|
Name |
Accession |
Description |
Interval |
E-value |
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
94-298 |
3.51e-93 |
|
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: 275.67 E-value: 3.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 94 DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAYGLQQNVVYIDSNGGLTASRILQLLQARTPDEEVQAGALQRIQVVRAF 173
Cdd:cd19489 1 GGGLRTGEITELVGESSSGKTQLCLTAAANVASRSGQNVLYIDTKSSFSARRLAQILKSRAQDAEEIDKALQRIRVVRVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 174 DIFQMLDVLQDCRGTLSQQVSSASGTVKVVIVDSVTAVVSPLLGGQQR-EGLALMMQLARELKTLARDLGMAVVVTNHMT 252
Cdd:cd19489 81 DPYELLDLLEELRNTLSQQQENLYSRLKLVIIDSLSALISPLLGGSKHsEGHALLASLARLLKKLAAEYQIAVLVTNLTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953097357 253 RDRDSG---ELKPALGRSWSFVPSTRILLDIDEGARASGSWRRACLTKS 298
Cdd:cd19489 161 RGGDGGqqgSTKPALGEYWESVPSTRLLLSRDENDPEESGVCTATLLKS 209
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
100-279 |
8.80e-49 |
|
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: 161.37 E-value: 8.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 100 GEVTEIVGGPGSGKTQVCLCVAANVAyGLQQNVVYIDSNGGLTASRILQLLQARTPDEEVQAGALQRIQVVRAFDIFQML 179
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANAL-LLGGGVVWIDTEGAFPPSRLVQILEASPSSELELAEALSRLLYFRPPDTLAHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 180 DVLqdcrgTLSQQVSSASGTVKVVIVDSVTAVVSPLLGGQ------QREGLALMMQLARELKTLARDLGMAVVVTNHMTR 253
Cdd:cd01393 80 LAL-----DSLPESLFPPPNTSLVVVDSVSALFRKAFPRGgdgdssSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTT 154
|
170 180 190
....*....|....*....|....*....|
gi 1953097357 254 DRDSGE----LKPALGRSWSFVPSTRILLD 279
Cdd:cd01393 155 KIRGGSgaslVPPALGNTWEHSVSTRLLLY 184
|
|
| recomb_radA |
TIGR02236 |
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ... |
10-315 |
3.98e-32 |
|
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: 121.77 E-value: 3.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 10 PGLTQDTVLQLRSRGVRTVVDLASADLEAVAQTCGLS----YKALVALRRvlLAQFSAFPSnGADLYEELKTSTAIlSTG 85
Cdd:TIGR02236 5 PGVGPATAEKLREAGYDTFEAIAVASPKELSEIAGISegtaAKIIQAARK--AADLGGFET-ADDVLERRKTIGKI-TTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 86 IGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAY-----GLQQNVVYIDSNGGLTASRILQLLQARTPDEEVq 160
Cdd:TIGR02236 81 SKELDELLGGGIETQAITEVFGEFGSGKTQICHQLAVNVQLpeekgGLGGKAVYIDTENTFRPERIMQMAEARGLDPDE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 161 agALQRIQVVRAFDI-FQMLDVLQdcrgtLSQQVSSASGTVKVVIVDSVTAVVSPLLGGqqREGLALMMQ-LARELKTLA 238
Cdd:TIGR02236 160 --VLKNIYVARAYNSnHQMLLVEK-----AEDLIKELNNPVKLLIVDSLTSHFRAEYVG--RGALAERQQkLNKHLHDLL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 239 R--DL-GMAVVVTNHMTRDRDS--GE-LKPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLPTGfQEMVDIG 312
Cdd:TIGR02236 231 RlaDLyNAAVVVTNQVMARPDAffGDpTRPIGGHILGHAATFRVYL-----RKGKGDKRIARLVDSPHLPEG-EAVFRIT 304
|
...
gi 1953097357 313 TWG 315
Cdd:TIGR02236 305 EKG 307
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
100-299 |
2.22e-31 |
|
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: 115.78 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 100 GEVTEIVGGPGSGKTQVCLCVAANV-----AYGLQQNVVYIDSNGGLtasrilqllqartpdeevqagalqRIQVVRAFD 174
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVqipkcFGGLAGEAIYIDTEGSF------------------------NIHYFRVHD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 175 IFQMLDVLQDCRGTLSQQVSsasgtVKVVIVDSVTAvvsPLLGGQQREGL--ALMMQLARELKTLARDLGMAVVVTNHMT 252
Cdd:cd19492 57 YVELLALINSLPKFLEDHPK-----VKLIVVDSIAF---PFRHDFDDLAQrtRLLNGLAQLLHSLARQHNLAVVLTNQVT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1953097357 253 ---RDRDSGELKPALGRSWSFVPSTRILLDIDEGARAsgswrrACLTKSP 299
Cdd:cd19492 129 tkiSEDGQSQLVPALGESWSHACTTRLFLTWDEKQRF------AHLYKSP 172
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
90-299 |
5.45e-30 |
|
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: 113.57 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 90 DKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-----YGLQQNVVYIDSNGGLTASRILQLLQARTP--------D 156
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkGGLDGGVLYIDTESKFSAERLAEIAEARFPeafsgfmeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 157 EEVQAGALQRIQVVRAFDIFQMLDVLQDCRGTLSQQvssasgTVKVVIVDSVTAVVSPLLGGQQREGLALMMQLARE--- 233
Cdd:cd19493 81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSS------GVRLVVIDSIAALVRREFGGSDGEVTERHNALAREass 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953097357 234 LKTLARDLGMAVVVTNHMTR-----DRDSGELKPALGRSWSFVPSTRILLDidegaRASGSWRRAC-LTKSP 299
Cdd:cd19493 155 LKRLAEEFRIAVLVTNQATThfgdaGDGSSGVTAALGDAWAHAVNTRLRLE-----RCLLQLRRVLeIVKSP 221
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
82-304 |
4.12e-28 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 108.80 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAygLQ-QNVVYIDSNgGLTASRILQLlqARTPDEEVq 160
Cdd:PRK09361 5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAA--KNgKKVIYIDTE-GLSPERFKQI--AGEDFEEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 161 agaLQRIQVVRAFDIFQMLDVLQDCRGTLSQQVSsasgtvkVVIVDSVTAVVSpLLGGQQREGLALMMQLARELKTL--- 237
Cdd:PRK09361 79 ---LSNIIIFEPSSFEEQSEAIRKAEKLAKENVG-------LIVLDSATSLYR-LELEDEEDNSKLNRELGRQLTHLlkl 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 238 ARDLGMAVVVTNHMTRDRDSGELKPALGRS---WSfvpstRILLDIDegaRASGSWRRACLTKSPRLPTG 304
Cdd:PRK09361 148 ARKHDLAVVITNQVYSDIDSDGLRPLGGHTlehWS-----KTILRLE---KFRNGKRRATLEKHRSRPEG 209
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
10-304 |
1.57e-27 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 109.58 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 10 PGLTQDTVLQLRSRGVRTVVDLASADLEAVAQTCGLSYKA----LVALRRvlLAQFSAFPSnGADLYEELKtSTAILSTG 85
Cdd:PRK04301 12 PGVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTaakiIEAARE--AADIGGFET-ALEVLERRK-NVGKITTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 86 IGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAY-----GLQQNVVYIDSNGGLTASRILQLLQAR--TPDEe 158
Cdd:PRK04301 88 SKELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekgGLEGKAVYIDTEGTFRPERIEQMAEALglDPDE- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 159 vqagALQRIQVVRAFDI-FQMLdvLQDCRGTLSQQVSSasgtVKVVIVDSVTAVV-SPLLGgqqREGLALMMQ-LARELK 235
Cdd:PRK04301 167 ----VLDNIHVARAYNSdHQML--LAEKAEELIKEGEN----IKLVIVDSLTAHFrAEYVG---RGNLAERQQkLNKHLH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953097357 236 TLAR---DLGMAVVVTNHMTRDRDS--GE-LKPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLPTG 304
Cdd:PRK04301 234 DLLRladLYNAAVVVTNQVMARPDAffGDpTQPIGGHILGHTATFRIYL-----RKSKGNKRIARLVDSPHLPEG 303
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
82-311 |
6.13e-27 |
|
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: 105.47 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVA-YGLqqNVVYIDSNgGLTASRILQLLQARTPDeevq 160
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAkQGK--KVVYIDTE-GLSPERFQQIAGERFES---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 161 agALQRIQVVRAFDIFQMLDVLQDCRGTLSqqvssaSGTVKVVIVDSVTAVVSPLLGGQQREGLALMMQLAReLKTLARD 240
Cdd:cd01394 74 --IASNIIVFEPYSFDEQGVAIQEAEKLLK------SDKVDLVVVDSATALYRLELGDDSEANRELSRQMSK-LLSIARK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953097357 241 LGMAVVVTNHMTRDRDSGELKPALGRSWSFVPSTRILLDidegaRASGSWRRACLTKSPRLPTGFQEMVDI 311
Cdd:cd01394 145 YDIPVVITNQVYSDIDDDRLKPVGGTLLEHWSKAIIRLE-----KSPPGLRRATLEKHRSRPEGQSAGFRI 210
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
82-315 |
2.92e-26 |
|
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: 103.98 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAY-----GLQQNVVYIDSNGGLTASRILQLLQART-- 154
Cdd:cd19515 1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeegGLNGKAVYIDTENTFRPERIMQMAKALGld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 155 PDEevqagALQRIQVVRAFDI-FQMLDVLQdcrgtlSQQVSSASGTVKVVIVDSVTAVV-SPLLGgqqREGLALMMQ-LA 231
Cdd:cd19515 81 PDE-----VLDNIYVARAYNSnHQMLLVEK------AEDLIKEGNNIKLLIVDSLTSHFrAEYVG---RGTLAERQQkLN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 232 RELKTLAR--DL-GMAVVVTNHMTRDRDS---GELKPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLPTGf 305
Cdd:cd19515 147 KHLHDLHRlaDLyNIAVLVTNQVMAKPDAffgDPTQAIGGHILGHAATFRVYL-----RKGKGGKRIARLVDSPHLPEG- 220
|
250
....*....|
gi 1953097357 306 QEMVDIGTWG 315
Cdd:cd19515 221 EAVFRITEKG 230
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
89-302 |
6.32e-24 |
|
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: 98.13 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 89 LDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAY-----GLQQNVVYIDSNGGLTASRILQLLQ--ARTPDEEVQA 161
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLprelgGLGGGAVYICTESSFPSKRLQQLASslPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 162 GALQRIQVVRAFDifqmLDVLQDCrgtLSQQVSS--ASGTVKVVIVDSVTAVVSPLLGGQQREGL---ALMMQLARELKT 236
Cdd:cd19491 81 NFLDNIFVEHVAD----LETLEHC---LNYQLPAllERGPIRLVVIDSIAALFRSEFDTSRSDLVeraKYLRRLADHLKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 237 LARDLGMAVVVTNHMT-------------------------RDRDSGELKPALGRSWSFVPSTRILLD-----IDEGARA 286
Cdd:cd19491 154 LADKYNLAVVVVNQVTdrfdsssdasglgvldylsqfssfsGGVSGNRKVPALGLTWANLVNTRLMLSrtpkrITDSSAA 233
|
250
....*....|....*.
gi 1953097357 287 SGSWRRACLTKSPRLP 302
Cdd:cd19491 234 SISVRRLEVVFSPHLP 249
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
82-302 |
6.72e-24 |
|
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: 98.14 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQARTPD 156
Cdd:pfam08423 19 ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLChtLCVTCQLPLemgGGEGKALYIDTEGTFRPERLVAIAERYGLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 157 EEVqagALQRIQVVRAFDIFQMLDVLQDCRGTLSQqvssasGTVKVVIVDSVTAVVSPLLGGqqREGLAL-MMQLARELK 235
Cdd:pfam08423 99 PED---VLDNVAYARAYNSEHQMQLLQQAAAMMSE------SRFALLIVDSATALYRTDFSG--RGELAErQQHLAKFLR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953097357 236 TLAR---DLGMAVVVTNHMTRDRDSGEL-------KPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLP 302
Cdd:pfam08423 168 TLQRladEFGVAVVITNQVVAQVDGAAGmfsgdpkKPIGGHIMAHASTTRLSL-----RKGRGEQRICKIYDSPCLP 239
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
82-304 |
5.38e-22 |
|
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: 92.59 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQAR--T 154
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLChtLAVTCQLPIdrgGGEGKAIYIDTEGTFRPERLRAIAQRFglD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 155 PDEevqagALQRIQVVRAFDIFQMLDVLQDCRGTLSQQVssasgtVKVVIVDSVTAVVSPLLGGQQrEGLALMMQLA--- 231
Cdd:cd01123 81 PDD-----VLDNVAYARAFNSDHQTQLLDQAAAMMVESR------FKLLIVDSATALYRTDYSGRG-ELSARQMHLAkfl 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953097357 232 RELKTLARDLGMAVVVTNHMTRDRDSGEL------KPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLPTG 304
Cdd:cd01123 149 RMLQRLADEFGVAVVVTNQVVAQVDGAMMfaadpkKPIGGNILAHASTTRLYL-----RKGRGETRICKIYDSPCLPEA 222
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
11-302 |
5.88e-20 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 89.02 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 11 GLTQDTVLQLRSRGVRTVVDLASADLEAVAQTCGLS-YKALvalrRVLLAQFSAFP---SNGADLYEElKTSTAILSTGI 86
Cdd:PLN03186 35 GIAALDIKKLKDAGIHTVESLAYAPKKDLLQIKGISeAKVE----KILEAASKLVPlgfTTASQLHAQ-RQEIIQITTGS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 87 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQARTPDeevQA 161
Cdd:PLN03186 110 RELDKILEGGIETGSITEIYGEFRTGKTQLChtLCVTCQLPLdqgGGEGKAMYIDTEGTFRPQRLIQIAERFGLN---GA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 162 GALQRIQVVRAFDIFQMLDVLQDCRGTLSQQvssasgTVKVVIVDSVTAVVSPLLGGQQrEGLALMMQLARELKTLAR-- 239
Cdd:PLN03186 187 DVLENVAYARAYNTDHQSELLLEAASMMAET------RFALMIVDSATALYRTEFSGRG-ELSARQMHLGKFLRSLQRla 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 240 -DLGMAVVVTNHMTRDRDSG------ELKPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLP 302
Cdd:PLN03186 260 dEFGVAVVITNQVVAQVDGSaffagpQLKPIGGNIMAHASTTRLAL-----RKGRGENRICKVISSPCLP 324
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
100-251 |
1.55e-19 |
|
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: 85.48 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 100 GEVTEIVGGPGSGKTQVCLCVAAN----------VAYGLQQNVVYIDSNGGLTASRILQLLQAR--------------TP 155
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARcilpsswggvPLGGLEAAVVFIDTDGRFDILRLRSILEARiraaiqaanssddeED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 156 DEEVQAGALQRIQVVRAFDIFQMLDVLQDCRGTLSQQvsSASGTVKVVIVDSVTA------VVSPLLGGQQREGLALMMQ 229
Cdd:cd19490 81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSL--SANPELGLLLIDSISAfywqdrFSAELARAAPLLQEAALRA 158
|
170 180
....*....|....*....|..
gi 1953097357 230 LARELKTLARDLGMAVVVTNHM 251
Cdd:cd19490 159 ILRELRRLRRRFQLVVIATKQA 180
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
82-302 |
4.41e-18 |
|
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: 81.60 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQARTPD 156
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLPIdqgGGEGKALYIDTEGTFRPERLLAIAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 157 EEVqagALQRIQVVRAFDIFQMLDVLQDCRGTLSQQVSSasgtvkVVIVDSVTAVVSPLLGGQQrEGLALMMQLARELKT 236
Cdd:cd19513 81 GED---VLDNVAYARAYNTDHQMQLLIQASAMMAESRYA------LLIVDSATALYRTDYSGRG-ELSARQMHLAKFLRM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953097357 237 LAR---DLGMAVVVTNHMTRDRDSG------ELKPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLP 302
Cdd:cd19513 151 LQRladEFGVAVVITNQVVAQVDGAamfagdPKKPIGGNIMAHASTTRLYL-----RKGRGETRICKIYDSPCLP 220
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
82-302 |
1.29e-17 |
|
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: 80.48 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQARTPD 156
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLShtLCVTAQLPGsmgGGGGKVAYIDTEGTFRPDRIRPIAERFGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 157 eevQAGALQRIQVVRAFDIFQMLDVLQDCRGTLSQqvssaSGTVKVVIVDSVTAVVSPLLGG-------QQRegLALMMQ 229
Cdd:cd19514 81 ---HDAVLDNILYARAYTSEHQMELLDYVAAKFHE-----EAVFRLLIIDSIMALFRVDFSGrgelaerQQK--LAQMLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953097357 230 larELKTLARDLGMAVVVTNHMTRDRDSGEL------KPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLP 302
Cdd:cd19514 151 ---RLQKISEEYNVAVFITNQVTADPGAAMTfqadpkKPIGGHILAHASTTRISL-----RKGRGEERIAKIYDSPDLP 221
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
11-258 |
6.18e-17 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 80.04 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 11 GLTQDTVLQLRSRGVRTVvdlasadlEAVAQTC--------GLSY----KALVALRRVLLAQFSafpsNGADLYEeLKTS 78
Cdd:PTZ00035 30 GINAADIKKLKEAGICTV--------ESVAYATkkdlcnikGISEakveKIKEAASKLVPMGFI----SATEYLE-ARKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 79 TAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQAR 153
Cdd:PTZ00035 97 IIRITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLChtLCVTCQLPIeqgGGEGKVLYIDTEGTFRPERIVQIAERF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 154 TPDEEVqagALQRIQVVRAFDIFQMLDVLQDCRGTLSQQvssasgTVKVVIVDSVTAVVSPLLGG-------QQRegLAL 226
Cdd:PTZ00035 177 GLDPED---VLDNIAYARAYNHEHQMQLLSQAAAKMAEE------RFALLIVDSATALFRVDYSGrgelaerQQH--LGK 245
|
250 260 270
....*....|....*....|....*....|..
gi 1953097357 227 MMqlaRELKTLARDLGMAVVVTNHMTRDRDSG 258
Cdd:PTZ00035 246 FL---RALQKLADEFNVAVVITNQVMADVDGA 274
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
11-256 |
7.47e-17 |
|
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: 79.77 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 11 GLTQDTVLQLRSRGVRTVVDLASADLEAVAQTCGLS-YKA----LVALRRVLLAQFSAfpsngADLYEElKTSTAILSTG 85
Cdd:TIGR02239 8 GITAADIKKLQEAGLHTVESVAYAPKKQLLEIKGISeAKAdkilAEAAKLVPMGFTTA-----TEFHQR-RQEVIQLTTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 86 IGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQARTPDEEvq 160
Cdd:TIGR02239 82 SKELDKLLGGGIETGSITEIFGEFRTGKTQLChtLAVTCQLPIdqgGGEGKALYIDTEGTFRPERLLAIAERYGLNPE-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 161 aGALQRIQVVRAFDIFQMLDVLQDCRGTLSQQVSSasgtvkVVIVDSVTAVVSPLLGGQQrEGLALMMQLARELKTLAR- 239
Cdd:TIGR02239 160 -DVLDNVAYARAYNTDHQLQLLQQAAAMMSESRFA------LLIVDSATALYRTDFSGRG-ELSARQMHLARFLRSLQRl 231
|
250
....*....|....*....
gi 1953097357 240 --DLGMAVVVTNHMTRDRD 256
Cdd:TIGR02239 232 adEFGVAVVITNQVVAQVD 250
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
11-302 |
1.23e-14 |
|
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: 73.27 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 11 GLTQDTVLQLRSRGVRTVVDLASADLEAVAQTCGLSY----KALVALRRVLLAQFSAfpsngADLYEELKTSTAILSTGI 86
Cdd:TIGR02238 8 GINAADIKKLKSAGICTVNGVIMTTRRALCKIKGLSEakvdKIKEAASKIINPGFIT-----AFEISQKRKKVLKITTGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 87 GSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVAY---GLQQNVVYIDSNGGLTASRILQLLQARTPDEEVqa 161
Cdd:TIGR02238 83 QALDGILGGGIESMSITEVFGEFRCGKTQLShtLCVTAQLPRemgGGNGKVAYIDTEGTFRPDRIRAIAERFGVDPDA-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 162 gALQRIQVVRAFDIFQMLDVLQDCRGTLSqqvssaSGTVKVVIVDSVTAVVSPLLGG-------QQRegLALMMQlarEL 234
Cdd:TIGR02238 161 -VLDNILYARAYTSEHQMELLDYLAAKFS------EEPFRLLIVDSIMALFRVDFSGrgelserQQK--LAQMLS---RL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953097357 235 KTLARDLGMAVVVTNHMTRDRD------SGELKPALGRSWSFVPSTRILLdidegARASGSWRRACLTKSPRLP 302
Cdd:TIGR02238 229 NKISEEFNVAVFVTNQVQADPGatmtfiADPKKPIGGHVLAHASTTRILL-----RKGRGEERVAKLYDSPDMP 297
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
68-278 |
3.90e-11 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 63.26 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 68 GADLYEELKTSTAIlSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVC--LCVAANVA---YGLQQNVVYIDSNGGLT 142
Cdd:PLN03187 95 GSDALLKRKSVVRI-TTGSQALDELLGGGIETRCITEAFGEFRSGKTQLAhtLCVTTQLPtemGGGNGKVAYIDTEGTFR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 143 ASRILQLLQARTPDeevqAGA-LQRIQVVRAFDIFQMLDVLQDCRGTLSQQvssasgTVKVVIVDSVTAV--VSPLLGGQ 219
Cdd:PLN03187 174 PDRIVPIAERFGMD----ADAvLDNIIYARAYTYEHQYNLLLGLAAKMAEE------PFRLLIVDSVIALfrVDFTGRGE 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953097357 220 QREGLALMMQLARELKTLARDLGMAVVVTNHMTRDRDSGEL-----KPALGRSWSFVPSTRILL 278
Cdd:PLN03187 244 LAERQQKLAQMLSRLTKIAEEFNVAVYMTNQVIADPGGGMFisdpkKPAGGHVLAHAATIRLML 307
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
82-252 |
3.48e-10 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 59.16 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANvayGLQQN--VVYIdsngGLTASRILQLLQART----P 155
Cdd:COG0467 2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAE---GLRRGekGLYV----SFEESPEQLLRRAESlgldL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 156 DEEVQAGalqRIQVVRAFDIFQMLDVlqdcrGTLSQQVSSA--SGTVKVVIVDSVTAVVspLLGGQQREGLALMMQLARE 233
Cdd:COG0467 75 EEYIESG---LLRIIDLSPEELGLDL-----EELLARLREAveEFGAKRVVIDSLSGLL--LALPDPERLREFLHRLLRY 144
|
170
....*....|....*....
gi 1953097357 234 LKtlarDLGMAVVVTNHMT 252
Cdd:COG0467 145 LK----KRGVTTLLTSETG 159
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
83-249 |
2.23e-08 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 54.79 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 83 STGIGSLDKLL-DAGLYTGEVTEIVGGPGSGKTQVCLCVAANVayglQQN---VVYIDSNGGLTASR-------ILQLLQ 151
Cdd:COG0468 45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLALHAIAEA----QKAggiAAFIDAEHALDPEYakklgvdIDNLLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 152 ARtPD--EEvqagalqriqvvrAFDIFQMLdvlqdcrgtlsqqVSsaSGTVKVVIVDSVTAVVsP-----------LLGG 218
Cdd:COG0468 121 SQ-PDtgEQ-------------ALEIAETL-------------VR--SGAVDLIVVDSVAALV-PkaeiegemgdsHVGL 170
|
170 180 190
....*....|....*....|....*....|.
gi 1953097357 219 QQReglaLMMQLARELKTLARDLGMAVVVTN 249
Cdd:COG0468 171 QAR----LMSQALRKLTGAISKSNTTVIFIN 197
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
82-254 |
4.70e-08 |
|
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: 53.30 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAyGLQQNVVYI---DSNG--GLTASRilqlLQARTPD 156
Cdd:cd01121 64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKSTLLLQVAARLA-QRGGKVLYVsgeESLSqiKLRAER----LGLGSDN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 157 eevqagalqrIQVVRAFD---IFQMLDVLQdcrgtlsqqvssasgtVKVVIVDSVTAVVSPLLGG------QQREGLALM 227
Cdd:cd01121 139 ----------LYLLAETNleaILAEIEELK----------------PSLVVIDSIQTVYSPELTSspgsvsQVRECAAEL 192
|
170 180
....*....|....*....|....*..
gi 1953097357 228 MQLARElktlardLGMAVVVTNHMTRD 254
Cdd:cd01121 193 LRLAKE-------TGIPVFLVGHVTKD 212
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-266 |
5.62e-08 |
|
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: 51.22 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 99 TGEVTEIVGGPGSGKTQVCLCVAANVAYgLQQNVVYIDsnggltASRILQLLQARTPDEEVQAGALQRIQVVRAFDIFQM 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP-PGGGVIYID------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 179 LDVLQdcrgtlsqqvssasgtVKVVIVDSVTAvvsplLGGQQREGLALMMQLARELKTLARDLGMAVVVTNHMTRDRDSG 258
Cdd:smart00382 74 ARKLK----------------PDVLILDEITS-----LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
....*...
gi 1953097357 259 ELKPALGR 266
Cdd:smart00382 133 LLRRRFDR 140
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
82-293 |
1.89e-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: 51.11 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCL-CVAANVAYGlqQNVVYIdsngGL--TASRILQllQARTP--- 155
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLqFLYAGAKNG--EPGLFF----TFeeSPERLLR--NAKSFgwd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 156 -DEEVQAGalqRIQVVRAFDIFQMLDVLQDCRGTLSQQVssASGTVKVVIVDSVTAVVSPLLggQQREGLALMMQLAREL 234
Cdd:cd01124 73 fDEMEDEG---KLIIVDAPPTEAGRFSLDELLSRILSII--KSFKAKRVVIDSLSGLRRAKE--DQMRARRIVIALLNEL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953097357 235 ktlaRDLGMAVVVTNHMTRDRDSGELKPAlgrSWSFVPSTRILLDIDEgarASGSWRRA 293
Cdd:cd01124 146 ----RAAGVTTIFTSEMRSFLSSESAGGG---DVSFIVDGVILLRYVE---IEGELRRT 194
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
82-259 |
1.19e-06 |
|
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: 48.78 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAYGLQQNVVYI----DSNG--------G-----LTAS 144
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNGALKYGEPGVFVtleePPEDlrenarsfGwdlekLEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 145 RILQLLQARTPDEEvqagalqRIQVVRAFDIFQMLDVLQDCRGTLSqqvssasgtVKVVIVDSVTAvvsplLGGQQREGL 224
Cdd:pfam06745 81 GKLAIIDASTSGIG-------IAEVEDRFDLEELIERLREAIREIG---------AKRVVIDSITT-----LFYLLKPAV 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953097357 225 A--LMMQLARELKtlarDLGmavvVTNHMTRDRDSGE 259
Cdd:pfam06745 140 AreILRRLKRVLK----GLG----VTAIFTSEKPSGE 168
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
82-249 |
5.72e-06 |
|
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: 46.78 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLY-TGEVTEIVGGPGSGKTQVCLCVAANV--AYGlqqNVVYIDSNGGLT---ASRI------LQL 149
Cdd:cd00983 5 IPTGSLSLDIALGIGGLpRGRIIEIYGPESSGKTTLALHAIAEAqkLGG---TAAFIDAEHALDpeyAKKLgvdidnLLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 150 LQartPDEEVQAgalqriqvvrafdiFQMLDVLqdCRgtlsqqvssaSGTVKVVIVDSVTAVV--SPLLG--GQQREGL- 224
Cdd:cd00983 82 SQ---PDTGEQA--------------LEIADTL--IR----------SGAVDLIVVDSVAALVpkAEIEGemGDSHVGLq 132
|
170 180
....*....|....*....|....*.
gi 1953097357 225 -ALMMQLARELKTLARDLGMAVVVTN 249
Cdd:cd00983 133 aRLMSQALRKLTGSLSKSKTTVIFIN 158
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
105-254 |
5.86e-06 |
|
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: 46.79 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 105 IVGGPGSGKTQVCLCVAANVAYGLQQNVVYI---DSNG-------GLTASRILQLLQARTPD----EEVQAGALQRIQVV 170
Cdd:cd19483 3 IGAGSGIGKSTIVRELAYHLITEHGEKVGIIsleESVEetakglaGKHLGKPEPLELPRDDIteeeEDDAFDNELGSGRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 171 RAFDIFQMLDV---LQDCRgtlsQQVssASGTVKVVIVDSVTAVVSPLLGGQQREGLALMMQlarELKTLARDLGMAVVV 247
Cdd:cd19483 83 FLYDHFGSLDWdnlKEKIR----YMV--KVLGCKVIVLDHLTILVSGLDSSDERKELDEIMT---ELAALVKELGVTIIL 153
|
....*..
gi 1953097357 248 TNHMTRD 254
Cdd:cd19483 154 VSHLRRP 160
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
82-249 |
9.13e-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: 43.06 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAYGLQQNVVYIDSNGgltasriLQLLQARTPDEEVQA 161
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDES-------IGTLFERSEALGIDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 162 GALQRIQVVRafdiFQMLDVLQDCRGTLSQQVSSA--SGTVKVVIVDSVTAVVSPLlggqqREGLALMMQLARELKTLAR 239
Cdd:cd19487 74 RAMVEKGLLS----IEQIDPAELSPGEFAQRVRTSveQEDARVVVIDSLNGYLNAM-----PDERFLILQMHELLSYLNN 144
|
170
....*....|
gi 1953097357 240 dLGMAVVVTN 249
Cdd:cd19487 145 -QGVTTLLIV 153
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
100-256 |
1.54e-04 |
|
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: 41.98 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 100 GEVTEIVGGPGSGKTQVCLCVAANVAYGL----------QQNVVYIDSNGG--LTASRILQLLQARTPDEEvqagaLQRI 167
Cdd:pfam13481 33 GGLGLLAGAPGTGKTTLALDLAAAVATGKpwlggprvpeQGKVLYVSAEGPadELRRRLRAAGADLDLPAR-----LLFL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 168 QVVRAFDIFQMLDVLQDCRGTLSQ--QVSSASGTVKVVIVDSVTAVvsplLGGqQREGLALMMQLARELKTLARDLGMAV 245
Cdd:pfam13481 108 SLVESLPLFFLDRGGPLLDADVDAleAALEEVEDPDLVVIDPLARA----LGG-DENSNSDVGRLVKALDRLARRTGATV 182
|
170
....*....|.
gi 1953097357 246 VVTNHMTRDRD 256
Cdd:pfam13481 183 LLVHHVGKDGA 193
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
100-297 |
3.97e-04 |
|
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: 41.21 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 100 GEVTEIVGGPGSGKTQVCLCVAANVAYGL---------QQNVVYIDSNGGltASRILQLLQARTPDEEVQAGALQRIQVV 170
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVATGRdwlgerrvkQGRVVYLAAEDP--RDGLRRRLKAIGAHLGDEDAALAENLVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 171 RAFDIFQMLDVLqdcRGTLSQQVSSASGTVKVVIVDSVTAVvsplLGGQQREGLALMMQLARELKTLARDLGMAVVVTNH 250
Cdd:cd01125 79 ENLRGKPVSIDA---EAPELERIIEELEGVRLIIIDTLARV----LHGGDENDAADMGAFVAGLDRIARETGAAVLLVHH 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953097357 251 MTRDRDSGELKPALGRSwSFVPSTRILLDI-----------DEGARASGSWRRACLTK 297
Cdd:cd01125 152 TGKDAAGDSQQAARGSS-ALRGAADAEINLskmdateaekvGLDKDLRRRFVRLDVTK 208
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
82-247 |
1.83e-03 |
|
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: 39.32 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLdAGLYTGEVTeIVGG-PGSGKTQVCLCVAANVAYGLQQNVVYIdSnggLTASRIlQLLQ------ART 154
Cdd:pfam03796 2 LPTGFTDLDRLT-GGLQPGDLI-IIAArPSMGKTAFALNIARNAAVKHKKPVAIF-S---LEMSAE-QLVMrllaseAGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 155 PDEEVQAGALQR---IQVVRAFDIFQMLDVLQDCRGTLS-QQVSS------ASGTVKVVIVDSVTAVVSPLLGGQQREGL 224
Cdd:pfam03796 75 DSQKLRTGQLTDedwEKLAKAAGRLSEAPLYIDDTPGLSiAEIRAkarrlkREHGLGLIVIDYLQLMSGGSRGENRQQEI 154
|
170 180
....*....|....*....|...
gi 1953097357 225 AlmmQLARELKTLARDLGMAVVV 247
Cdd:pfam03796 155 S---EISRSLKALAKELNVPVIA 174
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
105-256 |
4.82e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 37.69 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 105 IVGGPGSGKTQVCLCVaanvayglqQNVVYIDSNGGLTAsrilqllqartpdeeVQAGALQRIQVVRAFdifqmldvlQD 184
Cdd:pfam13479 7 IYGPSGIGKTTFAKTL---------PKPLFLDTEKGSKA---------------LDGDRFPDIVIRDSW---------QD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 185 CRGTLSQQVSSASGTVKVVIVDSVTAVVSPLLG--------GQQREGL------ALMMQLARELKTLARDLGMAVVVTNH 250
Cdd:pfam13479 54 FLDAIDELTAAELADYKTIVIDTVDWLERLCLAyickqngkGSSIEDGgygkgyGELGEEFRRLLDALQELGKNVIFTAH 133
|
....*.
gi 1953097357 251 MTRDRD 256
Cdd:pfam13479 134 AKTRKD 139
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
82-254 |
6.00e-03 |
|
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: 37.73 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 82 LSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCVAANVAYGLQQNVVYI-------------DSNG----GLTAS 144
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPGVFVtfeespediiknmASFGwdlpKLVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953097357 145 RILQLLQART-PDEEVQAGalqriqvvrAFDIfqmldvlqdcrGTLSQQVSSASGTVKV--VIVDSVTAVVSpllggqqr 221
Cdd:cd19485 81 GKLLILDASPePSEEEVTG---------EYDL-----------EALLIRIEYAIRKIGAkrVSLDSLEAVFS-------- 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 1953097357 222 eGLALMMQLARELKTLA---RDLGMAVVVTNHMTRD 254
Cdd:cd19485 133 -GLSDSAVVRAELLRLFawlKQKGVTAIMTGERGED 167
|
|
| |
