|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
1-302 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 666.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 1 AALSQIERSFGKGSIMKLGSNEnVVEVETISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGIC 80
Cdd:PRK09354 13 AALKQIEKQFGKGSIMRLGDDA-AMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 81 AFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIEGEMGDSLPGLQARL 160
Cdd:PRK09354 92 AFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 161 MSQALRKLTASISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNK 240
Cdd:PRK09354 172 MSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNK 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513281 241 MAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFLRDN 302
Cdd:PRK09354 252 VAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKEN 313
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
1-302 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 648.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 1 AALSQIERSFGKGSIMKLGSNENVvEVETISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGIC 80
Cdd:COG0468 16 AALSQIEKQFGKGSIMRLGDKARQ-DVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 81 AFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIEGEMGDSLPGLQARL 160
Cdd:COG0468 95 AFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 161 MSQALRKLTASISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNK 240
Cdd:COG0468 175 MSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNK 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513281 241 MAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFLRDN 302
Cdd:COG0468 255 VAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKEN 316
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
1-302 |
0e+00 |
|
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: 588.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 1 AALSQIERSFGKGSIMKLGsNENVVEVETISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGIC 80
Cdd:TIGR02012 8 AALAQIEKQFGKGSIMRLG-EKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 81 AFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIEGEMGDSLPGLQARL 160
Cdd:TIGR02012 87 AFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 161 MSQALRKLTASISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNK 240
Cdd:TIGR02012 167 MSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNK 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513281 241 MAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFLRDN 302
Cdd:TIGR02012 247 VAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKEN 308
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
1-259 |
0e+00 |
|
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: 526.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 1 AALSQIERSFGKGSIMKLGSnENVVEVETISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGIC 80
Cdd:pfam00154 5 AALKQIEKQFGKGSIMKLGD-EKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 81 AFVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIEGEMGDSLPGLQARL 160
Cdd:pfam00154 84 AFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 161 MSQALRKLTASISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNK 240
Cdd:pfam00154 164 MSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNK 243
|
250
....*....|....*....
gi 960513281 241 MAPPFKQVEFDIMYGEGVS 259
Cdd:pfam00154 244 VAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
26-260 |
2.23e-173 |
|
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: 478.97 E-value: 2.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYARKLGVDLQNLL 105
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 106 ISQPDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTASISKSKCMVIFINQI 185
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 186 RMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNKMAPPFKQVEFDIMYGEGVSK 260
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
2-240 |
1.27e-115 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 350.93 E-value: 1.27e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 2 ALSQIERSFGKGSIMKLGsNENVVEVETISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICA 81
Cdd:PRK09519 14 AVAQIEKSYGKGSVMRLG-DEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 82 FVDAEHALDPVYARKLGVDLQNLLISQPDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIEGEMGDSLPGLQARLM 161
Cdd:PRK09519 93 FIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLM 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960513281 162 SQALRKLTASISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGAVKEREEVVGNQTRVKVVKNK 240
Cdd:PRK09519 173 SQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
49-217 |
7.61e-54 |
|
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: 173.69 E-value: 7.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 49 GRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYAR-----------KLGVDLQNLLISQPDTGEQALE 117
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLVqileaspsselELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 118 ITDTLVRSGA----VDILVVDSVAALTPRAEIEGEMGDSLPGLQARLMSQALRKLTASISKSKCMVIFINQIRMKIGVMF 193
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 960513281 194 G-SPETTTGGNALKFYASVRLDIRR 217
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
236-302 |
4.15e-22 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 96.32 E-value: 4.15e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 960513281 236 VVKNKMAPPFKQVEFDIMYGEGVSKTGELVDLGVKAGIVEKSGAWFSYNSQRLGQGRENAKTFLRDN 302
Cdd:PRK09519 687 VVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVEN 753
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
30-252 |
5.05e-21 |
|
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: 88.91 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEhALDP-----VYARKLGVDLQNL 104
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTE-GLSPerfqqIAGERFESIASNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 105 LISQP-DTGEQALEITDT--LVRSGAVDILVVDSVAALTpRAEiegEMGDSlpGLQARLMSQaLRKLTASISKSKCMVIF 181
Cdd:cd01394 79 IVFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 960513281 182 INQIRMKIGVMFGSPettTGGNALKfYASvrldirriGAVKEREEVVGNQTRVKVVKNKMAPPFKQVEFDI 252
Cdd:cd01394 152 TNQVYSDIDDDRLKP---VGGTLLE-HWS--------KAIIRLEKSPPGLRRATLEKHRSRPEGQSAGFRI 210
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
28-252 |
1.56e-14 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 71.43 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 28 ETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEhALDPVYARKLGVD-----LQ 102
Cdd:PRK09361 3 ERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIAGEdfeelLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 103 NLLISQP-DTGEQALEITDT--LVRSGaVDILVVDSVAALTpRAEIEGEMGDslpglqarlmSQALRKLTASIS------ 173
Cdd:PRK09361 81 NIIIFEPsSFEEQSEAIRKAekLAKEN-VGLIVLDSATSLY-RLELEDEEDN----------SKLNRELGRQLThllkla 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 174 -KSKCMVIFINQIRMKIGVMFGSPettTGGNALKfYAS---VRLDIRRIGavkEReevvgnqtRVKVVKNKMAPPFKQVE 249
Cdd:PRK09361 149 rKHDLAVVITNQVYSDIDSDGLRP---LGGHTLE-HWSktiLRLEKFRNG---KR--------RATLEKHRSRPEGESAE 213
|
...
gi 960513281 250 FDI 252
Cdd:PRK09361 214 FRI 216
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
37-252 |
3.84e-14 |
|
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: 69.75 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 37 LDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEhALDPVYARKLGVD-----LQNLLISQP-- 109
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDrperaLSNFIVFEVfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 110 -DTGEQALEITDTLVRSGAVDILVVDSVAALTpRAEIEGEMGDSLPGLQARLmsQALRKLTAsisKSKCMVIFINQIRMK 188
Cdd:TIGR02237 79 fDEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLAR---KKNLAVVITNQVYTD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 189 IGVMFGSPettTGGNALKFYASVRLDIRRigavkereevvGNQTRVKVV-KNKMAPPFKQVEFDI 252
Cdd:TIGR02237 153 VNNGTLRP---LGGHLLEHWSKVILRLEK-----------FRGRRLATLeKHRSRPEGESVYFRI 203
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
26-217 |
1.96e-13 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 69.52 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQ---KKGGI---CAFVDAE------------- 86
Cdd:PRK04301 80 NVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQlpeEKGGLegkAVYIDTEgtfrperieqmae 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 87 -HALDP-------VYARKLGVDLQNLLIsqpdtgEQALEitdtLVRSG-AVDILVVDSVAALTpRAEIEGEmgDSLPGLQ 157
Cdd:PRK04301 159 aLGLDPdevldniHVARAYNSDHQMLLA------EKAEE----LIKEGeNIKLVIVDSLTAHF-RAEYVGR--GNLAERQ 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513281 158 ARLMSQ--ALRKLtASISKskCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRR 217
Cdd:PRK04301 226 QKLNKHlhDLLRL-ADLYN--AAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
27-143 |
2.15e-13 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 68.03 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 27 VETISTGSLSLDIALGIGGLPKGRIVEIYGPE-SSGKTTLALQTIAEAQKKGGICAFVDAEHALdpvYA---RKLGVDLQ 102
Cdd:COG4544 26 RAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApglAAAGLDPE 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 960513281 103 NLLISQPDTGEQALEITDTLVRSGAVDILVVDsVAALTPRA 143
Cdd:COG4544 103 RLLLVRARRPADALWAAEEALRSGACGAVVAW-LERLDLTA 142
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
30-197 |
4.82e-13 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 66.86 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPV--YARKLGVDLQ----- 102
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLEeyies 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 103 -NLLISQPDTGEQALEITDTL------VRSGAVDILVVDSVAALtpRAEIEGEMgdslpglQARLMsqaLRKLTASISKS 175
Cdd:COG0467 81 gLLRIIDLSPEELGLDLEELLarlreaVEEFGAKRVVIDSLSGL--LLALPDPE-------RLREF---LHRLLRYLKKR 148
|
170 180
....*....|....*....|..
gi 960513281 176 KCMVIFINQIRMKIGVMFGSPE 197
Cdd:COG0467 149 GVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
30-217 |
2.61e-12 |
|
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: 65.24 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKT----TLAL--QTIAEAQKKGGICAFVDAEHALDPV----YARKLGV 99
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTqlchTLAVtcQLPIDRGGGEGKAIYIDTEGTFRPErlraIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 100 D----LQNLLISQPDTGEQALEITD---TLVRSGAVDILVVDSVAALTpRAEIEGEmGDslpgLQARLM--SQALRKLTA 170
Cdd:cd01123 80 DpddvLDNVAYARAFNSDHQTQLLDqaaAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 960513281 171 SISKSKCMVIFINQIRMKIG---VMFGSPETTTGGNALKFYASVRLDIRR 217
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK 203
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
30-217 |
3.10e-12 |
|
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: 65.08 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQK---KGGI---CAFVDAEHALDP----VYARKLGV 99
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeEGGLngkAVYIDTENTFRPerimQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 100 D----LQNLLISQP-DTGEQAL---EITDTLVRSGAVDILVVDSVAALTpRAEIEGEmgDSLPGLQARLmSQALRKLTAS 171
Cdd:cd19515 80 DpdevLDNIYVARAyNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 960513281 172 ISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRR 217
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK 201
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
30-224 |
2.49e-11 |
|
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: 62.26 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDiALGIGGLPKGRIVEIYGPESSGKTTLALQ-TIAEAQKKGGICAFVDA-EHALDPVY-ARKLGVDLQNLL- 105
Cdd:pfam06745 1 VKTGIPGLD-EILKGGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDLREnARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 106 --------ISQPDTGEQALEITDTL----------VRSGAVDILVVDSVAALtprAEIEGEMgdslpglQARlmsQALRK 167
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 168 LTASISKSKCMVIFINQIRMKigvmfgspETTTGGNALKFYAS---VRLDIRRIGAVKER 224
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEEERVR 198
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
30-217 |
4.48e-11 |
|
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: 61.60 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQ------KKGGICAFVDAEHALDP----VYARKLGV 99
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLSHTLCVTAQlpgsmgGGGGKVAYIDTEGTFRPdrirPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 100 D----LQNLLISQPDTGEQALEITDTL----VRSGAVDILVVDSVAAL-----TPRaeieGEMGDSlpglQARLmSQALR 166
Cdd:cd19514 80 DhdavLDNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALfrvdfSGR----GELAER----QQKL-AQMLS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 167 KLTaSISKSKCMVIFI-NQIRMKIG--VMFGS-PETTTGGNALKFYASVRLDIRR 217
Cdd:cd19514 151 RLQ-KISEEYNVAVFItNQVTADPGaaMTFQAdPKKPIGGHILAHASTTRISLRK 204
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
26-217 |
8.14e-11 |
|
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: 61.16 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQ---KKGGI---CAFVDAEHALDPV----YAR 95
Cdd:pfam08423 15 ELIQITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLCHTLCVTCQlplEMGGGegkALYIDTEGTFRPErlvaIAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 96 KLGVDLQNLLISQP-------DTGEQALEITDTLVRSGAVDILVVDSVAALTpRAEIEGEmGDslpgLQARLM--SQALR 166
Cdd:pfam08423 94 RYGLDPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 167 KLTASISKSKCMVIFINQIRMKIG---VMF-GSPETTTGGNALKFYASVRLDIRR 217
Cdd:pfam08423 168 TLQRLADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLRK 222
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
38-219 |
8.44e-11 |
|
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: 60.80 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 38 DIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEA---QKKGG---ICAFVDAEHAL------------DPVYARK--- 96
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampARKGGldgGVLYIDTESKFsaerlaeiaearFPEAFSGfme 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 97 ----LGVDLQNLLISQPDTGEQALEITDTL---VRSGAVDILVVDSVAALTPRaeiegEMGDSLPGLQARlMSQALRKLT 169
Cdd:cd19493 80 enerAEEMLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER-HNALAREAS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 170 A--SISKSKCM-VIFINQIRMKIGVMFGSPETTTG--GNALKFYASVRLDIRRIG 219
Cdd:cd19493 154 SlkRLAEEFRIaVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCL 208
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
26-217 |
1.40e-10 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 61.33 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKT----TLALQTIAEAQKKGGI--CAFVDAEHALDP----VYAR 95
Cdd:PLN03187 104 SVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTqlahTLCVTTQLPTEMGGGNgkVAYIDTEGTFRPdrivPIAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 96 KLGVD----LQNLLISQPDTGEQaleITDTLVRSGA------VDILVVDSVAAL-----TPRaeieGEMGDSlpglQARL 160
Cdd:PLN03187 183 RFGMDadavLDNIIYARAYTYEH---QYNLLLGLAAkmaeepFRLLIVDSVIALfrvdfTGR----GELAER----QQKL 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 960513281 161 mSQALRKLTASISKSKCMVIFINQIRMKIG--VMFGSPETTTGGNALKFYASVRLDIRR 217
Cdd:PLN03187 252 -AQMLSRLTKIAEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-218 |
1.76e-10 |
|
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: 58.15 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 48 KGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYARKLGVDLQNLLISqpDTGEQALEITDTLVRSGA 127
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 128 VDILVVDSVAALTPRAEiegemgdslpgLQARLMSQALRKLTASISKSKCMVIFINQirmkigvmfgsPETTTGGNALKF 207
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTTN-----------DEKDLGPALLRR 136
|
170
....*....|.
gi 960513281 208 YASVRLDIRRI 218
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
30-197 |
5.28e-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: 55.35 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVY--ARKLGVDL-----Q 102
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLrnAKSFGWDFdemedE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 103 NLLI--SQPDTGEQALEITDTL------VRSGAVDILVVDSVAALTPRAEiegemgdslpglQARLMSQALRKLTASISK 174
Cdd:cd01124 80 GKLIivDAPPTEAGRFSLDELLsrilsiIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
|
170 180
....*....|....*....|....*.
gi 960513281 175 SKCMVIFINQ---IRMKIGVMFGSPE 197
Cdd:cd01124 148 AGVTTIFTSEmrsFLSSESAGGGDVS 173
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
27-217 |
3.37e-08 |
|
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: 54.01 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 27 VETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQ------KKGGICAFVDAEHALDP----VYARK 96
Cdd:TIGR02238 75 VLKITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLSHTLCVTAQlpremgGGNGKVAYIDTEGTFRPdrirAIAER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 97 LGVD----LQNLLISQPDTGEQALEITDTLVRSGAVD---ILVVDSVAALTpRAEIEGEmgDSLPGLQARLmSQALRKLT 169
Cdd:TIGR02238 154 FGVDpdavLDNILYARAYTSEHQMELLDYLAAKFSEEpfrLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQMLSRLN 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 960513281 170 ASISKSKCMVIFINQIRMKIG--VMFGS-PETTTGGNALKFYASVRLDIRR 217
Cdd:TIGR02238 230 KISEEFNVAVFVTNQVQADPGatMTFIAdPKKPIGGHVLAHASTTRILLRK 280
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
30-217 |
3.38e-08 |
|
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: 53.09 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKT----TLAL--QTIAEAQKKGGICAFVDAE----------------- 86
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTqlchTLAVtcQLPIDQGGGEGKALYIDTEgtfrperllaiaerygl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 87 ---HALDPV-YARKLGVDLQNLLISQpdtgeqaleiTDTLVRSGAVDILVVDSVAALTpRAEIEGEmGDslpgLQARLM- 161
Cdd:cd19513 80 ngeDVLDNVaYARAYNTDHQMQLLIQ----------ASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMh 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 162 -SQALRKLTASISKSKCMVIFINQIRMKI--GVMF-GSPETTTGGNALKFYASVRLDIRR 217
Cdd:cd19513 144 lAKFLRMLQRLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
37-185 |
3.95e-08 |
|
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: 53.06 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 37 LDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQ------KKGGICAFVDAEHAL-------------DPVYARKL 97
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprelgGLGGGAVYICTESSFpskrlqqlasslpKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 98 GVDLQNLLISQPDTGEQALEITDT----LVRSGAVDILVVDSVAALTpRAEIEGEMGDSLpgLQARLMSQALRKLTASIS 173
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYqlpaLLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 960513281 174 KSKCMVIFINQI 185
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
26-217 |
4.84e-08 |
|
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: 53.58 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKT----TLALQTIAEAQKKG--GICAFVDAE------------- 86
Cdd:TIGR02239 74 EVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEgtfrperllaiae 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 87 -------HALDPV-YARKLGVDLQNLLISQpdtgeqaleiTDTLVRSGAVDILVVDSVAALTpRAEIEGEmGDslpgLQA 158
Cdd:TIGR02239 153 ryglnpeDVLDNVaYARAYNTDHQLQLLQQ----------AAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSA 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 159 RLMSQA--LRKLTASISKSKCMVIFINQIRMKI---GVMF-GSPETTTGGNALKFYASVRLDIRR 217
Cdd:TIGR02239 217 RQMHLArfLRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK 281
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
30-166 |
1.33e-07 |
|
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: 51.20 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFV---DAEHALDPVyARKLGVDLQNLLI 106
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYItlsETEQELRAV-ALSHGWSLDGIHI 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960513281 107 ---SQPDTGEQALEITDTL----VRSGAVDILVVDSVAALTP-RAEIegemgDSLpgLQARLMSQ-ALR 166
Cdd:cd19488 79 felSPSESALDAAQQYTILhpseLELSETTRLIFERVERLKPsRVVI-----DSL--SELRLLAQdSLR 140
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
49-216 |
4.84e-07 |
|
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: 49.65 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 49 GRIVEIYGPESSGKTTLALQTIAEA---QKKGGICA--------FVDAEHALDPVYARKL-------------------G 98
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpSSWGGVPLggleaavvFIDTDGRFDILRLRSIleariraaiqaanssddeeD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 99 VD------LQNLLISQPDTGEQ------ALEIT-DTLVRSGAVDILVVDSVAAL--TPRAEiegemgDSLPGLQARLMSQ 163
Cdd:cd19490 81 VEeiarecLQRLHIFRCHSSLQllatllSLENYlLSLSANPELGLLLIDSISAFywQDRFS------AELARAAPLLQEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 960513281 164 ALRKLTASISKS----KCMVIFINQIRMKIgvmfGSPETTTGGNALKFYASVRLDIR 216
Cdd:cd19490 155 ALRAILRELRRLrrrfQLVVIATKQALFPG----KSASTDNPAANNAVSKASAPSHR 207
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
30-257 |
4.85e-07 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 50.38 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKT----TLAL--QTIAEAQKKGGICAFVDAEHALDP----VYARKLGV 99
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTqlchTLCVtcQLPIEQGGGEGKVLYIDTEGTFRPerivQIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 100 D----LQNLLISQPDTGEQALEItdtLVRSGA------VDILVVDSVAALTpRAEI--EGEMGDSLPGLqARLMSqALRK 167
Cdd:PTZ00035 179 DpedvLDNIAYARAYNHEHQMQL---LSQAAAkmaeerFALLIVDSATALF-RVDYsgRGELAERQQHL-GKFLR-ALQK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 168 LTASISKSkcmVIFINQIRMKIG---VMFGSPETTTGGNALKFYASVRLDIRrigavKEReevvGNQTRVKVVKnkmAPP 244
Cdd:PTZ00035 253 LADEFNVA---VVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLR-----KGR----GEQRICKIYD---SPN 317
|
250
....*....|...
gi 960513281 245 FKQVEFDIMYGEG 257
Cdd:PTZ00035 318 LPESEAVFAISEG 330
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
26-217 |
6.57e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 50.12 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKT----TLALQTIAEAQKKG--GICAFVDAEHALDP----VYAR 95
Cdd:PLN03186 101 EIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCQLPLDQGGgeGKAMYIDTEGTFRPqrliQIAE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 96 KLGVD----LQNLLISQPDTGEQALEItdtLVRSGA------VDILVVDSVAALTpRAEIEGEmGDslpgLQAR--LMSQ 163
Cdd:PLN03186 180 RFGLNgadvLENVAYARAYNTDHQSEL---LLEAASmmaetrFALMIVDSATALY-RTEFSGR-GE----LSARqmHLGK 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 960513281 164 ALRKLTASISKSKCMVIFINQIRMKI--GVMFGSPETT-TGGNALKFYASVRLDIRR 217
Cdd:PLN03186 251 FLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK 307
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
26-182 |
1.95e-06 |
|
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: 48.30 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPV--YARKLGVDLQN 103
Cdd:cd01121 60 EEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIklRAERLGLGSDN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 104 LLIsqpdTGEQALEITDTLVRSGAVDILVVDSVAALTpRAEIEgemgdSLPG--LQARLMSQALRKLtasiSKSKCMVIF 181
Cdd:cd01121 139 LYL----LAETNLEAILAEIEELKPSLVVIDSIQTVY-SPELT-----SSPGsvSQVRECAAELLRL----AKETGIPVF 204
|
.
gi 960513281 182 I 182
Cdd:cd01121 205 L 205
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
46-282 |
2.43e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 45.28 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 46 LPKGRIVEIYGPESSGKTTLALQ---TIAEAQK------KGGICAFVDAE----------HALDPVYARKLGVDLQNLLI 106
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQlaaAVAAGGPwlgrrvPPGKVLYLAAEddrgelrrrlKALGADLGLPFADLDGRLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 107 SQPDTGEQALEITDTL---VRSGAVDILVVDSVAALtpraeIEGEMGDSlpgLQARLMSQALRKLtasISKSKCMVIFIN 183
Cdd:COG3598 90 LSLAGDLDDTDDLEALeraIEEEGPDLVVIDPLARV-----FGGDENDA---EEMRAFLNPLDRL---AERTGAAVLLVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 184 QIRmKIGVMFGSPETTTGGNALKFYASVRLDIRRigavKEREEVVgnqtRVKVVKNKMAPPFkqvEFDIMYGEGVSKTGE 263
Cdd:COG3598 159 HTG-KGGAGKDSGDRARGSSALRGAARSVLVLSR----EKGEDLR----VLTRAKSNYGPEI---ALRWDNGGRLALEEV 226
|
250
....*....|....*....
gi 960513281 264 LVDLGVKAGIVEKSGAWFS 282
Cdd:COG3598 227 AALTAGAGEVELKELVGGV 245
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
30-137 |
7.70e-05 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 43.06 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVYAR--KLGVDLQ----- 102
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERseALGIDLRamvek 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 960513281 103 -NLLISQPDT-----GEQALEITDTLVRSGAvDILVVDSVA 137
Cdd:cd19487 80 gLLSIEQIDPaelspGEFAQRVRTSVEQEDA-RVVVIDSLN 119
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
52-206 |
3.23e-04 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 39.79 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 52 VEIYGPESSGKTTLALQTIAEAQKKGGicafvdaehaldpvyarklgvdlQNLLISQPDTGEQALEitdTLVRSGAVDIL 131
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDE-----------------------PVIFISFLDTILEAIE---DLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960513281 132 VVDSVAALTPRaeiegemgdsLPGLQARLMSQALRKLTASISKSKCMVIFINQIRMKIGVMFGSPETTTGGNALK 206
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
28-68 |
3.82e-04 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 40.97 E-value: 3.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 960513281 28 ETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQ 68
Cdd:COG2874 1 EIISTGNDELDKRLG-GGIPLGSLVLIEGENGTGKSVLSQQ 40
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
44-73 |
6.69e-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: 39.93 E-value: 6.69e-04
10 20 30
....*....|....*....|....*....|
gi 960513281 44 GGLPKGRIVEIYGPESSGKTTLALQTIAEA 73
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTQLCLTAAANV 31
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
30-140 |
1.19e-03 |
|
C-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: 410892 [Multi-domain] Cd Length: 218 Bit Score: 39.62 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 30 ISTGSLSLDIALGIGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVY--ARKLGVDLQNLLIS 107
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 960513281 108 Q---------PDTG-EQALEITDTLVRSGAVDILVVDSVAALT 140
Cdd:cd19484 81 GllkiicarpELYGlEDHLIIIKSEINEFKPSRVIVDPLSALA 123
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
48-182 |
1.73e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.85 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 48 KGRIVEIYGPESSGKTTLAlqtiAEAQKKggicAFVDAEHALDPVYARKLgvDLQNLLISQPDTGEQALEITDTLVRSga 127
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFA----KTLPKP----LFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELAD-- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 960513281 128 VDILVVDSVAALTP--------RAEIEGEMGDSLP----GLQARLMSQALRKLtasiSKSKCMVIFI 182
Cdd:pfam13479 69 YKTIVIDTVDWLERlclayickQNGKGSSIEDGGYgkgyGELGEEFRRLLDAL----QELGKNVIFT 131
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
38-103 |
2.32e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 39.30 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960513281 38 DIALGIgglPKGRIVEIYGPESSGKTTLaLQTIA--EAQKKGGICaF----VDAEHALDpvyaRKLGVDLQN 103
Cdd:PRK10851 20 DISLDI---PSGQMVALLGPSGSGKTTL-LRIIAglEHQTSGHIR-FhgtdVSRLHARD----RKVGFVFQH 82
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
28-140 |
4.08e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 38.71 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 28 ETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAEHALDPVY--ARKLGVDLQN-- 103
Cdd:PRK09302 253 ERISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIrnARSWGIDLEKme 331
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 960513281 104 ----LLI--SQPD-TG-EQALEITDTLVRSGAVDILVVDSVAALT 140
Cdd:PRK09302 332 ekglLKIicARPEsYGlEDHLIIIKREIEEFKPSRVAIDPLSALA 376
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
26-146 |
5.05e-03 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 37.64 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960513281 26 EVETISTGSLSLDIALGiGGLPKGRIVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDAE--------------HALDP 91
Cdd:PRK06067 3 KKEIISTGNEELDRKLG-GGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTEntsksylkqmesvkIDISD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 960513281 92 VYAR-KLGVDLQNLLISQ--PDTGEQALEITDTLVRSGAVDILVVDSVAALTPRAEIE 146
Cdd:PRK06067 82 FFLWgYLRIFPLNTEGFEwnSTLANKLLELIIEFIKSKREDVIIIDSLTIFATYAEED 139
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
51-85 |
6.14e-03 |
|
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: 37.30 E-value: 6.14e-03
10 20 30
....*....|....*....|....*....|....*
gi 960513281 51 IVEIYGPESSGKTTLALQTIAEAQKKGGICAFVDA 85
Cdd:pfam01637 22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDP 56
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
50-68 |
8.03e-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: 36.72 E-value: 8.03e-03
|
| |
