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Conserved domains on  [gi|19924117|ref|NP_598194|]
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DNA repair protein RAD51 homolog 2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
91-327 2.31e-96

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: 285.37  E-value: 2.31e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  91 DEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYF----NT 166
Cdd:cd19493   1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFsgfmEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 167 EEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqGNLKERNKFLAREASSLKYLA 246
Cdd:cd19493  81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSD-GEVTERHNALAREASSLKRLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 247 EEFSIPVILTNQITTHLSGAlasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILQYLDS-ERRQILIAKS 325
Cdd:cd19493 160 EEFRIAVLVTNQATTHFGDA-------------------GDGSSGVTAALGDAWAHAVNTRLRLERCLLqLRRVLEIVKS 220

                ..
gi 19924117 326 PL 327
Cdd:cd19493 221 PL 222
 
Name Accession Description Interval E-value
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
91-327 2.31e-96

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: 285.37  E-value: 2.31e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  91 DEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYF----NT 166
Cdd:cd19493   1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFsgfmEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 167 EEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqGNLKERNKFLAREASSLKYLA 246
Cdd:cd19493  81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSD-GEVTERHNALAREASSLKRLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 247 EEFSIPVILTNQITTHLSGAlasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILQYLDS-ERRQILIAKS 325
Cdd:cd19493 160 EEFRIAVLVTNQATTHFGDA-------------------GDGSSGVTAALGDAWAHAVNTRLRLERCLLqLRRVLEIVKS 220

                ..
gi 19924117 326 PL 327
Cdd:cd19493 221 PL 222
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
65-341 2.47e-48

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: 163.24  E-value: 2.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    65 QTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTE 144
Cdd:pfam08423   4 TTATELHQRRSELIQ---ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   145 SAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAq 223
Cdd:pfam08423  81 GTFRPERLVAIAE----RYgLDPEDVL----DNVAYARAYNSEHQMQLLQQAAAMMSESRFALLIVDSATALYRTDFSG- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   224 lQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSG-ALASQADLVSPaddlslsegtsgsscviaALGNTWSH 302
Cdd:pfam08423 152 -RGELAERQQHLAKFLRTLQRLADEFGVAVVITNQVVAQVDGaAGMFSGDPKKP------------------IGGHIMAH 212
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 19924117   303 SVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEG 341
Cdd:pfam08423 213 ASTTRLSLRKGRGEQRICKIYDSPCLPESEAVFAIGSGG 251
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
4-342 8.77e-38

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: 137.22  E-value: 8.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117     4 KKLKRVGlsqelcdrlsrhqILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafL 83
Cdd:TIGR02238  15 KKLKSAG-------------ICTVNGVIMTTRRALCKIKGLSEAKVDKIKEAASKIINPGFITAFEISQKRKKVLK---I 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    84 STTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY 163
Cdd:TIGR02238  79 TTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPREMGGGNGKVAYIDTEGTFRPDRIRAIAE----RF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   164 FNTEEKLLltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLK 243
Cdd:TIGR02238 155 GVDPDAVL---DNILYARAYTSEHQMELLDYLAAKFSEEPFRLLIVDSIMALFRVDFSG--RGELSERQQKLAQMLSRLN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   244 YLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIA 323
Cdd:TIGR02238 230 KISEEFNVAVFVTNQVQADPGATMTFIADPKKPIG------------------GHVLAHASTTRILLRKGRGEERVAKLY 291
                         330
                  ....*....|....*....
gi 19924117   324 KSPLAPFTSFVYTIKEEGL 342
Cdd:TIGR02238 292 DSPDMPEAEASFQITEGGI 310
PTZ00035 PTZ00035
Rad51 protein; Provisional
5-343 6.18e-37

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 135.90  E-value: 6.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    5 KLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLS 84
Cdd:PTZ00035  25 KLQSAGINAADIKKLKEAGICTVESVAYATKKDLCNIKGISEAKVEKIKEAASKLVPMGFISATEYLEARKNIIR---IT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   85 TTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY- 163
Cdd:PTZ00035 102 TGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAE----RFg 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  164 FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLK 243
Cdd:PTZ00035 178 LDPEDVL----DNIAYARAYNHEHQMQLLSQAAAKMAEERFALLIVDSATALFRVDYSG--RGELAERQQHLGKFLRALQ 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  244 YLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIA 323
Cdd:PTZ00035 252 KLADEFNVAVVITNQVMADVDGASMFVADPKKPIG------------------GHIIAHASTTRLSLRKGRGEQRICKIY 313
                        330       340
                 ....*....|....*....|
gi 19924117  324 KSPLAPFTSFVYTIKEEGLV 343
Cdd:PTZ00035 314 DSPNLPESEAVFAISEGGII 333
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
83-344 1.83e-11

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 63.01  E-value: 1.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILAtlptnmgglEGA-----VVYIDTESafSAERLVEIAE 157
Cdd:COG0467   2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLA--LQFLA---------EGLrrgekGLYVSFEE--SPEQLLRRAE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 158 SrfpryFNTEEKLLLTSSKVHL------YRELTCDEVLQRIeslEEEIISKGIKLVILDSVASVVRkefdaqLQGNLKER 231
Cdd:COG0467  69 S-----LGLDLEEYIESGLLRIidlspeELGLDLEELLARL---REAVEEFGAKRVVIDSLSGLLL------ALPDPERL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 232 NKFLAReassLKYLAEEFSIPVILTNQITTHLSgalasqadlvspaddlslsegtsgsscviAALGNTWSHSVNTRLILQ 311
Cdd:COG0467 135 REFLHR----LLRYLKKRGVTTLLTSETGGLED-----------------------------EATEGGLSYLADGVILLR 181
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 19924117 312 YLDSE---RRQILIAKSPLAPF--TSFVYTIKEEGLVL 344
Cdd:COG0467 182 YVELGgelRRALSVLKMRGSAHdrTIREFEITDGGIEV 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
101-268 5.25e-07

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.52  E-value: 5.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    101 GSLTEITGPPGCGKTQfcIMMSILATLPTNMGGlegaVVYIDTESAFSAERLVEIAESRFPRYFNTeekllltsskvhly 180
Cdd:smart00382   2 GEVILIVGPPGSGKTT--LARALARELGPPGGG----VIYIDGEDILEEVLDQLLLIIVGGKKASG-------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    181 reltcdEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLareasslkyLAEEFSIPVILTNQIT 260
Cdd:smart00382  62 ------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL---------LKSEKNLTVILTTNDE 126

                   ....*...
gi 19924117    261 THLSGALA 268
Cdd:smart00382 127 KDLGPALL 134
 
Name Accession Description Interval E-value
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
91-327 2.31e-96

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: 285.37  E-value: 2.31e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  91 DEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYF----NT 166
Cdd:cd19493   1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFPEAFsgfmEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 167 EEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqGNLKERNKFLAREASSLKYLA 246
Cdd:cd19493  81 NERAEEMLKRVAVVRVTTLAQLLERLPNLEEHILSSGVRLVVIDSIAALVRREFGGSD-GEVTERHNALAREASSLKRLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 247 EEFSIPVILTNQITTHLSGAlasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILQYLDS-ERRQILIAKS 325
Cdd:cd19493 160 EEFRIAVLVTNQATTHFGDA-------------------GDGSSGVTAALGDAWAHAVNTRLRLERCLLqLRRVLEIVKS 220

                ..
gi 19924117 326 PL 327
Cdd:cd19493 221 PL 222
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
101-312 5.15e-60

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: 191.03  E-value: 5.15e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 101 GSLTEITGPPGCGKTQFCIMMSILATLptnmggLEGAVVYIDTESAFSAERLVEIAESrfprYFNTEEKLLLTSSKVHLY 180
Cdd:cd01393   1 GKITEIYGPPGSGKTQLALQLAANALL------LGGGVVWIDTEGAFPPSRLVQILEA----SPSSELELAEALSRLLYF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 181 RELTCDEVLQRIESLEEEIIS-KGIKLVILDSVASVVRKEFDAQLQG--NLKERNKFLAREASSLKYLAEEFSIPVILTN 257
Cdd:cd01393  71 RPPDTLAHLLALDSLPESLFPpPNTSLVVVDSVSALFRKAFPRGGDGdsSSSLRARLLSQLARALQKLAAQFNLAVVVTN 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19924117 258 QITTHLSGAlasqadlvspaddlslsegtSGSSCVIAALGNTWSHSVNTRLILQY 312
Cdd:cd01393 151 QVTTKIRGG--------------------SGASLVPPALGNTWEHSVSTRLLLYR 185
XRCC3 cd19491
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ...
90-326 8.89e-49

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: 164.39  E-value: 8.89e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  90 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYFNTEEK 169
Cdd:cd19491   1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLALTVQLPRELGGLGGGAVYICTESSFPSKRLQQLASSLPKRYHLEKAK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 170 LLLTSSKVHLYREL-TCDEVLQriESLEEEIISKGIKLVILDSVASVVRKEFDAQlQGNLKERNKFLAREASSLKYLAEE 248
Cdd:cd19491  81 NFLDNIFVEHVADLeTLEHCLN--YQLPALLERGPIRLVVIDSIAALFRSEFDTS-RSDLVERAKYLRRLADHLKRLADK 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19924117 249 FSIPVILTNQITTHL-SGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTWSHSVNTRLILQYLDSERRQILIAKSP 326
Cdd:cd19491 158 YNLAVVVVNQVTDRFdSSSDASGLGVLDYLSQFSSFSGGVSGNRKVPALGLTWANLVNTRLMLSRTPKRITDSSAASIS 236
Rad51 pfam08423
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ...
65-341 2.47e-48

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: 163.24  E-value: 2.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    65 QTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTE 144
Cdd:pfam08423   4 TTATELHQRRSELIQ---ITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLCHTLCVTCQLPLEMGGGEGKALYIDTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   145 SAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAq 223
Cdd:pfam08423  81 GTFRPERLVAIAE----RYgLDPEDVL----DNVAYARAYNSEHQMQLLQQAAAMMSESRFALLIVDSATALYRTDFSG- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   224 lQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSG-ALASQADLVSPaddlslsegtsgsscviaALGNTWSH 302
Cdd:pfam08423 152 -RGELAERQQHLAKFLRTLQRLADEFGVAVVITNQVVAQVDGaAGMFSGDPKKP------------------IGGHIMAH 212
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 19924117   303 SVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEG 341
Cdd:pfam08423 213 ASTTRLSLRKGRGEQRICKIYDSPCLPESEAVFAIGSGG 251
Rad51C cd19492
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ...
101-326 1.01e-38

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: 135.43  E-value: 1.01e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 101 GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFsaerlveiaesrfpryfnteekllltssKVHLY 180
Cdd:cd19492   1 GKITEICGVPGVGKTQLCMQLAVNVQIPKCFGGLAGEAIYIDTEGSF----------------------------NIHYF 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 181 RELTCDEVLQRIESLEEEIIS-KGIKLVILDSVASVVRKEFDaqlqgNLKERNKFLAREASSLKYLAEEFSIPVILTNQI 259
Cdd:cd19492  53 RVHDYVELLALINSLPKFLEDhPKVKLIVVDSIAFPFRHDFD-----DLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQV 127
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19924117 260 TTHLSgalasqadlvspaddlslsegTSGSSCVIAALGNTWSHSVNTRLILqYLDSERRQILIAKSP 326
Cdd:cd19492 128 TTKIS---------------------EDGQSQLVPALGESWSHACTTRLFL-TWDEKQRFAHLYKSP 172
Rad51_DMC1_archRadA cd01123
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ...
83-342 2.20e-38

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: 136.89  E-value: 2.20e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 162
Cdd:cd01123   1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDRGGGEGKAIYIDTEGTFRPERLRAIAQR---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 yFNTEEKLLLtsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSL 242
Cdd:cd01123  77 -FGLDPDDVL--DNVAYARAFNSDHQTQLLDQAAAMMVESRFKLLIVDSATALYRTDYSG--RGELSARQMHLAKFLRML 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 243 KYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILI 322
Cdd:cd01123 152 QRLADEFGVAVVVTNQVVAQVDGAMMFAADPKKPIG------------------GNILAHASTTRLYLRKGRGETRICKI 213
                       250       260
                ....*....|....*....|
gi 19924117 323 AKSPLAPFTSFVYTIKEEGL 342
Cdd:cd01123 214 YDSPCLPEAEAVFAITADGV 233
recomb_DMC1 TIGR02238
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ...
4-342 8.77e-38

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: 137.22  E-value: 8.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117     4 KKLKRVGlsqelcdrlsrhqILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafL 83
Cdd:TIGR02238  15 KKLKSAG-------------ICTVNGVIMTTRRALCKIKGLSEAKVDKIKEAASKIINPGFITAFEISQKRKKVLK---I 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    84 STTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY 163
Cdd:TIGR02238  79 TTGSQALDGILGGGIESMSITEVFGEFRCGKTQLSHTLCVTAQLPREMGGGNGKVAYIDTEGTFRPDRIRAIAE----RF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   164 FNTEEKLLltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLK 243
Cdd:TIGR02238 155 GVDPDAVL---DNILYARAYTSEHQMELLDYLAAKFSEEPFRLLIVDSIMALFRVDFSG--RGELSERQQKLAQMLSRLN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   244 YLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIA 323
Cdd:TIGR02238 230 KISEEFNVAVFVTNQVQADPGATMTFIADPKKPIG------------------GHVLAHASTTRILLRKGRGEERVAKLY 291
                         330
                  ....*....|....*....
gi 19924117   324 KSPLAPFTSFVYTIKEEGL 342
Cdd:TIGR02238 292 DSPDMPEAEASFQITEGGI 310
PTZ00035 PTZ00035
Rad51 protein; Provisional
5-343 6.18e-37

Rad51 protein; Provisional


Pssm-ID: 185407 [Multi-domain]  Cd Length: 337  Bit Score: 135.90  E-value: 6.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    5 KLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLS 84
Cdd:PTZ00035  25 KLQSAGINAADIKKLKEAGICTVESVAYATKKDLCNIKGISEAKVEKIKEAASKLVPMGFISATEYLEARKNIIR---IT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   85 TTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY- 163
Cdd:PTZ00035 102 TGSTQLDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPIEQGGGEGKVLYIDTEGTFRPERIVQIAE----RFg 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  164 FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLK 243
Cdd:PTZ00035 178 LDPEDVL----DNIAYARAYNHEHQMQLLSQAAAKMAEERFALLIVDSATALFRVDYSG--RGELAERQQHLGKFLRALQ 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  244 YLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIA 323
Cdd:PTZ00035 252 KLADEFNVAVVITNQVMADVDGASMFVADPKKPIG------------------GHIIAHASTTRLSLRKGRGEQRICKIY 313
                        330       340
                 ....*....|....*....|
gi 19924117  324 KSPLAPFTSFVYTIKEEGLV 343
Cdd:PTZ00035 314 DSPNLPESEAVFAISEGGII 333
recomb_RAD51 TIGR02239
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ...
37-342 1.23e-36

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: 134.47  E-value: 1.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    37 ELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQ 116
Cdd:TIGR02239  35 QLLEIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRQEVIQ---LTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQ 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   117 FCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpRY-FNTEEKLlltsSKVHLYRELTCDEVLQRIESL 195
Cdd:TIGR02239 112 LCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE----RYgLNPEDVL----DNVAYARAYNTDHQLQLLQQA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   196 EEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALAS-QADLV 274
Cdd:TIGR02239 184 AAMMSESRFALLIVDSATALYRTDFSG--RGELSARQMHLARFLRSLQRLADEFGVAVVITNQVVAQVDGAGSMfAGDPK 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19924117   275 SPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 342
Cdd:TIGR02239 262 KPIG------------------GNIMAHASTTRLSLRKGRGEQRICKIYDSPCLPESEAMFAIYEDGI 311
PLN03186 PLN03186
DNA repair protein RAD51 homolog; Provisional
37-342 3.13e-36

DNA repair protein RAD51 homolog; Provisional


Pssm-ID: 178728 [Multi-domain]  Cd Length: 342  Bit Score: 134.09  E-value: 3.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   37 ELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSpafLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQ 116
Cdd:PLN03186  62 DLLQIKGISEAKVEKILEAASKLVPLGFTTASQLHAQRQEIIQ---ITTGSRELDKILEGGIETGSITEIYGEFRTGKTQ 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  117 FCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsRF-------------PRYFNTEEKLlltsskvhlyrel 183
Cdd:PLN03186 139 LCHTLCVTCQLPLDQGGGEGKAMYIDTEGTFRPQRLIQIAE-RFglngadvlenvayARAYNTDHQS------------- 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  184 tcdEVLQRIESLeeeIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHL 263
Cdd:PLN03186 205 ---ELLLEAASM---MAETRFALMIVDSATALYRTEFSG--RGELSARQMHLGKFLRSLQRLADEFGVAVVITNQVVAQV 276
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19924117  264 SGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGL 342
Cdd:PLN03186 277 DGSAFFAGPQLKPIG------------------GNIMAHASTTRLALRKGRGENRICKVISSPCLPEAEARFSISSEGV 337
Rad51 cd19513
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ...
83-341 4.59e-36

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: 130.52  E-value: 4.59e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAEsrfpR 162
Cdd:cd19513   1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKALYIDTEGTFRPERLLAIAE----R 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 Y-FNTEEKLlltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASS 241
Cdd:cd19513  77 YgLNGEDVL----DNVAYARAYNTDHQMQLLIQASAMMAESRYALLIVDSATALYRTDYSG--RGELSARQMHLAKFLRM 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 242 LKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQIL 321
Cdd:cd19513 151 LQRLADEFGVAVVITNQVVAQVDGAAMFAGDPKKPIG------------------GNIMAHASTTRLYLRKGRGETRICK 212
                       250       260
                ....*....|....*....|
gi 19924117 322 IAKSPLAPFTSFVYTIKEEG 341
Cdd:cd19513 213 IYDSPCLPEAEAVFAITEDG 232
DMC1 cd19514
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ...
83-342 3.11e-35

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: 128.63  E-value: 3.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpr 162
Cdd:cd19514   1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLSHTLCVTAQLPGSMGGGGGKVAYIDTEGTFRPDRIRPIAER---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 yFNTEEKLLLTSSkvhLY-RELTCDEVLQRIESLEEEIISKGI-KLVILDSVASVVRKEFDAqlQGNLKERNKFLAREAS 240
Cdd:cd19514  77 -FGVDHDAVLDNI---LYaRAYTSEHQMELLDYVAAKFHEEAVfRLLIIDSIMALFRVDFSG--RGELAERQQKLAQMLS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 241 SLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgsscviaalGNTWSHSVNTRLILQYLDSERRQI 320
Cdd:cd19514 151 RLQKISEEYNVAVFITNQVTADPGAAMTFQADPKKPIG------------------GHILAHASTTRISLRKGRGEERIA 212
                       250       260
                ....*....|....*....|..
gi 19924117 321 LIAKSPLAPFTSFVYTIKEEGL 342
Cdd:cd19514 213 KIYDSPDLPENEATFAITAGGI 234
archRadA cd19515
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ...
83-343 2.11e-34

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: 126.32  E-value: 2.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpR 162
Cdd:cd19515   1 ISTGSKELDKLLGGGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPPEEGGLNGKAVYIDTENTFRPERIMQMAKA---L 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 YFNTEEKLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG--IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREAS 240
Cdd:cd19515  78 GLDPDEVL----DNIYVARAYNSNHQMLLVEKA-EDLIKEGnnIKLLIVDSLTSHFRAEYVG--RGTLAERQQKLNKHLH 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 241 SLKYLAEEFSIPVILTNQitthlsgalasqadlVSPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQI 320
Cdd:cd19515 151 DLHRLADLYNIAVLVTNQ---------------VMAKPDAFFGDPTQ------AIGGHILGHAATFRVYLRKGKGGKRIA 209
                       250       260
                ....*....|....*....|...
gi 19924117 321 LIAKSPLAPFTSFVYTIKEEGLV 343
Cdd:cd19515 210 RLVDSPHLPEGEAVFRITEKGIE 232
radA PRK04301
DNA repair and recombination protein RadA; Validated
10-259 2.18e-34

DNA repair and recombination protein RadA; Validated


Pssm-ID: 235273 [Multi-domain]  Cd Length: 317  Bit Score: 128.46  E-value: 2.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   10 GLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACA-PKMQTAYGIKAQRSadfSPAFLSTTLS 88
Cdd:PRK04301  13 GVGPATAEKLREAGYDTVEAIAVASPKELSEAAGIGESTAAKIIEAAREAADiGGFETALEVLERRK---NVGKITTGSK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   89 ALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpRYFNTEE 168
Cdd:PRK04301  90 ELDELLGGGIETQSITEFYGEFGSGKTQICHQLAVNVQLPEEKGGLEGKAVYIDTEGTFRPERIEQMAEA---LGLDPDE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  169 KLlltsSKVHLYRELTCDEVLQRIESLeEEIISKG--IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLA 246
Cdd:PRK04301 167 VL----DNIHVARAYNSDHQMLLAEKA-EELIKEGenIKLVIVDSLTAHFRAEYVG--RGNLAERQQKLNKHLHDLLRLA 239
                        250
                 ....*....|...
gi 19924117  247 EEFSIPVILTNQI 259
Cdd:PRK04301 240 DLYNAAVVVTNQV 252
recomb_radA TIGR02236
DNA repair and recombination protein RadA; This family consists exclusively of archaeal RadA ...
34-343 3.04e-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: 122.54  E-value: 3.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    34 SPLELMKVTGLSyRGVHELLCMVSRACAP--KMQTAYGIKAQRSadfSPAFLSTTLSALDEALHGGVACGSLTEITGPPG 111
Cdd:TIGR02236  30 SPKELSEIAGIS-EGTAAKIIQAARKAADlgGFETADDVLERRK---TIGKITTGSKELDELLGGGIETQAITEVFGEFG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   112 CGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpRYFNTEEKLlltsSKVHLYRELTCDEVLQR 191
Cdd:TIGR02236 106 SGKTQICHQLAVNVQLPEEKGGLGGKAVYIDTENTFRPERIMQMAEA---RGLDPDEVL----KNIYVARAYNSNHQMLL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   192 IESLeEEIISKG---IKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQitthlsgala 268
Cdd:TIGR02236 179 VEKA-EDLIKELnnpVKLLIVDSLTSHFRAEYVG--RGALAERQQKLNKHLHDLLRLADLYNAAVVVTNQ---------- 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19924117   269 sqadlVSPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQILIAKSPLAPFTSFVYTIKEEGLV 343
Cdd:TIGR02236 246 -----VMARPDAFFGDPTR------PIGGHILGHAATFRVYLRKGKGDKRIARLVDSPHLPEGEAVFRITEKGIE 309
Rad51D cd19489
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ...
96-325 1.17e-31

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: 118.12  E-value: 1.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  96 GGVACGSLTEITGPPGCGKTQFCimMSILATLPTNMGgleGAVVYIDTESAFSAERLVEIAESRfpryFNTEEKLLLTSS 175
Cdd:cd19489   2 GGLRTGEITELVGESSSGKTQLC--LTAAANVASRSG---QNVLYIDTKSSFSARRLAQILKSR----AQDAEEIDKALQ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 176 KVHLYRELTCDEVLQRIESL------EEEIISKGIKLVILDSVASVVRKEFDA--QLQGNLkernkFLAREASSLKYLAE 247
Cdd:cd19489  73 RIRVVRVFDPYELLDLLEELrntlsqQQENLYSRLKLVIIDSLSALISPLLGGskHSEGHA-----LLASLARLLKKLAA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 248 EFSIPVILTNQITThlsgalasqadlvspaddlSLSEGTSGSSCviAALGNTWSHSVNTRLILQYLD-----SERRQILI 322
Cdd:cd19489 148 EYQIAVLVTNLTVR-------------------GGDGGQQGSTK--PALGEYWESVPSTRLLLSRDEndpeeSGVCTATL 206

                ...
gi 19924117 323 AKS 325
Cdd:cd19489 207 LKS 209
radB PRK09361
DNA repair and recombination protein RadB; Provisional
83-261 5.58e-31

DNA repair and recombination protein RadB; Provisional


Pssm-ID: 236482 [Multi-domain]  Cd Length: 225  Bit Score: 116.89  E-value: 5.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLptnmggLEGAVVYIDTESaFSAERLVEIAESRFpr 162
Cdd:PRK09361   5 LPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAK------NGKKVIYIDTEG-LSPERFKQIAGEDF-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  163 yfnteEKLLltsSKVHLYRELTCDEVLQRIESLeEEIISKGIKLVILDSVASVVRKEFDAQLQGnlKERNKFLAREASSL 242
Cdd:PRK09361  76 -----EELL---SNIIIFEPSSFEEQSEAIRKA-EKLAKENVGLIVLDSATSLYRLELEDEEDN--SKLNRELGRQLTHL 144
                        170
                 ....*....|....*....
gi 19924117  243 KYLAEEFSIPVILTNQITT 261
Cdd:PRK09361 145 LKLARKHDLAVVITNQVYS 163
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
83-261 4.92e-30

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: 113.95  E-value: 4.92e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILAtlpTNMGGLegaVVYIDTEsAFSAERLVEIAESRFPR 162
Cdd:cd01394   1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEA---AKQGKK---VVYIDTE-GLSPERFQQIAGERFES 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 yfnteeklllTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEfdaqlQGNLKERNKFLAREASSL 242
Cdd:cd01394  74 ----------IASNIIVFEPYSFDEQGVAIQEAEKLLKSDKVDLVVVDSATALYRLE-----LGDDSEANRELSRQMSKL 138
                       170
                ....*....|....*....
gi 19924117 243 KYLAEEFSIPVILTNQITT 261
Cdd:cd01394 139 LSIARKYDIPVVITNQVYS 157
PLN03187 PLN03187
meiotic recombination protein DMC1 homolog; Provisional
5-343 9.85e-30

meiotic recombination protein DMC1 homolog; Provisional


Pssm-ID: 215620 [Multi-domain]  Cd Length: 344  Bit Score: 116.42  E-value: 9.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    5 KLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSadfSPAFLS 84
Cdd:PLN03187  33 KLISQGINAGDVKKLQDAGIYTCNGLMMHTKKNLTGIKGLSEAKVDKICEAAEKLLNQGFITGSDALLKRK---SVVRIT 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   85 TTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESrfpryF 164
Cdd:PLN03187 110 TGSQALDELLGGGIETRCITEAFGEFRSGKTQLAHTLCVTTQLPTEMGGGNGKVAYIDTEGTFRPDRIVPIAER-----F 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  165 NTEEKLLLtsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAqlQGNLKERNKFLAREASSLKY 244
Cdd:PLN03187 185 GMDADAVL--DNIIYARAYTYEHQYNLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTG--RGELAERQQKLAQMLSRLTK 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  245 LAEEFSIPVILTNQItthlsgalasQADlvsPADDLSLSEGTSgsscviAALGNTWSHSVNTRLILQYLDSERRQILIAK 324
Cdd:PLN03187 261 IAEEFNVAVYMTNQV----------IAD---PGGGMFISDPKK------PAGGHVLAHAATIRLMLRKGKGEQRVCKVFD 321
                        330
                 ....*....|....*....
gi 19924117  325 SPLAPFTSFVYTIKEEGLV 343
Cdd:PLN03187 322 APNLPEAEAEFQITSGGIM 340
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
90-261 1.98e-28

DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).


Pssm-ID: 274047 [Multi-domain]  Cd Length: 209  Bit Score: 109.81  E-value: 1.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    90 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATlptnmgGLEGAVVYIDTEsAFSAERLVEIAESRFPRYFnteek 169
Cdd:TIGR02237   1 IDELLGGGVERGTITQIYGPPGSGKTNICMILAVNAA------RQGKKVVYIDTE-GLSPERFKQIAEDRPERAL----- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   170 llltsSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEfdaqLQGNLKERNKFLAREASSLKYLAEEF 249
Cdd:TIGR02237  69 -----SNFIVFEVFDFDEQGVAIQKTSKFIDRDSASLVVVDSFTALYRLE----LSDDRISRNRELARQLTLLLSLARKK 139
                         170
                  ....*....|..
gi 19924117   250 SIPVILTNQITT 261
Cdd:TIGR02237 140 NLAVVITNQVYT 151
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
101-311 7.05e-23

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: 95.11  E-value: 7.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 101 GSLTEITGPPGCGKTQFCIMMSILATLPTN-----MGGLEGAVVYIDTESAFSAERLVEIAESRF----------PRYFN 165
Cdd:cd19490   1 GDVIEITGPSGSGKTELLYHLAARCILPSSwggvpLGGLEAAVVFIDTDGRFDILRLRSILEARIraaiqaanssDDEED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 166 TEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIIS----KGIKLVILDSVAS---VVRKEFDAQLQGNLKERNkFLARE 238
Cdd:cd19490  81 VEEIARECLQRLHIFRCHSSLQLLATLLSLENYLLSlsanPELGLLLIDSISAfywQDRFSAELARAAPLLQEA-ALRAI 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19924117 239 ASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSgsscviaALGNTWSHSVNTRLILQ 311
Cdd:cd19490 160 LRELRRLRRRFQLVVIATKQALFPGKSASTDNPAANNAVSKASAPSHRE-------YLPRPWQRLVTHRLVLS 225
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
83-344 6.87e-12

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: 64.21  E-value: 6.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILATlptnmGGLEGA-VVYIDTESafSAERLVEIAESRFP 161
Cdd:cd01124   1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFG--LQFLYA-----GAKNGEpGLFFTFEE--SPERLLRNAKSFGW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 162 --RYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESleeEIISKGIKLVILDSVASvvrkefdaqLQGNLKERNKFLAREA 239
Cdd:cd01124  72 dfDEMEDEGKLIIVDAPPTEAGRFSLDELLSRILS---IIKSFKAKRVVIDSLSG---------LRRAKEDQMRARRIVI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 240 SSLKYLAEEFsIPVILTNQITTHLSGALASQADLVSPADdlslsegtsgssCVIaalgntwshsvntRLILQYLDSE-RR 318
Cdd:cd01124 140 ALLNELRAAG-VTTIFTSEMRSFLSSESAGGGDVSFIVD------------GVI-------------LLRYVEIEGElRR 193
                       250       260
                ....*....|....*....|....*...
gi 19924117 319 QILIAKSPLAPF--TSFVYTIKEEGLVL 344
Cdd:cd01124 194 TIRVLKMRGTGHdtGTHPFEITDKGIVV 221
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
83-344 1.83e-11

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 63.01  E-value: 1.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCimMSILAtlptnmgglEGA-----VVYIDTESafSAERLVEIAE 157
Cdd:COG0467   2 VPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLA--LQFLA---------EGLrrgekGLYVSFEE--SPEQLLRRAE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 158 SrfpryFNTEEKLLLTSSKVHL------YRELTCDEVLQRIeslEEEIISKGIKLVILDSVASVVRkefdaqLQGNLKER 231
Cdd:COG0467  69 S-----LGLDLEEYIESGLLRIidlspeELGLDLEELLARL---REAVEEFGAKRVVIDSLSGLLL------ALPDPERL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 232 NKFLAReassLKYLAEEFSIPVILTNQITTHLSgalasqadlvspaddlslsegtsgsscviAALGNTWSHSVNTRLILQ 311
Cdd:COG0467 135 REFLHR----LLRYLKKRGVTTLLTSETGGLED-----------------------------EATEGGLSYLADGVILLR 181
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 19924117 312 YLDSE---RRQILIAKSPLAPF--TSFVYTIKEEGLVL 344
Cdd:COG0467 182 YVELGgelRRALSVLKMRGSAHdrTIREFEITDGGIEV 219
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
101-335 7.72e-10

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 59.14  E-value: 7.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 101 GSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLE---GAVVYIDTESAFSA--ERLVEIAESRFPRYFNTEEKLLLTSs 175
Cdd:COG3598  13 GGVTLLAGPPGTGKSFLALQLAAAVAAGGPWLGRRvppGKVLYLAAEDDRGElrRRLKALGADLGLPFADLDGRLRLLS- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 176 kvhLYRELTCDEVLQRiesLEEEIISKGIKLVILDSVASVvrkefdaqLQGNLKERN---KFLAReassLKYLAEEFSIP 252
Cdd:COG3598  92 ---LAGDLDDTDDLEA---LERAIEEEGPDLVVIDPLARV--------FGGDENDAEemrAFLNP----LDRLAERTGAA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 253 VILtnqI--TTHLSGALASQadlvspaddlslsEGTSGSScviaALGNtwshSVNTRLILQYL-DSERRQILIAKSPLAP 329
Cdd:COG3598 154 VLL---VhhTGKGGAGKDSG-------------DRARGSS----ALRG----AARSVLVLSREkGEDLRVLTRAKSNYGP 209

                ....*.
gi 19924117 330 FTSFVY 335
Cdd:COG3598 210 EIALRW 215
RecA COG0468
RecA/RadA recombinase [Replication, recombination and repair];
84-219 2.23e-09

RecA/RadA recombinase [Replication, recombination and repair];


Pssm-ID: 440236 [Multi-domain]  Cd Length: 351  Bit Score: 58.26  E-value: 2.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  84 STTLSALDEAL-HGGVACGSLTEITGPPGCGKTQFCimMSILATLpTNMGGLegaVVYIDTESAFS---AERL-VEIaes 158
Cdd:COG0468  45 STGSLALDIALgVGGLPRGRIVEIYGPESSGKTTLA--LHAIAEA-QKAGGI---AAFIDAEHALDpeyAKKLgVDI--- 115
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19924117 159 rfpryfnteEKLLLTSSKvhlyrelTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKE 219
Cdd:COG0468 116 ---------DNLLVSQPD-------TGEQALEIAETL---VRSGAVDLIVVDSVAALVPKA 157
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
83-268 9.26e-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: 55.62  E-value: 9.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTqfcimmSILATLPTNMGGLEGAVVYIdtesafSAERLVEIAESRFPR 162
Cdd:cd01121  64 ISTGIGELDRVLGGGLVPGSVVLIGGDPGIGKS------TLLLQVAARLAQRGGKVLYV------SGEESLSQIKLRAER 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 yfnteekLLLTSSKVHLYREltcdevlQRIESLEEEIISKGIKLVILDSVASVVRKEFD------AQLqgnlkernkfla 236
Cdd:cd01121 132 -------LGLGSDNLYLLAE-------TNLEAILAEIEELKPSLVVIDSIQTVYSPELTsspgsvSQV------------ 185
                       170       180       190
                ....*....|....*....|....*....|...
gi 19924117 237 RE-ASSLKYLAEEFSIPVILTNQITThlSGALA 268
Cdd:cd01121 186 REcAAELLRLAKETGIPVFLVGHVTK--DGAIA 216
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
90-266 1.80e-07

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 51.48  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    90 LDEALHGGVACGSLTEITGPPGCGKTQFCIMMSIlatlptnmgglEGAV------VYIDTESafSAERLVEIAES---RF 160
Cdd:pfam06745   8 LDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLY-----------NGALkygepgVFVTLEE--PPEDLRENARSfgwDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   161 PRYFNtEEKLL---LTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLqgnlkeRNKFLAr 237
Cdd:pfam06745  75 EKLEE-EGKLAiidASTSGIGIAEVEDRFDLEELIERLREAIREIGAKRVVIDSITTLFYLLKPAVA------REILRR- 146
                         170       180
                  ....*....|....*....|....*....
gi 19924117   238 eassLKYLAEEFSIPVILTNQITTHLSGA 266
Cdd:pfam06745 147 ----LKRVLKGLGVTAIFTSEKPSGEGGI 171
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
82-231 2.30e-07

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: 51.02  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  82 FLSTTLSALDEAL-HGGVACGSLTEITGPPGCGKTQfcIMMSILAtlptNMGGLEGAVVYIDTESAFS---AERL-VEIa 156
Cdd:cd00983   4 VIPTGSLSLDIALgIGGLPRGRIIEIYGPESSGKTT--LALHAIA----EAQKLGGTAAFIDAEHALDpeyAKKLgVDI- 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19924117 157 esrfpryfnteEKLLLTSSKvhlyrelTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKefdAQLQGNLKER 231
Cdd:cd00983  77 -----------DNLLVSQPD-------TGEQALEIADTL---IRSGAVDLIVVDSVAALVPK---AEIEGEMGDS 127
RecA-like_Gp4D_helicase cd19483
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ...
106-264 4.33e-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: 50.26  E-value: 4.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 106 ITGPPGCGKTQFC--IMMSILATLPTNMGglegavvYIDTESAF--SAERLV-------EIAESRFPRYFNTEEKLLLT- 173
Cdd:cd19483   3 IGAGSGIGKSTIVreLAYHLITEHGEKVG-------IISLEESVeeTAKGLAgkhlgkpEPLELPRDDITEEEEDDAFDn 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 174 ---SSKVHLYRE---LTCDEVLQRIESLeeeIISKGIKLVILDSVASVVRKEfdaqlqgNLKERNKFLAREASSLKYLAE 247
Cdd:cd19483  76 elgSGRFFLYDHfgsLDWDNLKEKIRYM---VKVLGCKVIVLDHLTILVSGL-------DSSDERKELDEIMTELAALVK 145
                       170
                ....*....|....*..
gi 19924117 248 EFSIPVILTNqittHLS 264
Cdd:cd19483 146 ELGVTIILVS----HLR 158
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
101-268 5.25e-07

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.52  E-value: 5.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    101 GSLTEITGPPGCGKTQfcIMMSILATLPTNMGGlegaVVYIDTESAFSAERLVEIAESRFPRYFNTeekllltsskvhly 180
Cdd:smart00382   2 GEVILIVGPPGSGKTT--LARALARELGPPGGG----VIYIDGEDILEEVLDQLLLIIVGGKKASG-------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    181 reltcdEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLareasslkyLAEEFSIPVILTNQIT 260
Cdd:smart00382  62 ------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL---------LKSEKNLTVILTTNDE 126

                   ....*...
gi 19924117    261 THLSGALA 268
Cdd:smart00382 127 KDLGPALL 134
AAA_25 pfam13481
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
77-256 4.45e-06

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: 46.61  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    77 DFSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSI-LAT----LPTNMGGLEGAVVYIDTE-SAFSAE 150
Cdd:pfam13481   9 DVLADGLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAAaVATgkpwLGGPRVPEQGKVLYVSAEgPADELR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   151 RLVEIAESRFPRyfntEEKLLLTSSK--VHLYRELTCDEVLQR-IESLEEEII-SKGIKLVILDSVASVVR-KEFDAqlq 225
Cdd:pfam13481  89 RRLRAAGADLDL----PARLLFLSLVesLPLFFLDRGGPLLDAdVDALEAALEeVEDPDLVVIDPLARALGgDENSN--- 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 19924117   226 gnlKERNKFLAReassLKYLAEEFSIPVILT 256
Cdd:pfam13481 162 ---SDVGRLVKA----LDRLARRTGATVLLV 185
KaiC-like_C cd19487
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ...
83-278 9.74e-06

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: 46.14  E-value: 9.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILAtlptnMGGLEGAVVYI---DTESAFSAERLVEIAESR 159
Cdd:cd19487   1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAA-----AARGERSVLFSfdeSIGTLFERSEALGIDLRA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 160 FpryfntEEKLLLTSSKVHLyRELTCDEVLQRIESleeEIISKGIKLVILDSVASvvrkefdaqLQGNLKERNKFLAREA 239
Cdd:cd19487  76 M------VEKGLLSIEQIDP-AELSPGEFAQRVRT---SVEQEDARVVVIDSLNG---------YLNAMPDERFLILQMH 136
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19924117 240 SSLKYLAEEfSIPVILTNQITTHLSGALASQADLVSPAD 278
Cdd:cd19487 137 ELLSYLNNQ-GVTTLLIVAQHGLLGGDMGTPVDISYLAD 174
RecA pfam00154
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ...
83-259 1.36e-04

recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA repair systems. RecA protein catalyzes an ATP-dependent DNA strand-exchange reaction that is the central step in the repair of dsDNA breaks by homologous recombination.


Pssm-ID: 425488 [Multi-domain]  Cd Length: 262  Bit Score: 42.77  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117    83 LSTTLSALDEALH-GGVACGSLTEITGPPGCGKTQfcIMMSILATLPTNmgglEGAVVYIDTESAFSaerlveiaesrfP 161
Cdd:pfam00154  33 ISTGSLALDIALGiGGYPKGRIIEIYGPESSGKTT--LALHAIAEAQKA----GGTAAFIDAEHALD------------P 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   162 RY-----FNTEEklLLTSSKvhlyreltcDEVLQRIESLEEEIISKGIKLVILDSVASVVRKefdAQLQGNLKERNKFL- 235
Cdd:pfam00154  95 VYakklgVDIDN--LLVSQP---------DTGEQALEIADMLVRSGAIDLIVVDSVAALVPK---AEIEGEMGDSHVGLq 160
                         170       180
                  ....*....|....*....|....*...
gi 19924117   236 AREAS-SLKYLAEEFS---IPVILTNQI 259
Cdd:pfam00154 161 ARLMSqALRKLTGSISksnTTVIFINQI 188
DnaB_C cd00984
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ...
82-274 8.86e-04

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: 40.57  E-value: 8.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  82 FLSTTLSALDEALHGGVAcGSLTEITGPPGCGKTQFCIMMSIlatlptNMGGLEGAVVYIdtesaFSAE--------RLV 153
Cdd:cd00984   1 GLPTGFTDLDKLTGGLQP-GDLIIIAARPSMGKTAFALNIAE------NIALDEGLPVLF-----FSLEmsaeqlaeRLL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 154 eIAESRFPR------YFNTEEKLLLTSSKVHLYRE---------LTCDEVLQRIESLEEEiiSKGIKLVILDSVasvvrk 218
Cdd:cd00984  69 -SSESGVSLsklrtgRLDDEDWERLTAAMGELSELplyiddtpgLTVDEIRAKARRLKRE--HGGLGLIVIDYL------ 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19924117 219 efdaQL-QGNLKERNKFLAREASS--LKYLAEEFSIPVILTNQ-------------ITTHL--SGALASQADLV 274
Cdd:cd00984 140 ----QLiRGSKRAENRQQEVAEISrsLKALAKELNVPVIALSQlnrgvesrtdkrpMLSDLreSGSIEQDADVV 209
KaiC-N cd19485
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ...
83-232 3.46e-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: 38.50  E-value: 3.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117  83 LSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGlegavVYIDTESafSAERLVEIAESrfpr 162
Cdd:cd19485   1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQFLVNGIKEFGEPG-----VFVTFEE--SPEDIIKNMAS---- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117 163 yFNTEEKLLLTSSK---VHLYRELTCDEVLQR------IESLEEEIISKGIKLVILDSV---------ASVVRKEFdAQL 224
Cdd:cd19485  70 -FGWDLPKLVAEGKlliLDASPEPSEEEVTGEydlealLIRIEYAIRKIGAKRVSLDSLeavfsglsdSAVVRAEL-LRL 147

                ....*...
gi 19924117 225 QGNLKERN 232
Cdd:cd19485 148 FAWLKQKG 155
PRK13853 PRK13853
type IV secretion system protein VirB4; Provisional
103-142 4.22e-03

type IV secretion system protein VirB4; Provisional


Pssm-ID: 139913 [Multi-domain]  Cd Length: 789  Bit Score: 39.07  E-value: 4.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 19924117  103 LTEITGPPGCGKTQFciMMSILATLPTNMGGLEGAVVYID 142
Cdd:PRK13853 428 MTAIFGPIGRGKTTL--MTFILAMLEQSMVDRAGAVVFFD 465
TniB pfam05621
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ...
106-255 4.50e-03

Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein which is involved in Tn5053 mercury resistance transposition. This entry represents a P-loop domain.


Pssm-ID: 428547  Cd Length: 189  Bit Score: 37.57  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19924117   106 ITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERL-VEIAESRFPRYFNTEEKLLLTSSKVHLYRELt 184
Cdd:pfam05621  40 LVGDSNNGKTMIVERFARLHPPTDDEDAEIVPVVVVQMPPKPDEKRLyVAILEALGAPFRPRDRLSKLEQQVLRLLRAV- 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19924117   185 cdevlqriesleeeiiskGIKLVILDsvasvvrkEFDAQLQGNLKERNKFLAreasSLKYLAEEFSIPVIL 255
Cdd:pfam05621 119 ------------------GVRMLIID--------EFHNLLAGSARKQREFLN----VLKSLGNELRIPIVG 159
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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