|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
94-299 |
3.63e-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: 262.19 E-value: 3.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 94 DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSF 173
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 174 DIFRMLDMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQQR-EGLALMMQLARELKILARDLGVAVVVTNHLT 252
Cdd:cd19489 81 DPYELLDLLEELRNTLSQQQENLYSRLKLVIIDSLSALISPLLGGSKHsEGHALLASLARLLKKLAAEYQIAVLVTNLTV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 485464612 253 RDWDGRRF---KPALGRSWSFVPSTRILLDVTEGAGTlGSSQRTVCLTKS 299
Cdd:cd19489 161 RGGDGGQQgstKPALGEYWESVPSTRLLLSRDENDPE-ESGVCTATLLKS 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
100-279 |
1.87e-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: 154.82 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 100 GEVTEIVGGPGSGKTQVCLCVAANVAHsLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKQASALQRIQVVRSFDifrml 179
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALL-LGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYFRPPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 180 DMLQDLRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLGGQ------QREGLALMMQLARELKILARDLGVAVVVTNHLTR 253
Cdd:cd01393 75 TLAHLLALDSLPESLFPPPNTSLVVVDSVSALFRKAFPRGgdgdssSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTT 154
|
170 180 190
....*....|....*....|....*....|
gi 485464612 254 DWDGR----RFKPALGRSWSFVPSTRILLD 279
Cdd:cd01393 155 KIRGGsgasLVPPALGNTWEHSVSTRLLLY 184
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
90-300 |
1.26e-28 |
|
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: 109.72 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 90 DKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----HSLQQNVLYVDSNGGMTASRLLQLLQART--------QD 156
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkGGLDGGVLYIDTESKFSAERLAEIAEARFpeafsgfmEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 EEKQASALQRIQVVRSFDIFRMLDMLQDLRgtiaqqEATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARE--- 233
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLE------EHILSSGVRLVVIDSIAALVRREFGGSDGEVTERHNALAREass 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485464612 234 LKILARDLGVAVVVTNHL-TRDWDGRRF----KPALGRSWSFVPSTRILLDVtegagTLGSSQRTVCLTKSP 300
Cdd:cd19493 155 LKRLAEEFRIAVLVTNQAtTHFGDAGDGssgvTAALGDAWAHAVNTRLRLER-----CLLQLRRVLEIVKSP 221
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
10-249 |
1.85e-25 |
|
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: 103.28 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 10 PGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLS----YKALVALRRvlLAQFSAFPlNGADLYEELKTSTAIlSTG 85
Cdd:TIGR02236 5 PGVGPATAEKLREAGYDTFEAIAVASPKELSEIAGISegtaAKIIQAARK--AADLGGFE-TADDVLERRKTIGKI-TTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 86 IGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAH-----SLQQNVLYVDSNGGMTASRLLQLLQARTQDEEKq 160
Cdd:TIGR02236 81 SKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLpeekgGLGGKAVYIDTENTFRPERIMQMAEARGLDPDE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 161 asALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssGAVKVVIVDSVTAVV-APLLGgqqREGLALMMQ-LARELKILA 238
Cdd:TIGR02236 160 --VLKNIYVARAYNSNHQMLLVEKAEDLIKELN----NPVKLLIVDSLTSHFrAEYVG---RGALAERQQkLNKHLHDLL 230
|
250
....*....|....
gi 485464612 239 R--DL-GVAVVVTN 249
Cdd:TIGR02236 231 RlaDLyNAAVVVTN 244
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
100-300 |
7.52e-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: 98.07 E-value: 7.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 100 GEVTEIVGGPGSGKTQVCLCVAANV-----AHSLQQNVLYVDSNGgmtasrllqllqartqdeekqasalqriqvvrSFD 174
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVqipkcFGGLAGEAIYIDTEG--------------------------------SFN 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 175 I--FRMLDMLQdLRGTIAQQEA--TSSGAVKVVIVDSVTAvvaPLLGGQQREGL--ALMMQLARELKILARDLGVAVVVT 248
Cdd:cd19492 49 IhyFRVHDYVE-LLALINSLPKflEDHPKVKLIVVDSIAF---PFRHDFDDLAQrtRLLNGLAQLLHSLARQHNLAVVLT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 485464612 249 NHLT---RDWDGRRFKPALGRSWSFVPSTRILLdvtegagTLGSSQRTVCLTKSP 300
Cdd:cd19492 125 NQVTtkiSEDGQSQLVPALGESWSHACTTRLFL-------TWDEKQRFAHLYKSP 172
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
10-249 |
2.18e-23 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 97.64 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 10 PGLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSYKA----LVALRRVL-LAQFSAfplnGADLYEELKtSTAILST 84
Cdd:PRK04301 12 PGVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTaakiIEAAREAAdIGGFET----ALEVLERRK-NVGKITT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 85 GIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANV-----AHSLQQNVLYVDSNGGMTASRLLQLLQARTQDEEK 159
Cdd:PRK04301 87 GSKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVqlpeeKGGLEGKAVYIDTEGTFRPERIEQMAEALGLDPDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 160 qasALQRIQVVRSFDI---FRMLDMLQDLrgtIAQQEatssgAVKVVIVDSVTAVV-APLLGgqqREGLA-----LMMQL 230
Cdd:PRK04301 167 ---VLDNIHVARAYNSdhqMLLAEKAEEL---IKEGE-----NIKLVIVDSLTAHFrAEYVG---RGNLAerqqkLNKHL 232
|
250
....*....|....*....
gi 485464612 231 ARELKiLARDLGVAVVVTN 249
Cdd:PRK04301 233 HDLLR-LADLYNAAVVVTN 250
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
82-269 |
1.18e-22 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 93.77 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDSNgGMTASRLLQLLqartqdEEKQA 161
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAA-KNGKKVIYIDTE-GLSPERFKQIA------GEDFE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 162 SALQRIQVVRSFDiFRMLDM-LQDLRGTIAQQeatssgaVKVVIVDSVTAVVApLLGGQQREGLALMMQLARELKIL--- 237
Cdd:PRK09361 77 ELLSNIIIFEPSS-FEEQSEaIRKAEKLAKEN-------VGLIVLDSATSLYR-LELEDEEDNSKLNRELGRQLTHLlkl 147
|
170 180 190
....*....|....*....|....*....|....*
gi 485464612 238 ARDLGVAVVVTNHLTRDWDGRRFKPALGRS---WS 269
Cdd:PRK09361 148 ARKHDLAVVITNQVYSDIDSDGLRPLGGHTlehWS 182
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
82-262 |
2.29e-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: 92.76 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDSNgGMTASRLLQLLQARTQdeekqa 161
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAA-KQGKKVVYIDTE-GLSPERFQQIAGERFE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 162 SALQRIQVVRSFDIFRMLDMLQDLRGTIaqqeatSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQLARELKIlARDL 241
Cdd:cd01394 73 SIASNIIVFEPYSFDEQGVAIQEAEKLL------KSDKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLSI-ARKY 145
|
170 180
....*....|....*....|.
gi 485464612 242 GVAVVVTNHLTRDWDGRRFKP 262
Cdd:cd01394 146 DIPVVITNQVYSDIDDDRLKP 166
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
82-278 |
5.78e-22 |
|
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: 92.36 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:pfam08423 19 ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLChtLCVTCQLPLEMgggEGKALYIDTEGTFRPERLVAIAERYGLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGqqREGLAL-MMQLARELK 235
Cdd:pfam08423 99 PE---DVLDNVAYARAYNSEHQMQLLQQAAAMMSESR------FALLIVDSATALYRTDFSG--RGELAErQQHLAKFLR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 485464612 236 ILAR---DLGVAVVVTNHLTRDWDGRR--F-----KPALGRSWSFVPSTRILL 278
Cdd:pfam08423 168 TLQRladEFGVAVVITNQVVAQVDGAAgmFsgdpkKPIGGHIMAHASTTRLSL 220
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
89-300 |
5.02e-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: 89.66 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 89 LDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHS---LQQNVLYVDSNGGMTASRLLQLLQ--ARTQDEEKQA 161
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLClqLALTVQLPRElggLGGGAVYICTESSFPSKRLQQLASslPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 162 SALQRIQVVRSFDifrmldmLQDLRGTIAQQ--EATSSGAVKVVIVDSVTAVV-----APLLGGQQREglALMMQLAREL 234
Cdd:cd19491 81 NFLDNIFVEHVAD-------LETLEHCLNYQlpALLERGPIRLVVIDSIAALFrsefdTSRSDLVERA--KYLRRLADHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 235 KILARDLGVAVVVTNHLTRDWD-------------------------GRRFKPALGRSWSFVPSTRILLDVTEGAGTLGS 289
Cdd:cd19491 152 KRLADKYNLAVVVVNQVTDRFDsssdasglgvldylsqfssfsggvsGNRKVPALGLTWANLVNTRLMLSRTPKRITDSS 231
|
250
....*....|....*
gi 485464612 290 SQ----RTVCLTKSP 300
Cdd:cd19491 232 AAsisvRRLEVVFSP 246
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
82-278 |
4.81e-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: 86.65 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----HSLQQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQlppeeGGLNGKAVYIDTENTFRPERIMQMAKALGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 EEKqasALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgAVKVVIVDSVTAVV-APLLGgqqREGLALMMQ-LAREL 234
Cdd:cd19515 81 PDE---VLDNIYVARAYNSNHQMLLVEKAEDLIKEGN-----NIKLLIVDSLTSHFrAEYVG---RGTLAERQQkLNKHL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 485464612 235 KILAR--DL-GVAVVVTNHLTRDWD---GRRFKPALGRSWSFVPSTRILL 278
Cdd:cd19515 150 HDLHRlaDLyNIAVLVTNQVMAKPDaffGDPTQAIGGHILGHAATFRVYL 199
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
11-278 |
2.23e-19 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 86.71 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 11 GLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLS-YKALvalrRVLLAQFSAFPL---NGADLYEElKTSTAILSTGI 86
Cdd:PLN03186 35 GIAALDIKKLKDAGIHTVESLAYAPKKDLLQIKGISeAKVE----KILEAASKLVPLgftTASQLHAQ-RQEIIQITTGS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 87 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVahSLQQ-----NVLYVDSNGGMTASRLLQLLQARTQDeek 159
Cdd:PLN03186 110 RELDKILEGGIETGSITEIYGEFRTGKTQLChtLCVTCQL--PLDQgggegKAMYIDTEGTFRPQRLIQIAERFGLN--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 160 QASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGQQrEGLALMMQLARELKILAR 239
Cdd:PLN03186 185 GADVLENVAYARAYNTDHQSELLLEAASMMAETR------FALMIVDSATALYRTEFSGRG-ELSARQMHLGKFLRSLQR 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 485464612 240 ---DLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILL 278
Cdd:PLN03186 258 ladEFGVAVVITNQVVAQVDGSAFfagpqlKPIGGNIMAHASTTRLAL 305
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
82-278 |
4.45e-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: 81.42 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHS---LQQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLChtLAVTCQLPIDrggGEGKAIYIDTEGTFRPERLRAIAQRFGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGQQrEGLALMMQLARELKI 236
Cdd:cd01123 81 PD---DVLDNVAYARAFNSDHQTQLLDQAAAMMVESR------FKLLIVDSATALYRTDYSGRG-ELSARQMHLAKFLRM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 485464612 237 LAR---DLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILL 278
Cdd:cd01123 151 LQRladEFGVAVVVTNQVVAQVDGAMMfaadpkKPIGGNILAHASTTRLYL 201
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
82-257 |
6.34e-17 |
|
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: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLPIDQgggEGKALYIDTEGTFRPERLLAIAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVVAPLLGGQQrEGLALMMQLARELKI 236
Cdd:cd19513 81 GE---DVLDNVAYARAYNTDHQMQLLIQASAMMAESR------YALLIVDSATALYRTDYSGRG-ELSARQMHLAKFLRM 150
|
170 180
....*....|....*....|....
gi 485464612 237 LAR---DLGVAVVVTNHLTRDWDG 257
Cdd:cd19513 151 LQRladEFGVAVVITNQVVAQVDG 174
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
11-257 |
9.48e-17 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 79.27 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 11 GLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLSY----KALVALRRVLLAQFsafpLNGADLYEeLKTSTAILSTGI 86
Cdd:PTZ00035 30 GINAADIKKLKEAGICTVESVAYATKKDLCNIKGISEakveKIKEAASKLVPMGF----ISATEYLE-ARKNIIRITTGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 87 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSLQQN---VLYVDSNGGMTASRLLQLLQARTQDEEkqa 161
Cdd:PTZ00035 105 TQLDKLLGGGIETGSITELFGEFRTGKTQLChtLCVTCQLPIEQGGGegkVLYIDTEGTFRPERIVQIAERFGLDPE--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 162 SALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEatssgaVKVVIVDSVTAVV-------APLLGGQQRegLALMMqlaREL 234
Cdd:PTZ00035 182 DVLDNIAYARAYNHEHQMQLLSQAAAKMAEER------FALLIVDSATALFrvdysgrGELAERQQH--LGKFL---RAL 250
|
250 260
....*....|....*....|...
gi 485464612 235 KILARDLGVAVVVTNHLTRDWDG 257
Cdd:PTZ00035 251 QKLADEFNVAVVITNQVMADVDG 273
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
11-257 |
3.77e-16 |
|
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: 77.46 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 11 GLTEETVQLLRGRKIKTVADLAAADLEEVAQKCGLS-YKAlvalRRVLLAQFSAFPLN--GADLYEELKTSTAILSTGIG 87
Cdd:TIGR02239 8 GITAADIKKLQEAGLHTVESVAYAPKKQLLEIKGISeAKA----DKILAEAAKLVPMGftTATEFHQRRQEVIQLTTGSK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 88 SLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQDEEKqas 162
Cdd:TIGR02239 84 ELDKLLGGGIETGSITEIFGEFRTGKTQLChtLAVTCQLPIDQgggEGKALYIDTEGTFRPERLLAIAERYGLNPED--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 163 ALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEATssgavkVVIVDSVTAVVAPLLGGQQrEGLALMMQLA---RELKILAR 239
Cdd:TIGR02239 161 VLDNVAYARAYNTDHQLQLLQQAAAMMSESRFA------LLIVDSATALYRTDFSGRG-ELSARQMHLArflRSLQRLAD 233
|
250
....*....|....*...
gi 485464612 240 DLGVAVVVTNHLTRDWDG 257
Cdd:TIGR02239 234 EFGVAVVITNQVVAQVDG 251
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
100-278 |
8.76e-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: 74.69 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 100 GEVTEIVGGPGSGKTQVCLCVAAN----------VAHSLQQNVLYVDSNGGMTASRLLQLLQAR--------------TQ 155
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARcilpsswggvPLGGLEAAVVFIDTDGRFDILRLRSILEARiraaiqaanssddeED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 156 DEEKQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQQEAtsSGAVKVVIVDSVTA------VVAPLLGGQQREGLALMMQ 229
Cdd:cd19490 81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSLSA--NPELGLLLIDSISAfywqdrFSAELARAAPLLQEAALRA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485464612 230 LARELKILARDLGVAVVVTNHL---TRDWDGRR--------------FKPALGRSWSFVPSTRILL 278
Cdd:cd19490 159 ILRELRRLRRRFQLVVIATKQAlfpGKSASTDNpaannavskasapsHREYLPRPWQRLVTHRLVL 224
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
82-278 |
6.42e-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: 67.00 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLShtLCVTAQLPGSMgggGGKVAYIDTEGTFRPDRIRPIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 eekQASALQRIQVVRSFDIFRMLDMLQDLRGTIAQqeatsSGAVKVVIVDSVTAVVAPLLGG-------QQRegLALMMq 229
Cdd:cd19514 81 ---HDAVLDNILYARAYTSEHQMELLDYVAAKFHE-----EAVFRLLIIDSIMALFRVDFSGrgelaerQQK--LAQML- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 485464612 230 lARELKIlARDLGVAVVVTNHLTRDWDGRRF------KPALGRSWSFVPSTRILL 278
Cdd:cd19514 150 -SRLQKI-SEEYNVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISL 202
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
68-278 |
2.64e-11 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 63.26 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 68 GADLYEELKTSTAIlSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSLQ---QNVLYVDSNGGMT 142
Cdd:PLN03187 95 GSDALLKRKSVVRI-TTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAhtLCVTTQLPTEMGggnGKVAYIDTEGTFR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 143 ASRLLQLLQARTQDEEkqaSALQRIQVVRSFDIFRMLDMLQDLRGTIAQQeatssgAVKVVIVDSVTAVV-------APL 215
Cdd:PLN03187 174 PDRIVPIAERFGMDAD---AVLDNIIYARAYTYEHQYNLLLGLAAKMAEE------PFRLLIVDSVIALFrvdftgrGEL 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485464612 216 LGGQQRegLALMmqLARELKIlARDLGVAVVVTNHLTRDWDGRRF-----KPALGRSWSFVPSTRILL 278
Cdd:PLN03187 245 AERQQK--LAQM--LSRLTKI-AEEFNVAVYMTNQVIADPGGGMFisdpkKPAGGHVLAHAATIRLML 307
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
82-252 |
6.27e-11 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 61.08 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSlQQNVLYVDSNggMTASRLLQLLQARTQDEEKQA 161
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRR-GEKGLYVSFE--ESPEQLLRRAESLGLDLEEYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 162 SAlQRIQVVRSFDIFRMLD---MLQDLRGTIAQQEAtssgavKVVIVDSVTAVVapLLGGQQREGLALMMQLARELKila 238
Cdd:COG0467 79 ES-GLLRIIDLSPEELGLDleeLLARLREAVEEFGA------KRVVIDSLSGLL--LALPDPERLREFLHRLLRYLK--- 146
|
170
....*....|....
gi 485464612 239 rDLGVAVVVTNHLT 252
Cdd:COG0467 147 -KRGVTTLLTSETG 159
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
82-278 |
2.52e-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: 60.18 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAHSL---QQNVLYVDSNGGMTASRLLQLLQARTQD 156
Cdd:TIGR02238 78 ITTGSQALDGILGGGIESMSITEVFGEFRCGKTQLShtLCVTAQLPREMgggNGKVAYIDTEGTFRPDRIRAIAERFGVD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 EEkqaSALQRIQVVRSFDIFRMLDMLQDLrgtiaqQEATSSGAVKVVIVDSVTAVVAPLLGG-------QQRegLALMMQ 229
Cdd:TIGR02238 158 PD---AVLDNILYARAYTSEHQMELLDYL------AAKFSEEPFRLLIVDSIMALFRVDFSGrgelserQQK--LAQMLS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 485464612 230 larELKILARDLGVAVVVTNHLTRD--------WDGRrfKPALGRSWSFVPSTRILL 278
Cdd:TIGR02238 227 ---RLNKISEEFNVAVFVTNQVQADpgatmtfiADPK--KPIGGHVLAHASTTRILL 278
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
82-254 |
3.02e-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: 56.77 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYV---DSNG--GMTASRllqlLQARTQD 156
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLA-QRGGKVLYVsgeESLSqiKLRAER----LGLGSDN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 157 eekqasalqrIQVVRSFDIFRMLDMLQDLRgtiaqqeatssgaVKVVIVDSVTAVVAPLLGG------QQREGLALMMQL 230
Cdd:cd01121 139 ----------LYLLAETNLEAILAEIEELK-------------PSLVVIDSIQTVYSPELTSspgsvsQVRECAAELLRL 195
|
170 180
....*....|....*....|....
gi 485464612 231 ARElkilardLGVAVVVTNHLTRD 254
Cdd:cd01121 196 AKE-------TGIPVFLVGHVTKD 212
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
83-251 |
3.92e-08 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 54.02 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 83 STGIGSLDKLL-DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVahslQQN---VLYVDSNG----------GMTASRLLq 148
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEA----QKAggiAAFIDAEHaldpeyakklGVDIDNLL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 149 LLQARTQDeekQAsalqriqvvrsFDIfrmLDMLqdlrgtiaqqeaTSSGAVKVVIVDSVTAVV----------APLLGG 218
Cdd:COG0468 120 VSQPDTGE---QA-----------LEI---AETL------------VRSGAVDLIVVDSVAALVpkaeiegemgDSHVGL 170
|
170 180 190
....*....|....*....|....*....|...
gi 485464612 219 QQReglaLMMQLARELKILARDLGVAVVVTNHL 251
Cdd:COG0468 171 QAR----LMSQALRKLTGAISKSNTTVIFINQL 199
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
82-258 |
6.65e-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: 52.51 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAHSLQQNVLYVDSNggMTASRLLQ-LLQARTQDEek 159
Cdd:cd00984 2 LPTGFTDLDKLT-GGLQPGDLI-IIAArPSMGKTAFALNIAENIALDEGLPVLFFSLE--MSAEQLAErLLSSESGVS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 160 qasaLQRIQVVRSFD-----IFRMLDMLQDL--------RGTIAQQEATS------SGAVKVVIVDSVTAVVAPLLGGQQ 220
Cdd:cd00984 76 ----LSKLRTGRLDDedwerLTAAMGELSELplyiddtpGLTVDEIRAKArrlkreHGGLGLIVIDYLQLIRGSKRAENR 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 485464612 221 REGLAlmmQLARELKILARDLGVAVVVTNHLTRDWDGR 258
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 ... |
82-237 |
9.76e-08 |
|
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: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------DSNGGMTA----------S 144
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNGALKYGEPGVFVtleeppeDLRENARSfgwdlekleeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 145 RLLQLLQARTQDEEkqasalqRIQVVRSFDIFRMLDMLqdlrgtiaqQEATSSGAVKVVIVDSVTAVVAPLLGGQQREgl 224
Cdd:pfam06745 81 GKLAIIDASTSGIG-------IAEVEDRFDLEELIERL---------REAIREIGAKRVVIDSITTLFYLLKPAVARE-- 142
|
170
....*....|...
gi 485464612 225 aLMMQLARELKIL 237
Cdd:pfam06745 143 -ILRRLKRVLKGL 154
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
105-259 |
1.43e-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: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 105 IVGGPGSGKTQVCLCVAANVAHSLQQNVLYV---DSNGgMTASRLL-----------QLLQARTQDEEKQA-SALQRIQV 169
Cdd:cd19483 3 IGAGSGIGKSTIVRELAYHLITEHGEKVGIIsleESVE-ETAKGLAgkhlgkpepleLPRDDITEEEEDDAfDNELGSGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 170 VRSFDIFRMLDMlQDLRGTIAQqeATSSGAVKVVIVDSVTAVVAPLLGGQQREGLALMMQlarELKILARDLGVAVVVTN 249
Cdd:cd19483 82 FFLYDHFGSLDW-DNLKEKIRY--MVKVLGCKVIVLDHLTILVSGLDSSDERKELDEIMT---ELAALVKELGVTIILVS 155
|
170
....*....|
gi 485464612 250 HLTRDWDGRR 259
Cdd:cd19483 156 HLRRPGGGKG 165
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
82-294 |
3.02e-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: 50.34 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVdsngGM--TASRLLQllQART--QDE 157
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGA-KNGEPGLFF----TFeeSPERLLR--NAKSfgWDF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 158 EKQASALqRIQVVRSFDIFRMLDMLQDLRGTIAQqeATSSGAVKVVIVDSVTAVVAPLLggQQREGLALMMQLARELkil 237
Cdd:cd01124 74 DEMEDEG-KLIIVDAPPTEAGRFSLDELLSRILS--IIKSFKAKRVVIDSLSGLRRAKE--DQMRARRIVIALLNEL--- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 485464612 238 aRDLGVAVVVTNHLTrdwDGRRFKPALGRSWSFVPSTRILLDVTEGAGTLgssQRTV 294
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. |
100-254 |
5.71e-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: 48.92 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 100 GEVTEIVGGPGSGKTQVCLCVAANVA----------HSLQQNVLYVDSNGG--MTASRLLQLLQARTQDEEkqasaLQRI 167
Cdd:pfam13481 33 GGLGLLAGAPGTGKTTLALDLAAAVAtgkpwlggprVPEQGKVLYVSAEGPadELRRRLRAAGADLDLPAR-----LLFL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 168 QVVRSFDIFRMLDMLQDLRGTIAQ--QEATSSGAVKVVIVDSVTAVVAPllggqQREGLALMMQLARELKILARDLGVAV 245
Cdd:pfam13481 108 SLVESLPLFFLDRGGPLLDADVDAleAALEEVEDPDLVVIDPLARALGG-----DENSNSDVGRLVKALDRLARRTGATV 182
|
....*....
gi 485464612 246 VVTNHLTRD 254
Cdd:pfam13481 183 LLVHHVGKD 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-266 |
1.71e-06 |
|
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: 46.98 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 99 TGEVTEIVGGPGSGKTQVCLCVAANVAhSLQQNVLYVDsnggMTASRLLQLLQARTQDEEKQASALQRIQVVRsfdifRM 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG-PPGGGVIYID----GEDILEEVLDQLLLIIVGGKKASGSGELRLR-----LA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 179 LDMLQDLRgtiaqqeatssgaVKVVIVDSVTAvvaplLGGQQREGLALMMQLARELKILARDLGVAVVVTNHLTRDWDGR 258
Cdd:smart00382 71 LALARKLK-------------PDVLILDEITS-----LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
....*...
gi 485464612 259 RFKPALGR 266
Cdd:smart00382 133 LLRRRFDR 140
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
82-248 |
1.19e-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: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------------DSNG----GMTAS 144
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPGVFVtfeespediiknmASFGwdlpKLVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 145 RLLQLLQARTQDEEkqasalqrIQVVRSFDIFRMLdmlqdLRGTIAQQeatSSGAVKVVIvDSVTAVVApllggqqreGL 224
Cdd:cd19485 81 GKLLILDASPEPSE--------EEVTGEYDLEALL-----IRIEYAIR---KIGAKRVSL-DSLEAVFS---------GL 134
|
170 180
....*....|....*....|....*..
gi 485464612 225 ALMMQLARELKILA---RDLGVAVVVT 248
Cdd:cd19485 135 SDSAVVRAELLRLFawlKQKGVTAIMT 161
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
82-249 |
1.87e-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: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYVDSNGgmtasrlLQLLQARTqdeEKQA 161
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDES-------IGTLFERS---EALG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 162 SALQRIQVVRSFDIfRMLDMLQDLRGTIAQQEATS--SGAVKVVIVDSVTAVVAPLlggqqREGLALMMQLARELKILAR 239
Cdd:cd19487 71 IDLRAMVEKGLLSI-EQIDPAELSPGEFAQRVRTSveQEDARVVVIDSLNGYLNAM-----PDERFLILQMHELLSYLNN 144
|
170
....*....|
gi 485464612 240 dLGVAVVVTN 249
Cdd:cd19487 145 -QGVTTLLIV 153
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
82-251 |
2.17e-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: 44.85 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLY-TGEVTEIVGGPGSGKTQVCLCVAANvAHSLQQNVLYVDSNGGMT---ASRL------LQLLQ 151
Cdd:cd00983 5 IPTGSLSLDIALGIGGLpRGRIIEIYGPESSGKTTLALHAIAE-AQKLGGTAAFIDAEHALDpeyAKKLgvdidnLLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 152 ARTQDEekqasalqriqvvrsfdifrMLDMLQDLrgtiaqqeaTSSGAVKVVIVDSVTAVV--APLLG--GQQREGL--A 225
Cdd:cd00983 84 PDTGEQ--------------------ALEIADTL---------IRSGAVDLIVVDSVAALVpkAEIEGemGDSHVGLqaR 134
|
170 180
....*....|....*....|....*.
gi 485464612 226 LMMQLARELKILARDLGVAVVVTNHL 251
Cdd:cd00983 135 LMSQALRKLTGSLSKSKTTVIFINQL 160
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
82-248 |
4.18e-04 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 41.79 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAHSLQQNVLYV-------------DSNG----GMTAS 144
Cdd:PRK09302 13 LPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQFLVNGIKRFDEPGVFVtfeespediirnvASFGwdlqKLIDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 145 RLLQLLQARTQDEEkqasalqrIQVVRSFDIFRMLDMLQDlrgtiAQQeatSSGAVKVVIvDSVTAVVApllggqqreGL 224
Cdd:PRK09302 93 GKLFILDASPDPSE--------QEEAGEYDLEALFIRIEY-----AID---KIGAKRVVL-DSIEALFS---------GF 146
|
170 180
....*....|....*....|....*..
gi 485464612 225 ALMMQLARELKILA---RDLGVAVVVT 248
Cdd:PRK09302 147 SNEAVVRRELRRLFawlKQKGVTAVIT 173
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
82-258 |
9.28e-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: 40.09 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 82 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAHSLQQNVLYV--DsnggMTASRLLQ-LLqartqde 157
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLI-IIAArPSMGKTAFALNIARNAAVKHKKPVAIFslE----MSAEQLVMrLL------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 158 ekqaSALQRIQvvrsfdifrmldmLQDLR-GTIAQQE----ATSSGAV---KVVIVD----SVTAVVAPLLGGQQREGLA 225
Cdd:pfam03796 69 ----ASEAGVD-------------SQKLRtGQLTDEDweklAKAAGRLseaPLYIDDtpglSIAEIRAKARRLKREHGLG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 485464612 226 LMM----QL-----------------ARELKILARDLGVAVVVTNHLTRDWDGR 258
Cdd:pfam03796 132 LIVidylQLmsggsrgenrqqeiseiSRSLKALAKELNVPVIALSQLSRAVEQR 185
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
61-114 |
1.23e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 40.25 E-value: 1.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 485464612 61 FSAFPLNGADLyeELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKT 114
Cdd:PRK09302 236 ISVLPLTAMRL--TQRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKT 287
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
100-286 |
1.36e-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: 39.29 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 100 GEVTEIVGGPGSGKTQVCLCVAANVA--------HSLQQ-NVLYVDSNGGmtASRLLQLLQARTQDEEKQASALQRIQVV 170
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVAtgrdwlgeRRVKQgRVVYLAAEDP--RDGLRRRLKAIGAHLGDEDAALAENLVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 171 RSFDIFRMLDmlqDLRGTIAQQEATSSGAVKVVIVDSVTAVvaplLGGQQREGLALMMQLARELKILARDLGVAVVVTNH 250
Cdd:cd01125 79 ENLRGKPVSI---DAEAPELERIIEELEGVRLIIIDTLARV----LHGGDENDAADMGAFVAGLDRIARETGAAVLLVHH 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 485464612 251 LTRDWDGRRFKPALGRSwSFVPSTRILLDVTEGAGT 286
Cdd:cd01125 152 TGKDAAGDSQQAARGSS-ALRGAADAEINLSKMDAT 186
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
105-265 |
5.94e-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: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 105 IVGGPGSGKTQVCLCVaanvahslqQNVLYVDSNGGMTasrllqllqartqdeekqasalqRIQVVRsFDIFRMLDMLQD 184
Cdd:pfam13479 7 IYGPSGIGKTTFAKTL---------PKPLFLDTEKGSK-----------------------ALDGDR-FPDIVIRDSWQD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485464612 185 LRGTIAQQEATSSGAVKVVIVDSVTAVVAPLLG--------GQQREGL-------ALMMQLARELKILaRDLGVAVVVTN 249
Cdd:pfam13479 54 FLDAIDELTAAELADYKTIVIDTVDWLERLCLAyickqngkGSSIEDGgygkgygELGEEFRRLLDAL-QELGKNVIFTA 132
|
170 180
....*....|....*....|...
gi 485464612 250 HLTRDWDGR-------RFKPALG 265
Cdd:pfam13479 133 HAKTRKDEDpdgekytRYEPKLG 155
|
|
| |
