|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
5-309 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 648.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 5 GSIMRMGDgEAAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDVQ 84
Cdd:PRK09354 25 GSIMRLGD-DAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 85 YASKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTI 164
Cdd:PRK09354 104 YAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGNI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 165 KRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDI 244
Cdd:PRK09354 184 SKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTKVKVVKNKVAPPFKQAEFDI 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149395002 245 LYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESL 309
Cdd:PRK09354 264 MYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEIEKKIREKL 328
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
5-310 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 629.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 5 GSIMRMGDgEAAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDVQ 84
Cdd:COG0468 28 GSIMRLGD-KARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHAIAEAQKAGGIAAFIDAEHALDPE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 85 YASKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTI 164
Cdd:COG0468 107 YAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 165 KRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDI 244
Cdd:COG0468 187 SKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIGNRTRVKVVKNKVAPPFKEAEFDI 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149395002 245 LYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRESLA 310
Cdd:COG0468 267 MYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEIEAKIREKLG 332
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
4-307 |
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: 568.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 4 QGSIMRMGDgEAAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDV 83
Cdd:TIGR02012 19 KGSIMRLGE-KTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 84 QYASKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGT 163
Cdd:TIGR02012 98 VYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 164 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFD 243
Cdd:TIGR02012 178 LSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKVKVVKNKVAPPFREAEFD 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149395002 244 ILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNGEKIGQGKDNAREFLRENPEIAREIENRIRE 307
Cdd:TIGR02012 258 ILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKVRE 321
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
4-251 |
3.71e-174 |
|
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: 482.28 E-value: 3.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 4 QGSIMRMGDgEAAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDV 83
Cdd:pfam00154 16 KGSIMKLGD-EKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAGGTAAFIDAEHALDP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 84 QYASKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGT 163
Cdd:pfam00154 95 VYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 164 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFD 243
Cdd:pfam00154 175 ISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVVKNKVAPPFKEAEFD 254
|
....*...
gi 149395002 244 ILYGEGIS 251
Cdd:pfam00154 255 IMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
18-252 |
4.84e-168 |
|
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: 465.49 E-value: 4.84e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 18 NIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDVQYASKLGVNVPELL 97
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 98 ISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQI 177
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149395002 178 RMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISR 252
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
1-232 |
2.28e-108 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 332.44 E-value: 2.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 1 SVRQGSIMRMGDgEAAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHA 80
Cdd:PRK09519 21 SYGKGSVMRLGD-EARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 81 LDVQYASKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKL 160
Cdd:PRK09519 100 LDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKM 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149395002 161 TGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRIGSIKKNDEVIGNETRVKVVKNK 232
Cdd:PRK09519 180 TGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
41-209 |
3.89e-52 |
|
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: 169.46 E-value: 3.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 41 GRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDVQYA-----------SKLGVNVPELLISQPDTGEQALE 109
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 110 ITDALVRSGS----IDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMF 185
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 149395002 186 G-NPETTTGGNALKFYSSVRLDIRR 209
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
200-310 |
1.43e-27 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 112.88 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 200 YSSVR--LDIRRIGSIKKNDEVIGNETRVKVVKNKVSPPFREAIFDILYGEGISRQGEIIDLGVQAKIVDKAGAWYSYNG 277
Cdd:PRK09519 657 YSVIRevLPTRRARTFDLEVEELHTLVAEGVVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEG 736
|
90 100 110
....*....|....*....|....*....|...
gi 149395002 278 EKIGQGKDNAREFLRENPEIAREIENRIRESLA 310
Cdd:PRK09519 737 EQLGQGKENARNFLVENADVADEIEKKIKEKLG 769
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
22-262 |
1.07e-18 |
|
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: 82.75 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDVQYASKLGVNVPELL---- 97
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGLSPERFQQIAGERFESIAsnii 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 98 ISQP-DTGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEiegEMGDSlpGLQARLMSQaLRKLTGTIKRTNCLVIFI 174
Cdd:cd01394 80 VFEPySFDEQGVAIQEAekLLKSDKVDLVVVDSATALY-RLE---LGDDS--EANRELSRQ-MSKLLSIARKYDIPVVIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 175 NQIRMKIGVMFGNPettTGGNALKFYSSVRLDIRRIGSikkndevignETRVKVVKNKVSPPfreaifdilygEGISRQG 254
Cdd:cd01394 153 NQVYSDIDDDRLKP---VGGTLLEHWSKAIIRLEKSPP----------GLRRATLEKHRSRP-----------EGQSAGF 208
|
....*...
gi 149395002 255 EIIDLGVQ 262
Cdd:cd01394 209 RITDRGIR 216
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
22-189 |
7.24e-14 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 69.56 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALD--VQYASKLGVNVPELL-- 97
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEqlLRRAESLGLDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 98 -----------ISQPDTGEQALEITDAlVRSGSIDMIVIDSVAALVpkaeiegemgDSLPGLQARLmsQALRKLTGTIKR 166
Cdd:COG0467 81 gllriidlspeELGLDLEELLARLREA-VEEFGAKRVVIDSLSGLL----------LALPDPERLR--EFLHRLLRYLKK 147
|
170 180
....*....|....*....|...
gi 149395002 167 TNCLVIFINQIRMKIGVMFGNPE 189
Cdd:COG0467 148 RGVTTLLTSETGGLEDEATEGGL 170
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
22-250 |
1.25e-13 |
|
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: 69.25 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQK-IGGT---AAFIDAEHALD----VQYASKLGV 91
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLCVTCQLPLeMGGGegkALYIDTEGTFRperlVAIAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 92 NVPELLISQP-------DTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 162
Cdd:pfam08423 98 DPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LAERQQhlAKFLRTLQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 163 TIKRTNCLVIFINQIRMKIG---VMF-GNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRV-KVVKnkvSP-- 235
Cdd:pfam08423 172 LADEFGVAVVITNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRLSLR-----KGRG-----EQRIcKIYD---SPcl 238
|
250
....*....|....*
gi 149395002 236 PFREAIFDIlYGEGI 250
Cdd:pfam08423 239 PESEAVFAI-GSGGI 252
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
18-211 |
7.85e-13 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 66.42 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 18 NIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEhALDVQYASKL-GVNVPEL 96
Cdd:PRK09361 1 MDERLPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLSPERFKQIaGEDFEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 97 L----ISQP-DTGEQALEITDA--LVRSgSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQaLRKLTGTIKRTNC 169
Cdd:PRK09361 79 LsniiIFEPsSFEEQSEAIRKAekLAKE-NVGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKHDL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 149395002 170 LVIFINQIRMKIGvmfGNPETTTGGNALKFYSS--VRLDIRRIG 211
Cdd:PRK09361 154 AVVITNQVYSDID---SDGLRPLGGHTLEHWSKtiLRLEKFRNG 194
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
17-250 |
1.49e-12 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 66.82 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 17 ENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------IGGTAAFIDAEHALD----VQYA 86
Cdd:PRK04301 79 KNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQICHQLAVNVQLpeekggLEGKAVYIDTEGTFRperiEQMA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 87 SKLGVNVPELL-----ISQPDTGEQALEITDA--LVRSG-SIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLMSQ--A 156
Cdd:PRK04301 158 EALGLDPDEVLdnihvARAYNSDHQMLLAEKAeeLIKEGeNIKLVIVDSLTAHF-RAEYVGR--GNLAERQQKLNKHlhD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 157 LRKLTGTIkrtNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP- 235
Cdd:PRK04301 235 LLRLADLY---NAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK----SKGNKRI-----ARLVD---SPh 299
|
250
....*....|....*.
gi 149395002 236 -PFREAIFDILyGEGI 250
Cdd:PRK04301 300 lPEGEAVFRIT-EEGI 314
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
29-209 |
2.43e-12 |
|
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: 64.74 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 29 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEhALDVQYASKLGVNVPELLISQ------PD 102
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTE-GLSPERFKQIAEDRPERALSNfivfevFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 103 TGEQALEITDA--LVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLPGLQARlmsqaLRKLTGTIKRTNCLVIFINQIRMK 180
Cdd:TIGR02237 79 FDEQGVAIQKTskFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQ-----LTLLLSLARKKNLAVVITNQVYTD 152
|
170 180
....*....|....*....|....*....
gi 149395002 181 IGVMFGNPettTGGNALKFYSSVRLDIRR 209
Cdd:TIGR02237 153 VNNGTLRP---LGGHLLEHWSKVILRLEK 178
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
22-244 |
2.63e-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: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQK------IGGTAAFIDAEHALD----VQYASKLGV 91
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLCHQLAVNVQLppeeggLNGKAVYIDTENTFRperiMQMAKALGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 92 NVPELL-----ISQPDTGEQAL---EITDALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 163
Cdd:cd19515 80 DPDEVLdniyvARAYNSNHQMLlveKAEDLIKEGNNIKLLIVDSLTSHF-RAEYVGR--GTLAERQQKL-NKHLHDLHRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 164 IKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKnkvSP--PFREAI 241
Cdd:cd19515 156 ADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRK----GKGGKRI-----ARLVD---SPhlPEGEAV 223
|
...
gi 149395002 242 FDI 244
Cdd:cd19515 224 FRI 226
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
30-212 |
1.34e-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: 63.11 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 30 DIALGvGGLPRGRVVEIYGPESSGKT----TLTLQVIAELQKIGGTAA--FIDAEHALDVQ-------------YASKLG 90
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTqfalTLASSAAMPARKGGLDGGvlYIDTESKFSAErlaeiaearfpeaFSGFME 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 91 VNVPELLISQ------PDTGEQALEITDAL---VRSGSIDMIVIDSVAALVPKaeiegEMGDSLPGLQARlmSQALRKLT 161
Cdd:cd19493 80 ENERAEEMLKrvavvrVTTLAQLLERLPNLeehILSSGVRLVVIDSIAALVRR-----EFGGSDGEVTER--HNALAREA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 149395002 162 GTIKRT----NCLVIFINQIRMKIGVMFGNPETTTG--GNALKFYSSVRLDIRRIGS 212
Cdd:cd19493 153 SSLKRLaeefRIAVLVTNQATTHFGDAGDGSSGVTAalGDAWAHAVNTRLRLERCLL 209
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
11-126 |
2.76e-11 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 62.25 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 11 GDGEAAENIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPE-SSGKTTLTLQVIAELQKIGGTAAFIDAEHALdvqYA--- 86
Cdd:COG4544 18 GEGLAAAARAVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYDL---YApgl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 149395002 87 SKLGVNVPELLISQPDTGEQALEITDALVRSGSIDMIVID 126
Cdd:COG4544 95 AAAGLDPERLLLVRARRPADALWAAEEALRSGACGAVVAW 134
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-210 |
7.38e-11 |
|
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: 59.31 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 40 RGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDVQYASKLGVNVPELLISqpDTGEQALEITDALVRSGS 119
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 120 IDMIVIDSVAALVPKAEiegemgdslpgLQARLMSQALRKLTGTIKRTNCLVIFINqirmkigvmfgNPETTTGGNALKF 199
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|.
gi 149395002 200 YSSVRLDIRRI 210
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
29-177 |
3.24e-10 |
|
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: 59.23 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 29 LDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIA------ELQKIGGTAAFIDAEHALDVQ----------------YA 86
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALtvqlprELGGLGGGAVYICTESSFPSKrlqqlasslpkryhleKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 87 SKLGVNVPELLISQPDTGEQALEITD-ALVRSGSIDMIVIDSVAALVpKAEIEGEMGDSLpgLQARLMSQALRKLTGTIK 165
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYQLpALLERGPIRLVVIDSIAALF-RSEFDTSRSDLV--ERAKYLRRLADHLKRLAD 156
|
170
....*....|..
gi 149395002 166 RTNCLVIFINQI 177
Cdd:cd19491 157 KYNLAVVVVNQV 168
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
22-244 |
4.86e-10 |
|
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: 58.52 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQKI----GGTAAFIDAEHALD----VQYASKLGV 91
Cdd:cd19514 1 ISTGSTELDKLLG-GGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGTFRpdriRPIAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 92 N----VPELLISQPDTGEQALEITDAL----VRSGSIDMIVIDSVAALVpKAEI--EGEMGDSlpglQARLmSQALRKLT 161
Cdd:cd19514 80 DhdavLDNILYARAYTSEHQMELLDYVaakfHEEAVFRLLIIDSIMALF-RVDFsgRGELAER----QQKL-AQMLSRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 162 GTIKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFR 238
Cdd:cd19514 154 KISEEYNVAVFITNQVTADPGaaMTFqADPKKPIGGHILAHASTTRISLRK-GR---------GEERIAKIYDSPDLPEN 223
|
....*.
gi 149395002 239 EAIFDI 244
Cdd:cd19514 224 EATFAI 229
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
22-212 |
4.88e-10 |
|
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: 58.80 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAE-LQKIGGTAAFIDA-EHALDV-QYASKLGVNVPELL- 97
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQFLYNgALKYGEPGVFVTLeEPPEDLrENARSFGWDLEKLEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 98 --------ISQPDTGEQALEITDAL----------VRSGSIDMIVIDSVAALvpkAEIEGEMgdslpglQARlmsQALRK 159
Cdd:pfam06745 80 egklaiidASTSGIGIAEVEDRFDLeelierlreaIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 149395002 160 LTGTIKRTNCLVIFINQIRMKigvmfgnpETTTGGNALKFYSS---VRLDIRRIGS 212
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
22-250 |
1.52e-09 |
|
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: 57.15 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQ----KIGGTAAFIDAEHALD----VQYASKLGV 91
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLchTLAVTCQLPidrgGGEGKAIYIDTEGTFRperlRAIAQRFGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 92 NVPELL----ISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 162
Cdd:cd01123 80 DPDDVLdnvaYARAFNSDHQTQLLDqaaAMMVESRFKLLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 163 TIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFRE 239
Cdd:cd01123 154 LADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRK-GR---------GETRICKIYDSPCLPEAE 223
|
250
....*....|.
gi 149395002 240 AIFDIlYGEGI 250
Cdd:cd01123 224 AVFAI-TADGV 233
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
17-244 |
1.19e-08 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 55.51 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 17 ENIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKIG-GTAAFIDAEHALD----VQYA 86
Cdd:PLN03186 101 EIIQI-TTGSRELDKILE-GGIETGSITEIYGEFRTGKTQLchTLCVTCQLpldQGGGeGKAMYIDTEGTFRpqrlIQIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 87 SKLGVNVPELL----ISQPDTGEQALEItdaLVRSGSI------DMIVIDSVAALVpKAEIEGEmGDslpgLQAR--LMS 154
Cdd:PLN03186 179 ERFGLNGADVLenvaYARAYNTDHQSEL---LLEAASMmaetrfALMIVDSATALY-RTEFSGR-GE----LSARqmHLG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 155 QALRKLTGTIKRTNCLVIFINQIRMKI--GVMFGNPETT-TGGNALKFYSSVRLDIRRigsiKKNDEVIgnetrVKVVKN 231
Cdd:PLN03186 250 KFLRSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALRK----GRGENRI-----CKVISS 320
|
250
....*....|...
gi 149395002 232 KVSPPfREAIFDI 244
Cdd:PLN03186 321 PCLPE-AEARFSI 332
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
22-178 |
1.37e-08 |
|
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: 54.19 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALD--VQYASKLGVNVPEL--- 96
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPErlLRNAKSFGWDFDEMede 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 97 ----LISQPDTGEQALEITD------ALVRSGSIDMIVIDSVAALvpkaeiegemgdSLPGLQARLMSQALRKLTGTIKR 166
Cdd:cd01124 80 gkliIVDAPPTEAGRFSLDEllsrilSIIKSFKAKRVVIDSLSGL------------RRAKEDQMRARRIVIALLNELRA 147
|
170
....*....|..
gi 149395002 167 TNCLVIFINQIR 178
Cdd:cd01124 148 AGVTTIFTSEMR 159
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
22-250 |
1.57e-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: 54.25 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKIG-GTAAFIDAEHALD----VQYASKLGV 91
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAIAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 92 NVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--SQALRKLTG 162
Cdd:cd19513 80 NGEDVLDNvayarayNTDHQMQLLIQASAMMAESRYALLIVDSATALY-RTDYSGR-GE----LSARQMhlAKFLRMLQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 163 TIKRTNCLVIFINQIRMKI--GVMF-GNPETTTGGNALKFYSSVRLDIRRigsikkndeviGN-ETRVKVVKNKVSPPFR 238
Cdd:cd19513 154 LADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK-----------GRgETRICKIYDSPCLPEA 222
|
250
....*....|..
gi 149395002 239 EAIFDIlYGEGI 250
Cdd:cd19513 223 EAVFAI-TEDGI 233
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
16-251 |
1.95e-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: 54.73 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 16 AENIQVvSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKIG-GTAAFIDAEHALD----VQY 85
Cdd:TIGR02239 73 QEVIQL-TTGSKELDKLLG-GGIETGSITEIFGEFRTGKTQLchTLAVTCQLpidQGGGeGKALYIDTEGTFRperlLAI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 86 ASKLGVNVPELLIS-------QPDTGEQALEITDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLMSQA-- 156
Cdd:TIGR02239 151 AERYGLNPEDVLDNvayarayNTDHQLQLLQQAAAMMSESRFALLIVDSATALY-RTDFSGR-GE----LSARQMHLArf 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 157 LRKLTGTIKRTNCLVIFINQIRMKI---GVMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNK 232
Cdd:TIGR02239 225 LRSLQRLADEFGVAVVITNQVVAQVdgaGSMFaGDPKKPIGGNIMAHASTTRLSLRK-GR---------GEQRICKIYDS 294
|
250
....*....|....*....
gi 149395002 233 VSPPFREAIFDIlYGEGIS 251
Cdd:TIGR02239 295 PCLPESEAMFAI-YEDGIG 312
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
22-209 |
2.41e-08 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 54.40 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL--QKIGGTA--AFIDAEHALD----VQYASKLGV 91
Cdd:PLN03187 108 ITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLahTLCVTTQLptEMGGGNGkvAYIDTEGTFRpdriVPIAERFGM 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 92 N----VPELLISQPDTGEQ---ALEITDALVRSGSIDMIVIDSVAALVPKAEI-EGEMGDSlpglQARLmSQALRKLTGT 163
Cdd:PLN03187 187 DadavLDNIIYARAYTYEHqynLLLGLAAKMAEEPFRLLIVDSVIALFRVDFTgRGELAER----QQKL-AQMLSRLTKI 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 149395002 164 IKRTNCLVIFINQIRMKIG--VMFGNPETTTGGNALKFYSSVRLDIRR 209
Cdd:PLN03187 262 AEEFNVAVYMTNQVIADPGggMFISDPKKPAGGHVLAHAATIRLMLRK 309
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
41-182 |
1.08e-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: 51.58 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 41 GRVVEIYGPESSGKTTLTLQVIA---------ELQKIGGTAA--FIDAEHALDV------------QYASKLGVNVPE-- 95
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAArcilpsswgGVPLGGLEAAvvFIDTDGRFDIlrlrsilearirAAIQAANSSDDEed 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 96 -----------LLISQPDTGEQ------ALEIT-DALVRSGSIDMIVIDSVAALVPKAEIEGEMGDSLPGLQARLM---S 154
Cdd:cd19490 81 veeiareclqrLHIFRCHSSLQllatllSLENYlLSLSANPELGLLLIDSISAFYWQDRFSAELARAAPLLQEAALraiL 160
|
170 180
....*....|....*....|....*...
gi 149395002 155 QALRKLTgtiKRTNCLVIFINQIRMKIG 182
Cdd:cd19490 161 RELRRLR---RRFQLVVIATKQALFPGK 185
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
14-258 |
1.15e-07 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 52.31 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 14 EAAENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAEL---QKIG-GTAAFIDAEHALD----V 83
Cdd:PTZ00035 92 EARKNIIRITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTQLchTLCVTCQLpieQGGGeGKVLYIDTEGTFRperiV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 84 QYASKLGVNVPELL----ISQPDTGEQALEI---TDALVRSGSIDMIVIDSVAALVpKAEIEGEmGDslpgLQARLM--S 154
Cdd:PTZ00035 171 QIAERFGLDPEDVLdniaYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYSGR-GE----LAERQQhlG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 155 QALRKLTGTIKRTNCLVIFINQIRMKIG---VMFGNPETTTGGNALKFYSSVRLDIRrigsiKKNDevignETRVKVVKN 231
Cdd:PTZ00035 245 KFLRALQKLADEFNVAVVITNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLR-----KGRG-----EQRICKIYD 314
|
250 260
....*....|....*....|....*..
gi 149395002 232 KVSPPFREAIFdilygeGISRQGeIID 258
Cdd:PTZ00035 315 SPNLPESEAVF------AISEGG-IID 334
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
21-244 |
2.51e-07 |
|
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: 51.32 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 21 VVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTL--TLQVIAELQKIGGTA----AFIDAEHALD----VQYASKLG 90
Cdd:TIGR02238 77 KITTGSQALDGILG-GGIESMSITEVFGEFRCGKTQLshTLCVTAQLPREMGGGngkvAYIDTEGTFRpdriRAIAERFG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 91 VN----VPELLISQPDTGEQALEITD---ALVRSGSIDMIVIDSVAALVpKAEIEGEmgDSLPGLQARLmSQALRKLTGT 163
Cdd:TIGR02238 156 VDpdavLDNILYARAYTSEHQMELLDylaAKFSEEPFRLLIVDSIMALF-RVDFSGR--GELSERQQKL-AQMLSRLNKI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 164 IKRTNCLVIFINQIRMKIG--VMF-GNPETTTGGNALKFYSSVRLDIRRiGSikkndevigNETRVKVVKNKVSPPFREA 240
Cdd:TIGR02238 232 SEEFNVAVFVTNQVQADPGatMTFiADPKKPIGGHVLAHASTTRILLRK-GR---------GEERVAKLYDSPDMPEAEA 301
|
....
gi 149395002 241 IFDI 244
Cdd:TIGR02238 302 SFQI 305
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
16-174 |
2.93e-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: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 16 AENIQVVSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAEHALDvQY---ASKLGVN 92
Cdd:cd01121 58 AEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLS-QIklrAERLGLG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 93 VPELLIsqpdTGEQALEITDALVRSGSIDMIVIDSVAALVPKAEiegemgDSLPG--LQARLMSQALRKLTgtiKRTNCL 170
Cdd:cd01121 136 SDNLYL----LAETNLEAILAEIEELKPSLVVIDSIQTVYSPEL------TSSPGsvSQVRECAAELLRLA---KETGIP 202
|
....
gi 149395002 171 VIFI 174
Cdd:cd01121 203 VFLV 206
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
38-174 |
3.63e-07 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 50.67 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 38 LPRGRVVEIYGPESSGKTTLTLQVIAEL---------QKIGGTAAFIDAE-HALDVQ-----YASKLGVNVPEL-----L 97
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrRVPPGKVLYLAAEdDRGELRrrlkaLGADLGLPFADLdgrlrL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 98 IS-----QPDTGEQALEitdALVRSGSIDMIVIDSVAALVPKAEIEGEmgdslpglQARLMSQALRKLtgtIKRTNCLVI 172
Cdd:COG3598 90 LSlagdlDDTDDLEALE---RAIEEEGPDLVVIDPLARVFGGDENDAE--------EMRAFLNPLDRL---AERTGAAVL 155
|
..
gi 149395002 173 FI 174
Cdd:COG3598 156 LV 157
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
41-182 |
1.09e-06 |
|
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51C, together with the other RAD51 paralogs, RAD51B, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site. Additionally, RAD51C acts as a mediator in the early steps of DNA damage signaling.
Pssm-ID: 410900 [Multi-domain] Cd Length: 172 Bit Score: 47.99 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 41 GRVVEIYGPESSGKTTLTLQVIAELQ------KIGGTAAFIDAE-----HALDV-QYASKLGV--NVPELLISQPDtgeq 106
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAVNVQipkcfgGLAGEAIYIDTEgsfniHYFRVhDYVELLALinSLPKFLEDHPK---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149395002 107 aleitdalvrsgsIDMIVIDSVAALVpKAEIEGemgdslPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIG 182
Cdd:cd19492 77 -------------VKLIVVDSIAFPF-RHDFDD------LAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVTTKIS 132
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
22-75 |
7.20e-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: 46.19 E-value: 7.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 149395002 22 VSTGSLGLDIALGvGGLPRGRVVEIYGPESSGKTTLTLQVIAELQKIGGTAAFI 75
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYI 53
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
44-198 |
9.54e-06 |
|
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: 44.03 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 44 VEIYGPESSGKTTLTLQVIAELQKIGGTAAFIDAehaldvqyasklgvnvpellisqPDTGEQALEitdALVRSGSIDMI 123
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF-----------------------LDTILEAIE---DLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149395002 124 VIDSVAALVPKaeiegemgdsLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGNPETTTGGNALK 198
Cdd:cd01120 55 IIDSLSSLARA----------SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
40-174 |
8.17e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 40.00 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 40 RGRVVEIYGPESSGKTTLTLQViaelqkigGTAAFIDAEHALDVQYASKLgvNVPELLISQPDTGEQALEITDALVRsgS 119
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRF--PDIVIRDSWQDFLDAIDELTAAELA--D 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149395002 120 IDMIVIDSVAALV-----------PKAEIEGEMGDSLP-GLQARLMSQALRKLTGTIKRtnclVIFI 174
Cdd:pfam13479 69 YKTIVIDTVDWLErlclayickqnGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGKN----VIFT 131
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
36-132 |
2.31e-03 |
|
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: 38.39 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 36 GGLPRGRVVEIYGPESSGKT----TLTLQVIAELQKI-------GGTAA-----FIDAEHALDVQYASKLG----VNV-- 93
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTqlclTAAANVASRSGQNvlyidtkSSFSArrlaqILKSRAQDAEEIDKALQrirvVRVfd 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 149395002 94 PELLISQPDTGEQALEiTDALVRSGSIDMIVIDSVAALV 132
Cdd:cd19489 82 PYELLDLLEELRNTLS-QQQENLYSRLKLVIIDSLSALI 119
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
46-132 |
2.52e-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: 38.46 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 46 IYGPESSGKTTLTLQVIAELQKIGGTAAFIDA-----EHALDVQYASK-----LGVNVPELLISQPDTGEQALE-ITDAL 114
Cdd:pfam01637 25 IYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEEVRrlaeaLGIAVPKAELEESKLAFLAIElLLEAL 104
|
90
....*....|....*...
gi 149395002 115 VRSGSIDMIVIDSVAALV 132
Cdd:pfam01637 105 KRRGKKIAIIIDEVQQAI 122
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
38-174 |
4.36e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 37.75 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 38 LPRGRVVEIYGPESSGKTTLTLQVIA-----------ELQKIGGTAAFIDAEHALDVQ----YASKLGVNVPELL----- 97
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAavatgkpwlggPRVPEQGKVLYVSAEGPADELrrrlRAAGADLDLPARLlflsl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 98 -----ISQPDTGEQAL-----EITDALVRSGSIDMIVIDSVAALVPkaeiegemGDSLPGLQARLMSQALRKLtgtIKRT 167
Cdd:pfam13481 110 veslpLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG--------GDENSNSDVGRLVKALDRL---ARRT 178
|
....*..
gi 149395002 168 NCLVIFI 174
Cdd:pfam13481 179 GATVLLV 185
|
|
| RecA-like_NVL_r2-like |
cd19530 |
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
32-172 |
5.94e-03 |
|
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410938 [Multi-domain] Cd Length: 161 Bit Score: 36.70 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 32 ALGVGgLPRGrvVEIYGPESSGKTTLTLQVIAELQkiggtAAFIDaehaldvqyasklgVNVPELLISQPDTGEQALEIT 111
Cdd:cd19530 24 ALGID-LPTG--VLLYGPPGCGKTLLAKAVANESG-----ANFIS--------------VKGPELLNKYVGESERAVRQV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149395002 112 DALVRSGSIDMIVIDSVAALVPKaeiegeMGDSLPGLQARLMSQALRKLTGTIKRTNCLVI 172
Cdd:cd19530 82 FQRARASAPCVIFFDEVDALVPK------RGDGGSWASERVVNQLLTEMDGLEERSNVFVI 136
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-129 |
7.42e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 37.44 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149395002 30 DIALGVgglPRGRVVEIYGPESSGKTTLtlqviaeLQKIGGTAAFIDAEHALDvqyasklGVNVPELLISQPDTGEQALE 109
Cdd:PRK11831 25 NISLTV---PRGKITAIMGPSGIGKTTL-------LRLIGGQIAPDHGEILFD-------GENIPAMSRSRLYTVRKRMS 87
|
90 100
....*....|....*....|..
gi 149395002 110 ItdaLVRSGSI--DMIVIDSVA 129
Cdd:PRK11831 88 M---LFQSGALftDMNVFDNVA 106
|
|
| |
