARTQDeekQAsalqriqvvrsFDIfrmLDMLqdlrgtiaqqeaTSSGAVKVVIVDSVTAVV----------APLLGG 230
Cdd:COG0468 120 VSQPDTGE---QA-----------LEI---AETL------------VRSGAVDLIVVDSVAALVpkaeiegemgDSHVGL 170
|
170 180 190
....*....|....*....|....*....|...
gi 1907080609 231 QQReglaLMMQLARELKILARDLGVAVVVTNHL 263
Cdd:COG0468 171 QAR----LMSQALRKLTGAISKSNTTVIFINQL 199
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
94-270 |
6.44e-08 |
|
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 410864 [Multi-domain] Cd Length: 256 Bit Score: 52.90 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAHSLQQNVLYVDSNggMTASRLLQ-LLQARTQDEek 171
Cdd:cd00984 2 LPTGFTDLDKLT-GGLQPGDLI-IIAArPSMGKTAFALNIAENIALDEGLPVLFFSLE--MSAEQLAErLLSSESGVS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 172 qasaLQRIQVVRSFD-----IFRMLDMLQDL--------RGTIAQQEATS------SGAVKVVIVDSVTAVVAPLLGGQQ 232
Cdd:cd00984 76 ----LSKLRTGRLDDedwerLTAAMGELSELplyiddtpGLTVDEIRAKArrlkreHGGLGLIVIDYLQLIRGSKRAENR 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907080609 233 REGLAlmmQLARELKILARDLGVAVVVTNHLTRDWDGR 270
Cdd:cd00984 152 QQEVA---EISRSLKALAKELNVPVIALSQLNRGVESR 186
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
94-249 |
1.19e-07 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 51.86 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------DSNGGMTA----------S 156
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNGALKYGEPGVFVtleeppeDLRENARSfgwdlekleeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 157 RLLQLLQARTQDEEkqasalqRIQVVRSFDIFRMLDMLqdlrgtiaqQEATSSGAVKVVIVDSVTAVVAPLLGGQQREgl 236
Cdd:pfam06745 81 GKLAIIDASTSGIG-------IAEVEDRFDLEELIERL---------REAIREIGAKRVVIDSITTLFYLLKPAVARE-- 142
|
170
....*....|...
gi 1907080609 237 aLMMQLARELKIL 249
Cdd:pfam06745 143 -ILRRLKRVLKGL 154
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
117-271 |
1.73e-07 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410891 [Multi-domain] Cd Length: 231 Bit Score: 51.42 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 117 IVGGPGSGKTQVCLCVAANVAHSLQQNVLYV---DSNGgMTASRLL-----------QLLQARTQDEEKQA-SALQRIQV 181
Cdd:cd19483 3 IGAGSGIGKSTIVRELAYHLITEHGEKVGIIsleESVE-ETAKGLAgkhlgkpepleLPRDDITEEEEDDAfDNELGSGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 182 VRSFDIFRMLDMlQDLRGTIAQqeATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQlarELKILARDLGVAVVVTN 261
Cdd:cd19483 82 FFLYDHFGSLDW-DNLKEKIRY--MVKVLGCKVIVLDHLTILVSGLDSSDERKELDEIMT---ELAALVKELGVTIILVS 155
|
170
....*....|
gi 1907080609 262 HLTRDWDGRR 271
Cdd:cd19483 156 HLRRPGGGKG 165
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
94-306 |
2.91e-07 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVdsngGM--TASRLLQllQART--QDE 169
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGA-KNGEPGLFF----TFeeSPERLLR--NAKSfgWDF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 170 EKQASALqRIQVVRSFDIFRMLDMLQDLRGTIAQqeATSSGAVKVVIVDSVTAVVAPLLggQQREGLALMMQLARELkil 249
Cdd:cd01124 74 DEMEDEG-KLIIVDAPPTEAGRFSLDELLSRILS--IIKSFKAKRVVIDSLSGLRRAKE--DQMRARRIVIALLNEL--- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080609 250 aRDLGVAVVVTNHLTrdwDGRRFKPALGRSWSFVPSTRILLDVTEGAGTLgssQRTV 306
Cdd:cd01124 146 -RAAGVTTIFTSEMR---SFLSSESAGGGDVSFIVDGVILLRYVEIEGEL---RRTI 195
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
112-266 |
4.51e-07 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 49.69 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 112 GEVTEIVGGPGSGKTQVCLCVAANVA----------HSLQQNVLYVDSNGG--MTASRLLQLLQARTQDEEkqasaLQRI 179
Cdd:pfam13481 33 GGLGLLAGAPGTGKTTLALDLAAAVAtgkpwlggprVPEQGKVLYVSAEGPadELRRRLRAAGADLDLPAR-----LLFL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 180 QVVRSFDIFRMLDMLQDLRGTIAQ--QEATSSGAVKVVIVDSVTAVVAPllggqQREGLALMMQLARELKILARDLGVAV 257
Cdd:pfam13481 108 SLVESLPLFFLDRGGPLLDADVDAleAALEEVEDPDLVVIDPLARALGG-----DENSNSDVGRLVKALDRLARRTGATV 182
|
....*....
gi 1907080609 258 VVTNHLTRD 266
Cdd:pfam13481 183 LLVHHVGKD 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
111-278 |
9.29e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 111 TGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDsnggMTASRLLQLLQARTQDEEKQASALQRIQVVRsfdifRM 190
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG-PPGGGVIYID----GEDILEEVLDQLLLIIVGGKKASGSGELRLR-----LA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 191 LDMLQDLRgtiaqqeatssgaVKVVIVDSVTAvvaplLGGQQREGLALMMQLARELKILARDLGVAVVVTNHLTRDWDGR 270
Cdd:smart00382 71 LALARKLK-------------PDVLILDEITS-----LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
....*...
gi 1907080609 271 RFKPALGR 278
Cdd:smart00382 133 LLRRRFDR 140
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
94-260 |
1.41e-05 |
|
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410893 [Multi-domain] Cd Length: 226 Bit Score: 45.44 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------------DSNG----GMTAS 156
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPGVFVtfeespediiknmASFGwdlpKLVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 157 RLLQLLQARTQDEEkqasalqrIQVVRSFDIFRMLdmlqdLRGTIAQQeatSSGAVKVVIvDSVTAVVApllggqqreGL 236
Cdd:cd19485 81 GKLLILDASPEPSE--------EEVTGEYDLEALL-----IRIEYAIR---KIGAKRVSL-DSLEAVFS---------GL 134
|
170 180
....*....|....*....|....*..
gi 1907080609 237 ALMMQLARELKILA---RDLGVAVVVT 260
Cdd:cd19485 135 SDSAVVRAELLRLFawlKQKGVTAIMT 161
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
94-261 |
2.17e-05 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 44.98 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGgmtasrlLQLLQARTqdeEKQA 173
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDES-------IGTLFERS---EALG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 174 SALQRIQVVRSFDIfRMLDMLQDLRGTIAQQEATS--SGAVKVVIVDSVTAVVAPLlggqqREGLALMMQLARELKILAR 251
Cdd:cd19487 71 IDLRAMVEKGLLSI-EQIDPAELSPGEFAQRVRTSveQEDARVVVIDSLNGYLNAM-----PDERFLILQMHELLSYLNN 144
|
170
....*....|
gi 1907080609 252 dLGVAVVVTN 261
Cdd:cd19487 145 -QGVTTLLIV 153
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
94-263 |
3.50e-05 |
|
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange.
Pssm-ID: 410863 [Multi-domain] Cd Length: 235 Bit Score: 44.47 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLY-TGEVTEIVGGPGSGKTQVCLCVAANvAHSLQQNVLYVDSNGGMT---ASRL------LQLLQ 163
Cdd:cd00983 5 IPTGSLSLDIALGIGGLpRGRIIEIYGPESSGKTTLALHAIAE-AQKLGGTAAFIDAEHALDpeyAKKLgvdidnLLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 164 ARTQDEekqasalqriqvvrsfdifrMLDMLQDLrgtiaqqeaTSSGAVKVVIVDSVTAVV--APLLG--GQQREGL--A 237
Cdd:cd00983 84 PDTGEQ--------------------ALEIADTL---------IRSGAVDLIVVDSVAALVpkAEIEGemGDSHVGLqaR 134
|
170 180
....*....|....*....|....*.
gi 1907080609 238 LMMQLARELKILARDLGVAVVVTNHL 263
Cdd:cd00983 135 LMSQALRKLTGSLSKSKTTVIFINQL 160
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
94-260 |
4.96e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.79 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------------DSNG----GMTAS 156
Cdd:PRK09302 13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQFLVNGIKRFDEPGVFVtfeespediirnvASFGwdlqKLIDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 157 RLLQLLQARTQDEEkqasalqrIQVVRSFDIFRMLDMLQDlrgtiAQQeatSSGAVKVVIvDSVTAVVApllggqqreGL 236
Cdd:PRK09302 93 GKLFILDASPDPSE--------QEEAGEYDLEALFIRIEY-----AID---KIGAKRVVL-DSIEALFS---------GF 146
|
170 180
....*....|....*....|....*..
gi 1907080609 237 ALMMQLARELKILA---RDLGVAVVVT 260
Cdd:PRK09302 147 SNEAVVRRELRRLFawlKQKGVTAVIT 173
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
94-270 |
8.93e-04 |
|
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 427509 [Multi-domain] Cd Length: 254 Bit Score: 40.48 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 94 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAHSLQQNVLYV--DsnggMTASRLLQ-LLqartqde 169
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLI-IIAArPSMGKTAFALNIARNAAVKHKKPVAIFslE----MSAEQLVMrLL------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 170 ekqaSALQRIQvvrsfdifrmldmLQDLR-GTIAQQE----ATSSGAV---KVVIVD----SVTAVVAPLLGGQQREGLA 237
Cdd:pfam03796 69 ----ASEAGVD-------------SQKLRtGQLTDEDweklAKAAGRLseaPLYIDDtpglSIAEIRAKARRLKREHGLG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907080609 238 LMM----QL-----------------ARELKILARDLGVAVVVTNHLTRDWDGR 270
Cdd:pfam03796 132 LIVidylQLmsggsrgenrqqeiseiSRSLKALAKELNVPVIALSQLSRAVEQR 185
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
112-298 |
1.11e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 40.06 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 112 GEVTEIVGGPGSGKTQVCLCVAANVA--------HSLQQ-NVLYVDSNGGmtASRLLQLLQARTQDEEKQASALQRIQVV 182
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVAtgrdwlgeRRVKQgRVVYLAAEDP--RDGLRRRLKAIGAHLGDEDAALAENLVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 183 RSFDIFRMLDmlqDLRGTIAQQEATSSGAVKVVIVDSVTAVvaplLGGQQREGLALMMQLARELKILARDLGVAVVVTNH 262
Cdd:cd01125 79 ENLRGKPVSI---DAEAPELERIIEELEGVRLIIIDTLARV----LHGGDENDAADMGAFVAGLDRIARETGAAVLLVHH 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907080609 263 LTRDWDGRRFKPALGRSwSFVPSTRILLDVTEGAGT 298
Cdd:cd01125 152 TGKDAAGDSQQAARGSS-ALRGAADAEINLSKMDAT 186
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
73-126 |
1.45e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 40.25 E-value: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907080609 73 FSAFPLNGADLyeELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKT 126
Cdd:PRK09302 236 ISVLPLTAMRL--TQRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKT 287
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
117-277 |
6.91e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 37.31 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 117 IVGGPGSGKTQVCLCVaanvahslqQNVLYVDSNGGMTasrllqllqartqdeekqasalqRIQVVRsFDIFRMLDMLQD 196
Cdd:pfam13479 7 IYGPSGIGKTTFAKTL---------PKPLFLDTEKGSK-----------------------ALDGDR-FPDIVIRDSWQD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080609 197 LRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLG--------GQQREGL-------ALMMQLARELKILaRDLGVAVVVTN 261
Cdd:pfam13479 54 FLDAIDELTAAELADYKTIVIDTVDWLERLCLAyickqngkGSSIEDGgygkgygELGEEFRRLLDAL-QELGKNVIFTA 132
|
170 180
....*....|....*....|...
gi 1907080609 262 HLTRDWDGR-------RFKPALG 277
Cdd:pfam13479 133 HAKTRKDEDpdgekytRYEPKLG 155
|
|
| |
