|
Name |
Accession |
Description |
Interval |
E-value |
| recA |
PRK09354 |
recombinase A; Provisional |
13-341 |
0e+00 |
|
recombinase A; Provisional
Pssm-ID: 236476 [Multi-domain] Cd Length: 349 Bit Score: 655.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 13 AAPNSDKLKALQAAMDKIEKSYGKGSIMKLGDEKIEDIAVIPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHA 92
Cdd:PRK09354 1 MAMDEEKQKALEAALKQIEKQFGKGSIMRLGDDAAMDVEVISTGSLALDIALGIGGLPRGRIVEIYGPESSGKTTLALHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 93 IAEAQKAGGIAAFVDAEHAFDRFYAEKLGVDIGNLLISQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAELEGDM 172
Cdd:PRK09354 81 IAEAQKAGGTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADTLVRSGAVDLIVVDSVAALVPKAEIEGEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 173 GDSKMGLQARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIRRIGQLKDGEEVKG 252
Cdd:PRK09354 161 GDSHVGLQARLMSQALRKLTGNISKSNTTVIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 253 SQTRVKVVKNKVAPPFRKAEFDIMYGEGISRAGEIIDLGSDLGIVKKSGSWYSYNETKLGQGREAAKDMMRDNPELADEL 332
Cdd:PRK09354 241 NRTKVKVVKNKVAPPFKQAEFDIMYGEGISREGELIDLGVELGIIEKSGAWYSYNGEKIGQGRENAKQYLKENPELADEI 320
|
....*....
gi 1821116321 333 EQLIFAALK 341
Cdd:PRK09354 321 EKKIREKLG 329
|
|
| RecA |
COG0468 |
RecA/RadA recombinase [Replication, recombination and repair]; |
13-340 |
0e+00 |
|
RecA/RadA recombinase [Replication, recombination and repair];
Pssm-ID: 440236 [Multi-domain] Cd Length: 351 Bit Score: 650.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 13 AAPNSDKLKALQAAMDKIEKSYGKGSIMKLGDEKIEDIAVIPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHA 92
Cdd:COG0468 4 KVASSEKEKALEAALSQIEKQFGKGSIMRLGDKARQDVEVISTGSLALDIALGVGGLPRGRIVEIYGPESSGKTTLALHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 93 IAEAQKAGGIAAFVDAEHAFDRFYAEKLGVDIGNLLISQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAELEGDM 172
Cdd:COG0468 84 IAEAQKAGGIAAFIDAEHALDPEYAKKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDLIVVDSVAALVPKAEIEGEM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 173 GDSKMGLQARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIRRIGQLKDGEEVKG 252
Cdd:COG0468 164 GDSHVGLQARLMSQALRKLTGAISKSNTTVIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTIKDGDEVIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 253 SQTRVKVVKNKVAPPFRKAEFDIMYGEGISRAGEIIDLGSDLGIVKKSGSWYSYNETKLGQGREAAKDMMRDNPELADEL 332
Cdd:COG0468 244 NRTRVKVVKNKVAPPFKEAEFDIMYGEGISKEGELLDLAVELGIIEKSGAWYSYGGERLGQGRENAKQFLKENPELAEEI 323
|
....*...
gi 1821116321 333 EQLIFAAL 340
Cdd:COG0468 324 EAKIREKL 331
|
|
| tigrfam_recA |
TIGR02012 |
protein RecA; This model describes orthologs of the recA protein. RecA promotes hybridization ... |
18-336 |
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: 602.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 18 DKLKALQAAMDKIEKSYGKGSIMKLGDEKIEDIAVIPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQ 97
Cdd:TIGR02012 1 DKQKALEAALAQIEKQFGKGSIMRLGEKTVMDVETISTGSLALDLALGVGGLPKGRIIEIYGPESSGKTTLALHAIAEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 98 KAGGIAAFVDAEHAFDRFYAEKLGVDIGNLLISQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAELEGDMGDSKM 177
Cdd:TIGR02012 81 KAGGTAAFIDAEHALDPVYARKLGVDIDNLLVSQPDTGEQALEIAETLVRSGAVDIIVVDSVAALVPKAEIEGEMGDSHV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 178 GLQARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIRRIGQLKDGEEVKGSQTRV 257
Cdd:TIGR02012 161 GLQARLMSQALRKLTGALSKSNTTAIFINQIREKIGVMFGNPETTTGGNALKFYASVRLDIRRIGTVKQGEEVVGNRTKV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821116321 258 KVVKNKVAPPFRKAEFDIMYGEGISRAGEIIDLGSDLGIVKKSGSWYSYNETKLGQGREAAKDMMRDNPELADELEQLI 336
Cdd:TIGR02012 241 KVVKNKVAPPFREAEFDILYGEGISKLGEIIDLAVELDIIKKSGSWYSYGDEKLGQGRENAKAFLKENPELAQEIEKKV 319
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
21-282 |
2.16e-180 |
|
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: 499.62 E-value: 2.16e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 21 KALQAAMDKIEKSYGKGSIMKLGDEKIEDIAVIPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAG 100
Cdd:pfam00154 1 KALEAALKQIEKQFGKGSIMKLGDEKKLDVETISTGSLALDIALGIGGYPKGRIIEIYGPESSGKTTLALHAIAEAQKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 101 GIAAFVDAEHAFDRFYAEKLGVDIGNLLISQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAELEGDMGDSKMGLQ 180
Cdd:pfam00154 81 GTAAFIDAEHALDPVYAKKLGVDIDNLLVSQPDTGEQALEIADMLVRSGAIDLIVVDSVAALVPKAEIEGEMGDSHVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 181 ARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIRRIGQLKDGEEVKGSQTRVKVV 260
Cdd:pfam00154 161 ARLMSQALRKLTGSISKSNTTVIFINQIREKIGVMFGNPETTTGGRALKFYASVRLDIRRIGQIKQGEEVIGNKTKVKVV 240
|
250 260
....*....|....*....|..
gi 1821116321 261 KNKVAPPFRKAEFDIMYGEGIS 282
Cdd:pfam00154 241 KNKVAPPFKEAEFDIMYGEGIS 262
|
|
| RecA |
cd00983 |
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
49-283 |
9.67e-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: 466.26 E-value: 9.67e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 49 DIAVIPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRFYAEKLGVDIGNLL 128
Cdd:cd00983 1 DVEVIPTGSLSLDIALGIGGLPRGRIIEIYGPESSGKTTLALHAIAEAQKLGGTAAFIDAEHALDPEYAKKLGVDIDNLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 129 ISQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAELEGDMGDSKMGLQARLMSQALRKLTAAINKTNTTCIFINQL 208
Cdd:cd00983 81 VSQPDTGEQALEIADTLIRSGAVDLIVVDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKLTGSLSKSKTTVIFINQL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821116321 209 RDKIGVMFGNPETTTGGNALKFYASVRLDIRRIGQLKDGEEVKGSQTRVKVVKNKVAPPFRKAEFDIMYGEGISR 283
Cdd:cd00983 161 REKIGVMFGNPETTTGGNALKFYASVRLDIRRIELIKEGEDVIGNRTKVKVVKNKVAPPFKQAEFDILYGEGISR 235
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
18-263 |
5.68e-127 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 382.13 E-value: 5.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 18 DKLKALQAAMDKIEKSYGKGSIMKLGDEKIEDIAVIPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQ 97
Cdd:PRK09519 6 DREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 98 KAGGIAAFVDAEHAFDRFYAEKLGVDIGNLLISQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAELEGDMGDSKM 177
Cdd:PRK09519 86 AAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 178 GLQARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIRRIGQLKDGEEVKGSQTRV 257
Cdd:PRK09519 166 GLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRV 245
|
....*.
gi 1821116321 258 KVVKNK 263
Cdd:PRK09519 246 KVVKNK 251
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
72-240 |
1.02e-51 |
|
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: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 72 GRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRFYA-----------EKLGVDIGNLLISQPDNGEQALE 140
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEGAFPPSRLvqileaspsseLELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 141 IAEQLIRSSA----IDIVVIDSVAALTPKAELEGDMGDSKMGLQARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMF 216
Cdd:cd01393 81 ALDSLPESLFpppnTSLVVVDSVSALFRKAFPRGGDGDSSSSLRARLLSQLARALQKLAAQFNLAVVVTNQVTTKIRGGS 160
|
170 180
....*....|....*....|....*
gi 1821116321 217 G-NPETTTGGNALKFYASVRLDIRR 240
Cdd:cd01393 161 GaSLVPPALGNTWEHSVSTRLLLYR 185
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
259-336 |
1.51e-22 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 98.63 E-value: 1.51e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821116321 259 VVKNKVAPPFRKAEFDIMYGEGISRAGEIIDLGSDLGIVKKSGSWYSYNETKLGQGREAAKDMMRDNPELADELEQLI 336
Cdd:PRK09519 687 VVVHNCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKI 764
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
53-199 |
2.42e-17 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 79.67 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEH-AFDRFYA---EKLGVDIGNLL 128
Cdd:cd01394 1 LSTGSKSLDSLLG-GGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGlSPERFQQiagERFESIASNII 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821116321 129 ISQP-DNGEQALEI--AEQLIRSSAIDIVVIDSVAALTpKAELEGDMG-DSKMGLQARLMSQALRKLTAAINKTN 199
Cdd:cd01394 80 VFEPySFDEQGVAIqeAEKLLKSDKVDLVVVDSATALY-RLELGDDSEaNRELSRQMSKLLSIARKYDIPVVITN 153
|
|
| COG4544 |
COG4544 |
Uncharacterized conserved protein [Function unknown]; |
51-166 |
1.96e-15 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443609 [Multi-domain] Cd Length: 230 Bit Score: 74.58 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 51 AVIPTGSIGLNAALGVGGFPRGRVIEIYGPE-SSGKTTLAIHAIAEAQKAGGIAAFVDAEHAfdrFYA---EKLGVDIGN 126
Cdd:COG4544 27 AVLPTGFAALDAALPGGGLPRGALHEILGPApGIGELGLLLPLLARLAQAGGPVLWIAPPYD---LYApglAAAGLDPER 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1821116321 127 LLISQPDNGEQALEIAEQLIRSSAIDIVVIDsVAALTPKA 166
Cdd:COG4544 104 LLLVRARRPADALWAAEEALRSGACGAVVAW-LERLDLTA 142
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
53-220 |
5.84e-15 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 73.03 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRF--YAEKLGVDI------ 124
Cdd:COG0467 2 VPTGIPGLDELLG-GGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLlrRAESLGLDLeeyies 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 125 GNLLI---SQPDNGEQALEIAEQL---IRSSAIDIVVIDSVAALTPKaelegdMGDSKMglqARLMsqaLRKLTAAINKT 198
Cdd:COG0467 81 GLLRIidlSPEELGLDLEELLARLreaVEEFGAKRVVIDSLSGLLLA------LPDPER---LREF---LHRLLRYLKKR 148
|
170 180
....*....|....*....|..
gi 1821116321 199 NTTCIFINQLRDKIGVMFGNPE 220
Cdd:COG0467 149 GVTTLLTSETGGLEDEATEGGL 170
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
53-213 |
5.57e-14 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 70.28 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEhAF--DRF------YAEKLgvdI 124
Cdd:PRK09361 5 LPTGCKMLDELLG-GGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-GLspERFkqiageDFEEL---L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 125 GNLLISQP---DNGEQALEIAEQLIRSSaIDIVVIDSVAALTpKAELEGDMGDSKmgLQARLMSQaLRKLTAAINKTNTT 201
Cdd:PRK09361 80 SNIIIFEPssfEEQSEAIRKAEKLAKEN-VGLIVLDSATSLY-RLELEDEEDNSK--LNRELGRQ-LTHLLKLARKHDLA 154
|
170
....*....|..
gi 1821116321 202 CIFINQLRDKIG 213
Cdd:PRK09361 155 VVITNQVYSDID 166
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
53-211 |
2.26e-13 |
|
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: 68.44 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDR--------FYAEKLGVDI 124
Cdd:cd01124 1 VKTGIPGLDELLG-GGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERllrnaksfGWDFDEMEDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 125 GNLLISQ-------PDNGEQALEIAEQLIRSSAIDIVVIDSVAALTPKAElegdmgdskmglQARLMSQALRKLTAAINK 197
Cdd:cd01124 80 GKLIIVDappteagRFSLDELLSRILSIIKSFKAKRVVIDSLSGLRRAKE------------DQMRARRIVIALLNELRA 147
|
170
....*....|....
gi 1821116321 198 TNTTCIFINQLRDK 211
Cdd:cd01124 148 AGVTTIFTSEMRSF 161
|
|
| recomb_radB |
TIGR02237 |
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ... |
60-213 |
1.31e-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: 65.90 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 60 LNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEH-AFDRFYA---EKLGVDIGNLLISQP--- 132
Cdd:TIGR02237 1 IDELLG-GGVERGTITQIYGPPGSGKTNICMILAVNAARQGKKVVYIDTEGlSPERFKQiaeDRPERALSNFIVFEVfdf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 133 DNGEQALEIAEQLIRSSAIDIVVIDSVAALTpKAELEGDMGDSKMGLQARLmsQALRKLTAainKTNTTCIFINQLRDKI 212
Cdd:TIGR02237 80 DEQGVAIQKTSKFIDRDSASLVVVDSFTALY-RLELSDDRISRNRELARQL--TLLLSLAR---KKNLAVVITNQVYTDV 153
|
.
gi 1821116321 213 G 213
Cdd:TIGR02237 154 N 154
|
|
| ImuA_translesion |
NF033429 |
translesion DNA synthesis-associated protein ImuA; A three-gene cassette encoding ImuA, ImuB, ... |
51-150 |
1.78e-12 |
|
translesion DNA synthesis-associated protein ImuA; A three-gene cassette encoding ImuA, ImuB, and ImuC ("inducible mutagenesis") is induced by DNA damage, is capable of DNA synthesis across DNA damage lesions, and consequently is associated with mutagenesis. This family, ImuA (previously misnamed SulA in Pseudomonas putida) shows some homology to SulA itself and to RecA. ImuB resembles Y-family polymerases but may be catalytically inactive. ImuC is a C-family polymerase, and catalytically active.
Pssm-ID: 468022 Cd Length: 181 Bit Score: 64.80 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 51 AVIPTGSIGLNAALGVGGFPRGRVIEIYGP-ESSGKTTLAIHAIAEAQKAGGIAAFVDAEHafdRFYAE---KLGVDIGN 126
Cdd:NF033429 14 RVVPTGFAALDAELPGGGWPLGALTELLSPqPGIGELRLLLPALARLTQRGRRIVLVAPPH---LPYAPalaAAGIDLEQ 90
|
90 100
....*....|....*....|....
gi 1821116321 127 LLISQPDNGEQALEIAEQLIRSSA 150
Cdd:NF033429 91 LLVVRADSPADALWAAEQCLRSGA 114
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
71-241 |
9.45e-12 |
|
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: 62.01 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 71 RGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRFYAEKLGVDIGNLLISqpDNGEQALEIAEQLIRSSA 150
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS--GSGELRLRLALALARKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 151 IDIVVIDSVAALTPKAElegdmgdskmgLQARLMSQALRKLTAAINKTNTTCIFINqlrdkigvmfgNPETTTGGNALKF 230
Cdd:smart00382 79 PDVLILDEITSLLDAEQ-----------EALLLLLEELRLLLLLKSEKNLTVILTT-----------NDEKDLGPALLRR 136
|
170
....*....|.
gi 1821116321 231 YASVRLDIRRI 241
Cdd:smart00382 137 RFDRRIVLLLI 147
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
53-243 |
1.14e-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: 63.80 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIH-AIAEAQKAGGIAAFVDA-EHAFD-RFYAEKLGVDI----- 124
Cdd:pfam06745 1 VKTGIPGLDEILK-GGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLeEPPEDlRENARSFGWDLeklee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 125 -GNLLI-------------SQPDNGEQALEIAEQLIRSSAIDIVVIDSVAALtpkAELEGDMgdskmglQARlmsQALRK 190
Cdd:pfam06745 80 eGKLAIidastsgigiaevEDRFDLEELIERLREAIREIGAKRVVIDSITTL---FYLLKPA-------VAR---EILRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821116321 191 LTAAINKTNTTCIFINQLRDKigvmfgnpETTTGGNALKFYAS---VRLDIRRIGQ 243
Cdd:pfam06745 147 LKRVLKGLGVTAIFTSEKPSG--------EGGIGGYGVEEFIVdgvIRLDLKEIEE 194
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
53-250 |
5.78e-11 |
|
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: 61.78 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAiHAIA-------EAQKAGGIAAFVDAEHAF--DRF--YAEKLG 121
Cdd:cd01123 1 ITTGSKELDKLLG-GGIETGSITEMFGEFRTGKTQLC-HTLAvtcqlpiDRGGGEGKAIYIDTEGTFrpERLraIAQRFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 122 VD----IGNLLISQPDNGEQALEI---AEQLIRSSAIDIVVIDSVAALTpKAELEGdmgdsKMGLQARLM--SQALRKLT 192
Cdd:cd01123 79 LDpddvLDNVAYARAFNSDHQTQLldqAAAMMVESRFKLLIVDSATALY-RTDYSG-----RGELSARQMhlAKFLRMLQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821116321 193 AAINKTNTTCIFINQLRDKIG---VMFGNPETTTGGNALKFYASVRLDIR------RIGQLKDGEEV 250
Cdd:cd01123 153 RLADEFGVAVVVTNQVVAQVDgamMFAADPKKPIGGNILAHASTTRLYLRkgrgetRICKIYDSPCL 219
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
53-260 |
1.70e-10 |
|
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: 60.39 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKT----TLAIHAIAEAQKAG--GIAAFVDAEHAF--DRFY--AEKLGV 122
Cdd:pfam08423 19 ITTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLCVTCQLPLEMGGgeGKALYIDTEGTFrpERLVaiAERYGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 123 DIGNLLISQP-------DNGEQALEIAEQLIRSSAIDIVVIDSVAALTpKAELE--GDMGDSKMGLqARLMSqALRKLTA 193
Cdd:pfam08423 98 DPEDVLDNVAyaraynsEHQMQLLQQAAAMMSESRFALLIVDSATALY-RTDFSgrGELAERQQHL-AKFLR-TLQRLAD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821116321 194 AINktntTCIFI-NQLRDKIG---VMF-GNPETTTGGNALKFYASVRLdirrigQLKDGeevKGSQTRVKVV 260
Cdd:pfam08423 175 EFG----VAVVItNQVVAQVDgaaGMFsGDPKKPIGGHIMAHASTTRL------SLRKG---RGEQRICKIY 233
|
|
| PLN03187 |
PLN03187 |
meiotic recombination protein DMC1 homolog; Provisional |
21-272 |
8.82e-10 |
|
meiotic recombination protein DMC1 homolog; Provisional
Pssm-ID: 215620 [Multi-domain] Cd Length: 344 Bit Score: 59.41 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 21 KALQAAMDKIEKSYGKGSIMKLgdeKIEDIAVIPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAiHAIA------ 94
Cdd:PLN03187 79 KICEAAEKLLNQGFITGSDALL---KRKSVVRITTGSQALDELLG-GGIETRCITEAFGEFRSGKTQLA-HTLCvttqlp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 95 -EAQKAGGIAAFVDAEHAF--DRF--YAEKLGVD----IGNLLISQPDNGEQ--------ALEIAEQLIRssaidIVVID 157
Cdd:PLN03187 154 tEMGGGNGKVAYIDTEGTFrpDRIvpIAERFGMDadavLDNIIYARAYTYEHqynlllglAAKMAEEPFR-----LLIVD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 158 SVAAL-----TPKAELEGDmgdskmglQARLmSQALRKLTAAINKTNTTCIFINQLR-DKIGVMF-GNPETTTGGNALKF 230
Cdd:PLN03187 229 SVIALfrvdfTGRGELAER--------QQKL-AQMLSRLTKIAEEFNVAVYMTNQVIaDPGGGMFiSDPKKPAGGHVLAH 299
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1821116321 231 YASVRLDIRRigqlkdgeeVKGSQTRVKVVKnkvAPPFRKAE 272
Cdd:PLN03187 300 AATIRLMLRK---------GKGEQRVCKVFD---APNLPEAE 329
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
60-213 |
8.18e-09 |
|
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: 55.38 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 60 LNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQ---KAGGI---AAFVDAEHAF-------------DRFYAEKL 120
Cdd:cd19491 1 LDELLG-GGIPVGGITEIAGESGAGKTQLCLQLALTVQlprELGGLgggAVYICTESSFpskrlqqlasslpKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 121 GVDIGNLLISQPDNGEQALEIAEQ----LIRSSAIDIVVIDSVAALtpkAELEGDMGDSKMGLQARLMSQALRKLTAAIN 196
Cdd:cd19491 80 KNFLDNIFVEHVADLETLEHCLNYqlpaLLERGPIRLVVIDSIAAL---FRSEFDTSRSDLVERAKYLRRLADHLKRLAD 156
|
170
....*....|....*..
gi 1821116321 197 KTNTTCIFINQLRDKIG 213
Cdd:cd19491 157 KYNLAVVVVNQVTDRFD 173
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
61-162 |
8.29e-09 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 55.02 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 61 NAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEA----QKAGGIAA--FVDAEHAF-------------------DRF 115
Cdd:cd19493 1 DTALA-GGLPLGAITEITGASGSGKTQFALTLASSAampaRKGGLDGGvlYIDTESKFsaerlaeiaearfpeafsgFME 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1821116321 116 YAEKLGVDIGNLLISQPDNGEQALEIAEQL---IRSSAIDIVVIDSVAAL 162
Cdd:cd19493 80 ENERAEEMLKRVAVVRVTTLAQLLERLPNLeehILSSGVRLVVIDSIAAL 129
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
45-240 |
5.94e-08 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 53.34 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 45 EKIEDIAVIPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAiHAIA-------EAQKAGGIAAFVDAEHAF--DRF 115
Cdd:PRK04301 76 ERRKNVGKITTGSKELDELLG-GGIETQSITEFYGEFGSGKTQIC-HQLAvnvqlpeEKGGLEGKAVYIDTEGTFrpERI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 116 --YAEKLGVDIG----NLLISQPDNGE-QAL--EIAEQLIRSS-AIDIVVIDSVAALTpKAEL--EGDMGDSkmglQARL 183
Cdd:PRK04301 154 eqMAEALGLDPDevldNIHVARAYNSDhQMLlaEKAEELIKEGeNIKLVIVDSLTAHF-RAEYvgRGNLAER----QQKL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821116321 184 MsQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIRR 240
Cdd:PRK04301 229 N-KHLHDLLRLADLYNAAVVVTNQVMARPDAFFGDPTQPIGGHILGHTATFRIYLRK 284
|
|
| archRadA |
cd19515 |
archaeal recombinase Rad51/RadA; This group includes the archaeal protein RadA which is a ... |
53-246 |
7.34e-08 |
|
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: 52.37 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAiHAIA-------EAQKAGGIAAFVDAEHAF--DRF--YAEKLG 121
Cdd:cd19515 1 ISTGSKELDKLLG-GGIETQAITEVFGEFGSGKTQLC-HQLAvnvqlppEEGGLNGKAVYIDTENTFrpERImqMAKALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 122 VDIGNLL----ISQPDNGE---QALEIAEQLIRSS-AIDIVVIDSVAALTpKAELegdMGDSKMGLQARLMSQALRKLTA 193
Cdd:cd19515 79 LDPDEVLdniyVARAYNSNhqmLLVEKAEDLIKEGnNIKLLIVDSLTSHF-RAEY---VGRGTLAERQQKLNKHLHDLHR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821116321 194 AINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALKFYASVRLDIR------RIGQLKD 246
Cdd:cd19515 155 LADLYNIAVLVTNQVMAKPDAFFGDPTQAIGGHILGHAATFRVYLRkgkggkRIARLVD 213
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
75-229 |
1.21e-07 |
|
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: 49.81 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 75 IEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAehaFDRfyaeklgvdignllisqpdngeqALEIAEQLIRSSAIDIV 154
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISF---LDT-----------------------ILEAIEDLIEEKKLDII 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821116321 155 VIDSVAALTPKAElegdmgdskmGLQARLMSQALRKLTAAINKTNTTCIFINQLRDKIGVMFGNPETTTGGNALK 229
Cdd:cd01120 55 IIDSLSSLARASQ----------GDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDIDRGGSSNDERLLKSLR 119
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
48-286 |
3.33e-07 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 51.27 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 48 EDIAVIPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKT----TLAIHAIAEAQKAG--GIAAFVDAEHAF--DRFY--A 117
Cdd:PLN03186 100 QEIIQITTGSRELDKILE-GGIETGSITEIYGEFRTGKTqlchTLCVTCQLPLDQGGgeGKAMYIDTEGTFrpQRLIqiA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 118 EKLGVD----IGNLLISQPDNGEQALEI---AEQLIRSSAIDIVVIDSVAALTpKAELEGdmgdsKMGLQAR--LMSQAL 188
Cdd:PLN03186 179 ERFGLNgadvLENVAYARAYNTDHQSELlleAASMMAETRFALMIVDSATALY-RTEFSG-----RGELSARqmHLGKFL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 189 RKLTAAINKTNTTCIFINQLRDKI--GVMFGNPETT-TGGNALKFYASVRLDIRrigqlkdgeevKG-SQTRV-KVVKNK 263
Cdd:PLN03186 253 RSLQRLADEFGVAVVITNQVVAQVdgSAFFAGPQLKpIGGNIMAHASTTRLALR-----------KGrGENRIcKVISSP 321
|
250 260
....*....|....*....|...
gi 1821116321 264 VAPPfRKAEFDIMyGEGISRAGE 286
Cdd:PLN03186 322 CLPE-AEARFSIS-SEGVTDVKD 342
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
69-339 |
3.44e-07 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 51.05 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 69 FPRGRVIEIYGPESSGKTTLAIH---AIAEAQKAGGI------AAFVDAEHAFDRF------YAEKLGVDI----GNLLI 129
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQlaaAVAAGGPWLGRrvppgkVLYLAAEDDRGELrrrlkaLGADLGLPFadldGRLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 130 SQPDNGEQALEIAEQL---IRSSAIDIVVIDSVAALtpkaeLEGDMGDSKmglQARLMSQALRKLtaaINKTNTTCIFIN 206
Cdd:COG3598 90 LSLAGDLDDTDDLEALeraIEEEGPDLVVIDPLARV-----FGGDENDAE---EMRAFLNPLDRL---AERTGAAVLLVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 207 QLRdKIGVMFGNPETTTGGNALKFYASVRLDIRRigqLKDGEEVkgsqtRVKVVKNKVAPPFrkaEFDIMYGEGISRAGE 286
Cdd:COG3598 159 HTG-KGGAGKDSGDRARGSSALRGAARSVLVLSR---EKGEDLR-----VLTRAKSNYGPEI---ALRWDNGGRLALEEV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1821116321 287 IIDLGSDLGIVKKSGSWYSYNETKLGQGREAAKDMMRDNPELADELEQLIFAA 339
Cdd:COG3598 227 AALTAGAGEVELKELVGGVARTGTDSELEEGLLEVPLAEAESAGEDAELAAKA 279
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
45-286 |
4.11e-07 |
|
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: 50.88 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 45 EKIEDIAVIPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKT----TLAIHAIAEAQKAG--GIAAFVDAEHAF--DRFY 116
Cdd:TIGR02239 70 QRRQEVIQLTTGSKELDKLLG-GGIETGSITEIFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEGTFrpERLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 117 --AEKLGVD----IGNLLISQPDNGEQALEI---AEQLIRSSAIDIVVIDSVAALTpKAELEGdmgdsKMGLQARLMSQA 187
Cdd:TIGR02239 149 aiAERYGLNpedvLDNVAYARAYNTDHQLQLlqqAAAMMSESRFALLIVDSATALY-RTDFSG-----RGELSARQMHLA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 188 --LRKLTAAINKTNTTCIFINQLR---DKIGVMF-GNPETTTGGNALKFYASVRLDIRRigqlkdgeeVKGSQTRVKVVK 261
Cdd:TIGR02239 223 rfLRSLQRLADEFGVAVVITNQVVaqvDGAGSMFaGDPKKPIGGNIMAHASTTRLSLRK---------GRGEQRICKIYD 293
|
250 260
....*....|....*....|....*
gi 1821116321 262 NKVAPPfRKAEFDImYGEGISRAGE 286
Cdd:TIGR02239 294 SPCLPE-SEAMFAI-YEDGIGDPKE 316
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
53-240 |
1.60e-06 |
|
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: 48.47 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKT----TLAIHAIAEAQKAG--GIAAFVDAEHAF--DRFY--AEKLGV 122
Cdd:cd19513 1 ITTGSKELDKLLG-GGIETGSITELFGEFRTGKTqlchTLAVTCQLPIDQGGgeGKALYIDTEGTFrpERLLaiAERYGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 123 D----IGNLLISQPDNGEQALEIaeqLIRSSAI------DIVVIDSVAALTpKAELEGdMGDskmgLQARLM--SQALRK 190
Cdd:cd19513 80 NgedvLDNVAYARAYNTDHQMQL---LIQASAMmaesryALLIVDSATALY-RTDYSG-RGE----LSARQMhlAKFLRM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821116321 191 LTAAINKTNTTCIFINQLRDKI--GVMF-GNPETTTGGNALKFYASVRLDIRR 240
Cdd:cd19513 151 LQRLADEFGVAVVITNQVVAQVdgAAMFaGDPKKPIGGNIMAHASTTRLYLRK 203
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
53-240 |
2.91e-06 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 48.46 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKT----TLAIHA--IAEAQKAGGIAAFVDAEHAF--DRF--YAEKLGV 122
Cdd:PTZ00035 100 ITTGSTQLDKLLG-GGIETGSITELFGEFRTGKTqlchTLCVTCqlPIEQGGGEGKVLYIDTEGTFrpERIvqIAERFGL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 123 D----IGNLLISQPDNGEQALEI---AEQLIRSSAIDIVVIDSVAALTpKAEL--EGDMGDSKMGLqARLMSqALRKLTA 193
Cdd:PTZ00035 179 DpedvLDNIAYARAYNHEHQMQLlsqAAAKMAEERFALLIVDSATALF-RVDYsgRGELAERQQHL-GKFLR-ALQKLAD 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1821116321 194 AINktntTCIFI-NQLRDKIG---VMFGNPETTTGGNALKFYASVRLDIRR 240
Cdd:PTZ00035 256 EFN----VAVVItNQVMADVDgasMFVADPKKPIGGHIIAHASTTRLSLRK 302
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
72-113 |
4.17e-06 |
|
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: 47.34 E-value: 4.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1821116321 72 GRVIEIYGPESSGKTTLAIHAIAEA---QKAGGIAA--------FVDAEHAFD 113
Cdd:cd19490 1 GDVIEITGPSGSGKTELLYHLAARCilpSSWGGVPLggleaavvFIDTDGRFD 53
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
53-160 |
9.44e-06 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 46.14 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRFY--AEKLGVDI------ 124
Cdd:cd19487 1 VSSGVPELDELLG-GGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFerSEALGIDLramvek 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1821116321 125 GNLLISQPDNGE-QALEIAeQLIRSSA----IDIVVIDSVA 160
Cdd:cd19487 80 GLLSIEQIDPAElSPGEFA-QRVRTSVeqedARVVVIDSLN 119
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
74-156 |
1.05e-05 |
|
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: 45.77 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 74 VIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDA-----EHAFDRFY-----AEKLGVDIGNLLISQPDNGEQALEIAE 143
Cdd:pfam01637 22 IYVIYGPEGCGKTALLRESIENLLDLGYYVIYYDPlrryfISKLDRFEevrrlAEALGIAVPKAELEESKLAFLAIELLL 101
|
90
....*....|...
gi 1821116321 144 QLIRSSAIDIVVI 156
Cdd:pfam01637 102 EALKRRGKKIAII 114
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
40-159 |
4.93e-05 |
|
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: 44.44 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 40 MKLGDEKIEDIAVIPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFD--RFYA 117
Cdd:cd01121 51 LPLSDVEAEEEERISTGIGELDRVLG-GGLVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSqiKLRA 129
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1821116321 118 EKLGVDIGNLLISQpdngEQALEIAEQLIRSSAIDIVVIDSV 159
Cdd:cd01121 130 ERLGLGSDNLYLLA----ETNLEAILAEIEELKPSLVVIDSI 167
|
|
| Rad51D |
cd19489 |
RAD51D recombinase; RAD51D recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
67-201 |
5.56e-05 |
|
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: 43.78 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 67 GGFPRGRVIEIYGPESSGKT----TLAIHAIAEaqkAGGIAAFVDAEHAfdrFYAEKlgvdIGNLLISQPDNGEQALEIA 142
Cdd:cd19489 2 GGLRTGEITELVGESSSGKTqlclTAAANVASR---SGQNVLYIDTKSS---FSARR----LAQILKSRAQDAEEIDKAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 143 EQLIRSSAIDI---------------------------VVIDSVAAL-TP----KAELEgdmGDSKMGLQARLMSQALRK 190
Cdd:cd19489 72 QRIRVVRVFDPyelldlleelrntlsqqqenlysrlklVIIDSLSALiSPllggSKHSE---GHALLASLARLLKKLAAE 148
|
170
....*....|.
gi 1821116321 191 LTAAINKTNTT 201
Cdd:cd19489 149 YQIAVLVTNLT 159
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
53-163 |
1.35e-04 |
|
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: 42.70 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGVGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRFY--AEKLGVDIGNLLIS 130
Cdd:cd19484 1 ISTGIPRLDAMLGGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIrnAKSIGIDLEQMERK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1821116321 131 Q--------PDNG--EQALEIAEQLIRSSAIDIVVIDSVAALT 163
Cdd:cd19484 81 GllkiicarPELYglEDHLIIIKSEINEFKPSRVIVDPLSALA 123
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
71-196 |
1.46e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 42.31 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 71 RGRVIEIYGPESSGKTTLAIHAiaeaqkagGIAAFVDAEHAFDRFYAEKLGVDIGNLLISQPDNGEQALEIAEQlirsSA 150
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTL--------PKPLFLDTEKGSKALDGDRFPDIVIRDSWQDFLDAIDELTAAEL----AD 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821116321 151 IDIVVIDSVAAL-----------TPKAELEGDMGDSKM-GLQARLMSQALRKLTAAIN 196
Cdd:pfam13479 69 YKTIVIDTVDWLerlclayickqNGKGSSIEDGGYGKGyGELGEEFRRLLDALQELGK 126
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
53-146 |
1.70e-04 |
|
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: 42.34 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFD--RFYAEKLGVDIGNLLIS 130
Cdd:cd19488 1 ISTGIPGLDDILR-GGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQelRAVALSHGWSLDGIHIF 79
|
90
....*....|....*.
gi 1821116321 131 QPDNGEQALEIAEQLI 146
Cdd:cd19488 80 ELSPSESALDAAQQYT 95
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
66-209 |
6.38e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 40.44 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 66 VGGF-PRGRVIEIYGPESSGKTTLAIH---AIAEAQKAGGIAA--------FVDAEHAFD----RFYAEKLGVD------ 123
Cdd:pfam13481 26 IKGLlPAGGLGLLAGAPGTGKTTLALDlaaAVATGKPWLGGPRvpeqgkvlYVSAEGPADelrrRLRAAGADLDlparll 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 124 ----IGNLLISQPDNGEQAL-----EIAEQLIRSSAIDIVVIDSVAALTPkaelegdmGDSKMGLQARLMSQALRKLTAa 194
Cdd:pfam13481 106 flslVESLPLFFLDRGGPLLdadvdALEAALEEVEDPDLVVIDPLARALG--------GDENSNSDVGRLVKALDRLAR- 176
|
170
....*....|....*
gi 1821116321 195 inKTNTTCIFINQLR 209
Cdd:pfam13481 177 --RTGATVLLVHHVG 189
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
53-163 |
2.76e-03 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 39.48 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 53 IPTGSIGLNAALGvGGFPRGRVIEIYGPESSGKTTLAIHAIAEAQKAGGIAAFVDAEHAFDRFY--AEKLGVDI------ 124
Cdd:PRK09302 255 ISSGVPDLDEMLG-GGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIrnARSWGIDLekmeek 333
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1821116321 125 GNLLI--SQPDNG--EQALEIAEQLIRSSAIDIVVIDSVAALT 163
Cdd:PRK09302 334 GLLKIicARPESYglEDHLIIIKREIEEFKPSRVAIDPLSALA 376
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
73-157 |
5.69e-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: 37.11 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 73 RVIEIYGPESSGKTTLAiHAIAEAQKaggiAAFVDaEHAfdRFYAEKLGvdiGNLLISQPDN---GEQALEiaEQLIRSS 149
Cdd:COG3172 9 KKIVLLGAESTGKTTLA-RALAAHYN----TPWVP-EYG--REYLEEKG---RALTYDDLLAiarGQLALE--DAAAKRA 75
|
....*...
gi 1821116321 150 AiDIVVID 157
Cdd:COG3172 76 N-KLLFCD 82
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
83-155 |
6.78e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 37.51 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821116321 83 SGKTTLAIHAIAEAQKAGGIAAF-----VDAEHAFDRF--YAEKLGVDIGNLLISQPdnGEQALEIAEQlIRSSAIDIVV 155
Cdd:cd17992 77 SGKTVVAALAMLAAVENGYQVALmapteILAEQHYDSLkkLLEPLGIRVALLTGSTK--AKEKREILEK-IASGEIDIVI 153
|
|
| |
