|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-204 |
4.04e-167 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 463.11 E-value: 4.04e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 1 LAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKT 80
Cdd:PRK09354 11 LEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 81 CAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQAR 160
Cdd:PRK09354 91 AAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQAR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 410369200 161 LMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGN 204
Cdd:PRK09354 171 LMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGN 214
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-204 |
1.78e-163 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 453.86 E-value: 1.78e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 1 LAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKT 80
Cdd:COG0468 14 LEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 81 CAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQAR 160
Cdd:COG0468 94 AAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQAR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 410369200 161 LMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGN 204
Cdd:COG0468 174 LMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGN 217
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-204 |
3.36e-147 |
|
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: 409.48 E-value: 3.36e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 1 LAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKT 80
Cdd:pfam00154 3 LEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 81 CAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQAR 160
Cdd:pfam00154 83 AAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 410369200 161 LMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGN 204
Cdd:pfam00154 163 LMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGR 206
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-204 |
1.64e-146 |
|
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization of homolgous regions of DNA. A segment of ssDNA can be hybridized to another ssDNA region, or to a dsDNA region. ATP is hydrolyzed in the process. Part of the SOS respones, it is regulated by LexA via autocatalytic cleavage. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 162659 [Multi-domain] Cd Length: 321 Bit Score: 409.84 E-value: 1.64e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 1 LAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKT 80
Cdd:TIGR02012 6 LEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 81 CAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQAR 160
Cdd:TIGR02012 86 AAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 410369200 161 LMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGGN 204
Cdd:TIGR02012 166 LMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGN 209
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
27-204 |
2.23e-129 |
|
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: 363.41 E-value: 2.23e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 27 DIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLL 106
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 107 ISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQI 186
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170
....*....|....*...
gi 410369200 187 RMKIGVMFGSPETTTGGN 204
Cdd:cd00983 161 REKIGVMFGNPETTTGGN 178
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-203 |
3.11e-98 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 301.63 E-value: 3.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 1 LAAALGQIEKQFG*GSIMRLGDSKTMDIEAISTGSLSLDVALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKT 80
Cdd:PRK09519 11 LELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 81 CAFVDAEHALDPIYAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIEGEMGDSHVGLQAR 160
Cdd:PRK09519 91 AAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQAR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 410369200 161 LMSQALRKLTANIKNANCLCIFINQIRMKIGVMFGSPETTTGG 203
Cdd:PRK09519 171 LMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGG 213
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
50-204 |
8.67e-48 |
|
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.
Pssm-ID: 410881 [Multi-domain] Cd Length: 185 Bit Score: 154.82 E-value: 8.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 50 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPIYA-----------AKLGVNVDDLLISQPDTGEQALE 118
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 119 ICDMLVRSNA----VDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIGVMF 194
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170
....*....|.
gi 410369200 195 G-SPETTTGGN 204
Cdd:cd01393 161 GaSLVPPALGN 171
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
31-191 |
1.76e-17 |
|
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: 76.97 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEhALDP-----IYAAKLGVNVDDL 105
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 106 LISQP-DTGEQALEICDM--LVRSNAVDVIIVDSVAALTpKAEiegEMGDShvGLQARLMSQaLRKLTANIKNANCLCIF 182
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151
|
....*....
gi 410369200 183 INQIRMKIG 191
Cdd:cd01394 152 TNQVYSDID 160
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
31-198 |
4.99e-15 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 70.71 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPI--YAAKLGVNVDDLL-- 106
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 107 ----ISQPDTGEQALEICDML------VRSNAVDVIIVDSVAALtpkaeiEGEMGDShvglqaRLMSQALRKLTANIKNA 176
Cdd:COG0467 81 gllrIIDLSPEELGLDLEELLarlreaVEEFGAKRVVIDSLSGL------LLALPDP------ERLREFLHRLLRYLKKR 148
|
170 180
....*....|....*....|..
gi 410369200 177 NCLCIFINQIRMKIGVMFGSPE 198
Cdd:COG0467 149 GVTTLLTSETGGLEDEATEGGL 170
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
38-191 |
7.67e-13 |
|
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: 64.36 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 38 LDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEhALDP-----IYAAKLGVNVDDLLISQP-D 111
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPerfkqIAEDRPERALSNFIVFEVfD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 112 TGEQALEICDM--LVRSNAVDVIIVDSVAALTpKAEIEGEMGDSHVGLQARLmsQALRKLTANIKNAnclCIFINQIRMK 189
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLARKKNLA---VVITNQVYTD 152
|
..
gi 410369200 190 IG 191
Cdd:TIGR02237 153 VN 154
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
30-144 |
2.66e-12 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 63.41 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 30 AISTGSLSLDVALGIGGLPCGRIVEIYGPE-SSGKTTLTLQVIAEAQKKGKTCAFVDAEHALdpiYA---AKLGVNVDDL 105
Cdd:COG4544 28 VLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPERL 104
|
90 100 110
....*....|....*....|....*....|....*....
gi 410369200 106 LISQPDTGEQALEICDMLVRSNAVDVIIVDsVAALTPKA 144
Cdd:COG4544 105 LLVRARRPADALWAAEEALRSGACGAVVAW-LERLDLTA 142
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
26-204 |
5.46e-12 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 63.36 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 26 MDIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQK------KGKTCAFVDAE------------ 87
Cdd:PRK04301 79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEgtfrperieqma 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 88 --------HALDPIYAAKlGVNVDD--LLIsqpdtgEQALEICDmlvRSNAVDVIIVDSVAALTpKAEiegemgdsHVGL 157
Cdd:PRK04301 158 ealgldpdEVLDNIHVAR-AYNSDHqmLLA------EKAEELIK---EGENIKLVIVDSLTAHF-RAE--------YVGR 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 410369200 158 ------QARLMSQ--ALRKLtANIKnaNCLCIFINQIRMKIGVMFGSPETTTGGN 204
Cdd:PRK04301 219 gnlaerQQKLNKHlhDLLRL-ADLY--NAAVVVTNQVMARPDAFFGDPTQPIGGH 270
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
28-140 |
2.20e-11 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 60.65 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 28 IEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEhALDPIYAAKL-GVNVDDLL 106
Cdd:PRK09361 2 DERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEELL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 410369200 107 ----ISQP-DTGEQALEICDM--LVRSNaVDVIIVDSVAAL 140
Cdd:PRK09361 80 sniiIFEPsSFEEQSEAIRKAekLAKEN-VGLIVLDSATSL 119
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
31-204 |
9.11e-10 |
|
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: 56.22 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKK------GKTCAFVDAEHALDP----IYAAKLGV 100
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLPpeegglNGKAVYIDTENTFRPerimQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 101 NVDDLL-----ISQPDTGEQAL---EICDMLVRSNAVDVIIVDSVAALTpKAEI--EGEMGDSHVGLqARLMSQALRklT 170
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYvgRGTLAERQQKL-NKHLHDLHR--L 155
|
170 180 190
....*....|....*....|....*....|....*
gi 410369200 171 ANIKNAnclCIFI-NQIRMKIGVMFGSPETTTGGN 204
Cdd:cd19515 156 ADLYNI---AVLVtNQVMAKPDAFFGDPTQAIGGH 187
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
39-191 |
3.53e-09 |
|
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: 54.63 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 39 DVALGiGGLPCGRIVEIYGPESSGKT----TLTLQVIAEAQKKGKT--CAFVDAEHALDP-----IYAAKLGVN------ 101
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDggVLYIDTESKFSAerlaeIAEARFPEAfsgfme 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 102 --------VDDLLISQPDTGEQALEICDML---VRSNAVDVIIVDSVAALTPKaeiegEMGDSHVGLQARlmSQALRKLT 170
Cdd:cd19493 80 eneraeemLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180
....*....|....*....|....*
gi 410369200 171 ANIKN-ANCLCIFI---NQIRMKIG 191
Cdd:cd19493 153 SSLKRlAEEFRIAVlvtNQATTHFG 177
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
31-198 |
6.87e-09 |
|
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: 53.81 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPIY--AAKLGVNVD----- 103
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFDemede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 104 -DLLISQPDTGEQALEICDML-------VRSNAVDVIIVDSVAALTPKAEiegemgdshvglQARLMSQALRKLTANIKN 175
Cdd:cd01124 80 gKLIIVDAPPTEAGRFSLDELlsrilsiIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
|
170 180
....*....|....*....|....*.
gi 410369200 176 ANCLCIFINQ---IRMKIGVMFGSPE 198
Cdd:cd01124 148 AGVTTIFTSEmrsFLSSESAGGGDVS 173
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-191 |
9.68e-09 |
|
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: 51.99 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 50 GRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPIYAAKLGVNVDDLLISqpDTGEQALEICDMLVRSNAV 129
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410369200 130 DVIIVDSVAALTPKaeiegemgdshVGLQARLMSQALRKLTANIKNANCLCIFINQIRMKIG 191
Cdd:smart00382 80 DVLILDEITSLLDA-----------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
31-204 |
1.26e-08 |
|
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: 53.07 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQK-----KGKtCAFVDAEHALDPI----YAAKLG 99
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLemgggEGK-ALYIDTEGTFRPErlvaIAERYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 100 VNVDDLLISQP-------DTGEQALEICDMLVRSNAVDVIIVDSVAALTpKAEIEGEmGDshvgLQARLM--SQALRKLt 170
Cdd:pfam08423 97 LDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTL- 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 410369200 171 ANIKNANCLCIFI-NQIRMKIG---VMF-GSPETTTGGN 204
Cdd:pfam08423 170 QRLADEFGVAVVItNQVVAQVDgaaGMFsGDPKKPIGGH 208
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
31-204 |
1.31e-08 |
|
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: 52.92 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKtCAFVDAEHALDPI----YAAKLG 99
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVtcqlpIDRGGGEGK-AIYIDTEGTFRPErlraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 100 VNVDDLL----ISQPDTGEQALEICD----MLVRSnAVDVIIVDSVAALTPKAEI-EGEMGDSHVGLqARLMSQALRklt 170
Cdd:cd01123 79 LDPDDVLdnvaYARAFNSDHQTQLLDqaaaMMVES-RFKLLIVDSATALYRTDYSgRGELSARQMHL-AKFLRMLQR--- 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 410369200 171 anIKNANCLCIFI-NQIRMKIG---VMFGSPETTTGGN 204
Cdd:cd01123 154 --LADEFGVAVVVtNQVVAQVDgamMFAADPKKPIGGN 189
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
31-188 |
2.92e-08 |
|
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.
Pssm-ID: 429095 [Multi-domain] Cd Length: 231 Bit Score: 51.86 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDvALGIGGLPCGRIVEIYGPESSGKTTLTLQVIAE-AQKKGKTCAFVDA-EHALDPIYAAK-LGVNVDDLL- 106
Cdd:pfam06745 1 VKTGIPGLD-EILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLRENARsFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 107 --------ISQPDTGEQALEICDML----------VRSNAVDVIIVDSVAALtpkAEIEGEMgdshvglQARlmsQALRK 168
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180
....*....|....*....|
gi 410369200 169 LTANIKNANCLCIFINQIRM 188
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPS 166
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
31-140 |
6.16e-08 |
|
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: 51.20 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQKK-----GKTCaFVDAEHALDP----IYAAKLG 99
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmggggGKVA-YIDTEGTFRPdrirPIAERFG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 410369200 100 VN----VDDLLISQPDTGEQALEICDMLVRSNAVD----VIIVDSVAAL 140
Cdd:cd19514 79 VDhdavLDNILYARAYTSEHQMELLDYVAAKFHEEavfrLLIIDSIMAL 127
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
18-137 |
1.04e-07 |
|
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: 50.61 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 18 MRLGDSKTMDIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPI--YA 95
Cdd:cd01121 51 LPLSDVEAEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 410369200 96 AKLGVNVDDLLIsqpdTGEQALE-ICDMLVRSNAvDVIIVDSV 137
Cdd:cd01121 130 ERLGLGSDNLYL----LAETNLEaILAEIEELKP-SLVVIDSI 167
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
38-186 |
2.41e-07 |
|
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: 49.60 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 38 LDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQ------KKGKTCAFVDAEHAL----------------DPIYA 95
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpkryHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 96 AKLGVNVddLLISQPDTgeQALEICDM-----LVRSNAVDVIIVDSVAALtpkAEIEGEMGDSHVGLQARLMSQALRKLT 170
Cdd:cd19491 80 KNFLDNI--FVEHVADL--ETLEHCLNyqlpaLLERGPIRLVVIDSIAAL---FRSEFDTSRSDLVERAKYLRRLADHLK 152
|
170
....*....|....*.
gi 410369200 171 ANIKNANCLCIFINQI 186
Cdd:cd19491 153 RLADKYNLAVVVVNQV 168
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
27-170 |
4.11e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 49.35 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 27 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKtCAFVDAEHALDP----IYA 95
Cdd:PLN03186 101 EIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVtcqlpLDQGGGEGK-AMYIDTEGTFRPqrliQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 96 AKLGVNVDDLL-----ISQPDTGEQA---LEICDMLVRSNaVDVIIVDSVAALTpKAEIEGEmGDshvgLQAR--LMSQA 165
Cdd:PLN03186 179 ERFGLNGADVLenvayARAYNTDHQSellLEAASMMAETR-FALMIVDSATALY-RTEFSGR-GE----LSARqmHLGKF 251
|
....*
gi 410369200 166 LRKLT 170
Cdd:PLN03186 252 LRSLQ 256
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
31-123 |
1.41e-06 |
|
N-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: 410896 [Multi-domain] Cd Length: 225 Bit Score: 46.96 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPI--YAAKLGVNVDDLLI- 107
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELraVALSHGWSLDGIHIf 79
|
90
....*....|....*...
gi 410369200 108 --SQPDTGEQALEICDML 123
Cdd:cd19488 80 elSPSESALDAAQQYTIL 97
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
31-141 |
2.76e-06 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 46.36 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHA----LDPIYAakLGVNVDDLL 106
Cdd:COG2874 3 ISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTtkefIKQMKS--LSYDISDYL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 410369200 107 IS--------QPDTGE----QALEICDMLVRSNA-----VDVIIVDSVAALT 141
Cdd:COG2874 80 LRgrllflpvHPLGFEwnskQRKDLLKRLMKYIAsnlweADVIIIDSLSALL 131
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
31-204 |
1.15e-05 |
|
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: 44.62 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKtCAFVDAEHALDP----IYAAKLG 99
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPerllAIAERYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 100 VNVDDLL-----ISQPDTGEQA---LEICDMLVRSNaVDVIIVDSVAALTpKAEIEGEmGDshvgLQARLM--SQALRKL 169
Cdd:cd19513 79 LNGEDVLdnvayARAYNTDHQMqllIQASAMMAESR-YALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRML 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 410369200 170 TaNIKNANCLCIFI-NQIRMKI--GVMF-GSPETTTGGN 204
Cdd:cd19513 152 Q-RLADEFGVAVVItNQVVAQVdgAAMFaGDPKKPIGGN 189
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
27-147 |
3.39e-05 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 43.04 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 27 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPiYAAK---LGVNVD 103
Cdd:PRK06067 3 KKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKS-YLKQmesVKIDIS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 410369200 104 DLLIS---------------QPDTGEQALEICDMLVRSNAVDVIIVDSVAALTPKAEIE 147
Cdd:PRK06067 81 DFFLWgylrifplntegfewNSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
31-140 |
4.47e-05 |
|
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: 43.23 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAEAQKKGK----TCAFVDAEHALDP----IYAAKLGV 100
Cdd:TIGR02238 78 ITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREMGggngKVAYIDTEGTFRPdrirAIAERFGV 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 410369200 101 N----VDDLLISQPDTGEQALEICDMLVRSNAVD---VIIVDSVAAL 140
Cdd:TIGR02238 157 DpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMAL 203
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
31-140 |
7.15e-05 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 42.68 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAE-----AQKKGKtCAFVDAEHALDP-----IyAAKL 98
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQlpieqGGGEGK-VLYIDTEGTFRPerivqI-AERF 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 410369200 99 GVN----VDDLLISQPDTGEQALE----ICDMLVRSNAVdVIIVDSVAAL 140
Cdd:PTZ00035 177 GLDpedvLDNIAYARAYNHEHQMQllsqAAAKMAEERFA-LLIVDSATAL 225
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
45-74 |
1.14e-04 |
|
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: 41.47 E-value: 1.14e-04
10 20 30
....*....|....*....|....*....|
gi 410369200 45 GGLPCGRIVEIYGPESSGKTTLTLQVIAEA 74
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANV 31
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
27-140 |
1.25e-04 |
|
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: 41.63 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 27 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQV-----IAEAQKKGKtCAFVDAEHALDPI----YA 95
Cdd:TIGR02239 74 EVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVtcqlpIDQGGGEGK-ALYIDTEGTFRPErllaIA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 410369200 96 AKLGVNVDDLLIS-------QPDTGEQALEICDMLVRSNAVDVIIVDSVAAL 140
Cdd:TIGR02239 152 ERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATAL 203
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
50-191 |
2.13e-04 |
|
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: 40.79 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 50 GRIVEIYGPESSGKTTLTLQVIA---------EAQKKGKTCA--FVDAEHALDP-----IYAAKLGVNVDDLLISQPDTG 113
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDIlrlrsILEARIRAAIQAANSSDDEED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 114 -EQALEIC-----------------------DMLVRSNA---VDVIIVDSVAALTPKAEIEGEMGDSHVGLQARLMSQAL 166
Cdd:cd19490 81 vEEIAREClqrlhifrchsslqllatllsleNYLLSLSAnpeLGLLLIDSISAFYWQDRFSAELARAAPLLQEAALRAIL 160
|
170 180
....*....|....*....|....*
gi 410369200 167 RKLTANIKNANCLCIFINQIRMKIG 191
Cdd:cd19490 161 RELRRLRRRFQLVVIATKQALFPGK 185
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
27-203 |
4.07e-04 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 40.15 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 27 DIEAISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTL--TLQVIAE-AQKKGKTC---AFVDAEHALDP----IYAA 96
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQlPTEMGGGNgkvAYIDTEGTFRPdrivPIAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 97 KLGVN----VDDLLISQPDTGEQ---ALEICDMLVRSNAVDVIIVDSVAALTPKAEI-EGEMGDShvglQARLmSQALRK 168
Cdd:PLN03187 183 RFGMDadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQMLSR 257
|
170 180 190
....*....|....*....|....*....|....*..
gi 410369200 169 LTANIKNANCLCIFINQIRMKIG--VMFGSPETTTGG 203
Cdd:PLN03187 258 LTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGG 294
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
52-86 |
4.30e-04 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 40.00 E-value: 4.30e-04
10 20 30
....*....|....*....|....*....|....*
gi 410369200 52 IVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDA 86
Cdd:pfam01637 22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDP 56
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
51-137 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 51 RIVeIYGPESSGKTTLtlqvIAEAQKKgktcAFVDAEHALDPIYAAKLGVnvddllISQPDTGEQALEICDMLVRSNAV- 129
Cdd:pfam13479 4 KIL-IYGPSGIGKTTF----AKTLPKP----LFLDTEKGSKALDGDRFPD------IVIRDSWQDFLDAIDELTAAELAd 68
|
....*....
gi 410369200 130 -DVIIVDSV 137
Cdd:pfam13479 69 yKTIVIDTV 77
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
31-82 |
2.65e-03 |
|
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: 37.66 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 410369200 31 ISTGSLSLDVALGiGGLPCGRIVEIYGPESSGKTTLTLQVIAEAQKKGKTCA 82
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSV 51
|
|
| Grc3 |
COG1341 |
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ... |
44-86 |
3.14e-03 |
|
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440952 Cd Length: 353 Bit Score: 37.69 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 410369200 44 IGGLPCGRIVeIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDA 86
Cdd:COG1341 30 ILSSGPGRIM-VLGPVDSGKSTLTTLLANKLLAEGLKVAIIDA 71
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
47-169 |
3.68e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 37.57 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 47 LPCGRIVEIYGPESSGKTTLTLQV---IAEAQK------KGKTCAFVDAEHALDPI------YAAKLGVNVDDL-----L 106
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLaaaVAAGGPwlgrrvPPGKVLYLAAEDDRGELrrrlkaLGADLGLPFADLdgrlrL 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410369200 107 IS-----QPDTGEQALEicdMLVRSNAVDVIIVDSVAALTPkaeiegemGDSHVGLQARLMSQALRKL 169
Cdd:COG3598 90 LSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFG--------GDENDAEEMRAFLNPLDRL 146
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
39-81 |
3.89e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 37.37 E-value: 3.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 410369200 39 DVALGIgglPCGRIVEIYGPESSGKTTLtLQVIA--EAQKKGKTC 81
Cdd:PRK10851 20 DISLDI---PSGQMVALLGPSGSGKTTL-LRIIAglEHQTSGHIR 60
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
51-69 |
5.85e-03 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 36.34 E-value: 5.85e-03
|
| AAA_22 |
pfam13401 |
AAA domain; |
51-144 |
6.03e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.40 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410369200 51 RIVEIYGPESSGKTTLTLQVIAEAQKKGKTCAFVDAEHALDPI-YAAKLGVNVDDLLISQPDTGEQALEICDMLVRSNAV 129
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKdLLRALLRALGLPLSGRLSKEELLAALQQLLLALAVA 85
|
90
....*....|....*
gi 410369200 130 DVIIVDSVAALTPKA 144
Cdd:pfam13401 86 VVLIIDEAQHLSLEA 100
|
|
| |
