|
Name |
Accession |
Description |
Interval |
E-value |
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
1-453 |
0e+00 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 853.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 1 MAKTKSKFICQSCGYESPKWMGKCPGCGAWNTMVEEMIKKAPANRRAafSHSVQTVQKPSPITSIETSEEPRVKTQLGEF 80
Cdd:COG1066 1 MAKTKTVYVCQECGYESPKWLGRCPECGAWNTLVEEVVAKAKKGRAA--SGAAGRASKPVPLSEVEAEEEPRISTGIGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 81 NRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDMEYIS 160
Cdd:COG1066 79 DRVLGGGLVPGSVVLIGGEPGIGKSTLLLQVAARLAKKGGKVLYVSGEESASQIKLRAERLGLLSDNLYLLAETDLEAIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 161 SAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVTKEGSIAGPRLLEHMVDTVLYF 240
Cdd:COG1066 159 ATIEELKPDLLVIDSIQTMYSEELESAPGSVSQVRECAAELIRLAKETGIAVFLVGHVTKEGSIAGPRVLEHMVDTVLYF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 241 EGERHHTFRILRAVKNRFGSTNEMGIFEMREEGLTEVLNPSEIFLEERSAGSAGSSITASMEGTRPILVEIQALISPTSF 320
Cdd:COG1066 239 EGDRHSRYRILRAVKNRFGSTNEIGVFEMTEKGLREVSNPSELFLSERDEPVPGSAVTVTMEGTRPLLVEVQALVSPSSF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 321 GNPRRMATGIDHNRVSLLMAVLEKRVGLLLQNQDAYLKVAGGVKLDEPAIDLAIVISIASSFRDTPPNPADCFIGEVGLT 400
Cdd:COG1066 319 GNPRRTAVGLDSNRLAMLLAVLEKRAGLPLGDQDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGEVGLT 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1238239004 401 GEVRRVSRIEQRVKEAAKLGFKRMIIPAANLDGWtKPKGIEVIGVANVAEALR 453
Cdd:COG1066 399 GEIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKL-KPKGIEIIGVSTLEEALE 450
|
|
| sms |
TIGR00416 |
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved ... |
1-452 |
0e+00 |
|
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved in both DNA repair and degradation of proteins, peptides, glycopeptides. Also known as sms. Residues 11-28 of the SEED alignment contain a putative Zn binding domain. Residues 110-117 of the seed contain a putative ATP binding site both documented in Haemophilus (SP:P45266) and in Listeria monocytogenes (SP:Q48761) . for E.coli see ( J. BACTERIOL. 178:5045-5048(1996)). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273067 [Multi-domain] Cd Length: 454 Bit Score: 795.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 1 MAKTKSKFICQSCGYESPKWMGKCPGCGAWNTMVEEMIK---KAPANRRAAFSHSVQTVQKPSPITSIETSEEPRVKTQL 77
Cdd:TIGR00416 1 MAKAKSKFVCQHCGADSPKWQGKCPACHAWNTITEERLHrslGAQKNRRNSGKAGIPQAQKSQTISAIELEEVPRFSSGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 78 GEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDME 157
Cdd:TIGR00416 81 GELDRVLGGGIVPGSLILIGGDPGIGKSTLLLQVACQLAKNQMKVLYVSGEESLQQIKMRAIRLGLPEPNLYVLSETNWE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 158 YISSAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVTKEGSIAGPRLLEHMVDTV 237
Cdd:TIGR00416 161 QICANIEEENPQACVIDSIQTLYSPDISSAPGSVSQVRECTAELMRLAKTRGIAIFIVGHVTKEGSIAGPKVLEHMVDTV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 238 LYFEGERHHTFRILRAVKNRFGSTNEMGIFEMREEGLTEVLNPSEIFLEERSAGSAGSSITASMEGTRPILVEIQALISP 317
Cdd:TIGR00416 241 LYFEGDRDSRFRILRSVKNRFGATNEIGIFEMTEQGLREVLNPSAIFLSRREEPMSGSSITVTWEGTRPLLVEIQALVSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 318 TSFGNPRRMATGIDHNRVSLLMAVLEKRVGLLLQNQDAYLKVAGGVKLDEPAIDLAIVISIASSFRDTPPNPADCFIGEV 397
Cdd:TIGR00416 321 TSFANPRRVATGLDQNRLALLLAVLEKRLGLPLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFLGEV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1238239004 398 GLTGEVRRVSRIEQRVKEAAKLGFKRMIIPAANLDGwTKPKGIEVIGVANVAEAL 452
Cdd:TIGR00416 401 GLAGEIRPVPSLEERLKEAAKLGFKRAIVPKANSPK-TAPEGIKVIGVKKVGDAL 454
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
8-277 |
6.77e-178 |
|
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: 498.21 E-value: 6.77e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 8 FICQSCGYESPKWMGKCPGCGAWNTMVEEMIKKAPANRRAAFSHSVQtvQKPSPITSIETSEEPRVKTQLGEFNRVLGGG 87
Cdd:cd01121 1 YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSSASRRASASPSP--SKPLPLSDVEAEEEERISTGIGELDRVLGGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 88 VVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDMEYISSAIQEMN 167
Cdd:cd01121 79 LVPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIKLRAERLGLGSDNLYLLAETNLEAILAEIEELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 168 PSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVTKEGSIAGPRLLEHMVDTVLYFEGERHHT 247
Cdd:cd01121 159 PSLVVIDSIQTVYSPELTSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVTKDGAIAGPKVLEHMVDTVLYFEGDRGSS 238
|
250 260 270
....*....|....*....|....*....|
gi 1238239004 248 FRILRAVKNRFGSTNEMGIFEMREEGLTEV 277
Cdd:cd01121 239 YRILRSVKNRFGPTNEIGVFEMTENGLREV 268
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
72-275 |
9.90e-26 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 104.23 E-value: 9.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 72 RVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGIN------N 145
Cdd:COG0467 1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRAESLGLDleeyieS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 146 PSLHVLSETDMEY----------ISSAIQEMNPSFVVVDSIqtvyqSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIV 215
Cdd:COG0467 81 GLLRIIDLSPEELgldleellarLREAVEEFGAKRVVIDSL-----SGLLLALPDPERLREFLHRLLRYLKKRGVTTLLT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238239004 216 GHVTKEGSIAGPRLLEHMVDTVLYF-----EGERHHTFRILravKNRfGSTNEMGIFEMR--EEGLT 275
Cdd:COG0467 156 SETGGLEDEATEGGLSYLADGVILLryvelGGELRRALSVL---KMR-GSAHDRTIREFEitDGGIE 218
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
73-275 |
1.43e-17 |
|
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: 81.16 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 73 VKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLS 152
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLRNAKSFGWDFDEMEDEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 153 ETDM-----------------EYISSAIQEMNPSFVVVDSIQTVYQSDITSapgsvSQVRECTAELMKIAKTKGIPIFIV 215
Cdd:cd01124 81 KLIIvdappteagrfsldellSRILSIIKSFKAKRVVIDSLSGLRRAKEDQ-----MRARRIVIALLNELRAAGVTTIFT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238239004 216 G--HVTKEGSIAGPRLLEHMVDTV--LYF---EGERHHTFRIlraVKNRFGStNEMGI--FEMREEGLT 275
Cdd:cd01124 156 SemRSFLSSESAGGGDVSFIVDGVilLRYveiEGELRRTIRV---LKMRGTG-HDTGThpFEITDKGIV 220
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
90-288 |
6.50e-17 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 81.10 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 90 KGSLVLIGGDPGIGKSTLLLQVSAQLSGSSN---------SVLYISGEESVKQTKLRADRLGIN--------NPSLHVLS 152
Cdd:COG3598 12 EGGVTLLAGPPGTGKSFLALQLAAAVAAGGPwlgrrvppgKVLYLAAEDDRGELRRRLKALGADlglpfadlDGRLRLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 153 ET-------DMEYISSAIQEMNPSFVVVDSIQTVYQSDITSApgsvSQVRECTAELMKIAKTKGIPIFIVGHVTKE---- 221
Cdd:COG3598 92 LAgdlddtdDLEALERAIEEEGPDLVVIDPLARVFGGDENDA----EEMRAFLNPLDRLAERTGAAVLLVHHTGKGgagk 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238239004 222 -------GSIAgprlLEHMVDTVLYFEGERHHTFRILRAVKNRFGSTNEMGIFEMREEGLTEVLNPSEIFLEER 288
Cdd:COG3598 168 dsgdrarGSSA----LRGAARSVLVLSREKGEDLRVLTRAKSNYGPEIALRWDNGGRLALEEVAALTAGAGEVE 237
|
|
| Rubredoxin_2 |
pfam18073 |
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ... |
8-35 |
2.67e-14 |
|
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found in Interest in lipopolysaccharide (LPS) assembly protein B (LapB). Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo. Other family members include RadA proteins which play a role in DNA damage repair. In E. coli, a protein known as RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain.
Pssm-ID: 436248 [Multi-domain] Cd Length: 28 Bit Score: 66.41 E-value: 2.67e-14
10 20
....*....|....*....|....*...
gi 1238239004 8 FICQSCGYESPKWMGKCPGCGAWNTMVE 35
Cdd:pfam18073 1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
83-223 |
4.06e-14 |
|
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: 70.87 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 83 VLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSN-----------SVLYISGEESVKQTKLRADRLGINNPS---L 148
Cdd:pfam13481 25 LIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATGKPwlggprvpeqgKVLYVSAEGPADELRRRLRAAGADLDLparL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 149 HVLSE-----------------TDMEYISSAIQEM-NPSFVVVDSIQTVYQSDITSApgsvSQVRECTAELMKIAKTKGI 210
Cdd:pfam13481 105 LFLSLveslplffldrggplldADVDALEAALEEVeDPDLVVIDPLARALGGDENSN----SDVGRLVKALDRLARRTGA 180
|
170
....*....|...
gi 1238239004 211 PIFIVGHVTKEGS 223
Cdd:pfam13481 181 TVLLVHHVGKDGA 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
90-241 |
2.77e-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: 61.24 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 90 KGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDMEYISSAIQEMNPS 169
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238239004 170 FVVVDsiqtvyqsDITSAPGSVS----QVRECTAELMKIAKTKGIPIFIVGHVTKegsIAGPRLLEHMVDTVLYFE 241
Cdd:smart00382 81 VLILD--------EITSLLDAEQeallLLLEELRLLLLLKSEKNLTVILTTNDEK---DLGPALLRRRFDRRIVLL 145
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
73-275 |
8.67e-11 |
|
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: 61.55 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 73 VKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGIN------NP 146
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERSEALGIDlramveKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 147 SLHVLSETDMEY--------ISSAIQEMNPSFVVVDSIqTVYQSDITSAPGSVSQVRectaELMKIAKTKGIPIFIVG-- 216
Cdd:cd19487 81 LLSIEQIDPAELspgefaqrVRTSVEQEDARVVVIDSL-NGYLNAMPDERFLILQMH----ELLSYLNNQGVTTLLIVaq 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238239004 217 HVTKEGSIAGPRLLEHMVDTVL---YFEGERhhtfRILRA---VKNRFGsTNEMGI--FEMREEGLT 275
Cdd:cd19487 156 HGLLGGDMGTPVDISYLADTVVllrYFEAEG----EVRKAisvLKKRTG-DHERTIreFRITRSGLK 217
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
73-274 |
1.21e-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: 61.49 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 73 VKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQV---SAQLSGSsnSVLYISGEESVKQTKLRADRLGIN----- 144
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFlynGALKYGE--PGVFVTLEEPPEDLRENARSFGWDlekle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 145 --------------NPSLHVLSETDME----YISSAIQEMNPSFVVVDSIQTVYQSDitsapgSVSQVRECTAELMKIAK 206
Cdd:pfam06745 79 eegklaiidastsgIGIAEVEDRFDLEelieRLREAIREIGAKRVVIDSITTLFYLL------KPAVAREILRRLKRVLK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238239004 207 TKGI-PIFIVGHVTKEGSIAGPRLLEHMVDTV--LYFEGERHHTFRILRAVKNRfGSTNEMG--IFEMREEGL 274
Cdd:pfam06745 153 GLGVtAIFTSEKPSGEGGIGGYGVEEFIVDGVirLDLKEIEEERVRTIEIVKMR-GTPHSMKryPFEITDNGI 224
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
61-253 |
1.43e-09 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 59.89 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 61 PITSIE---TSEEPRVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLR 137
Cdd:PRK09302 240 PLTAMRltqRSSNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQLIRN 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 138 ADRLGIN------NPSLHVLS--------ETDMEYISSAIQEMNPSFVVVDSIqtvyqsditSA---PGSVSQVRECTAE 200
Cdd:PRK09302 320 ARSWGIDlekmeeKGLLKIICarpesyglEDHLIIIKREIEEFKPSRVAIDPL---------SAlarGGSLNEFRQFVIR 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238239004 201 LMKIAKTKGI--------PIFIVGHVTKEGSIAGprllehMVDTVL---YFE--GERHHTFRILRA 253
Cdd:PRK09302 391 LTDYLKSEEItglftnltPDFMGSHSITESHISS------LTDTWIllqYVEinGEMNRALYVLKM 450
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
368-453 |
2.23e-09 |
|
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440371 [Multi-domain] Cd Length: 502 Bit Score: 59.28 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 368 PAIDLAIVISIASSFRDTPPNPAD--CFIGEVGLTGEVRRVSRIEQRVKEAAKLGFKRMIIPAANLD--GWtkPKGIEVI 443
Cdd:COG0606 78 SRFDLPIALGILAASGQIPAEALEdyVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAeaAL--VPGIEVY 155
|
90
....*....|
gi 1238239004 444 GVANVAEALR 453
Cdd:COG0606 156 GASSLLEVVA 165
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
84-277 |
4.77e-09 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 56.41 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 84 LGGGVVKGSLVLIGGDPGIGKSTLLLQ--VSAQLSGSsnSVLYISGE----ESVKQ-----TKLRADRLGINNPSlhvls 152
Cdd:PRK09361 16 LGGGFERGTITQIYGPPGSGKTNICLQlaVEAAKNGK--KVIYIDTEglspERFKQiagedFEELLSNIIIFEPS----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 153 etDMEYISSAIQEM------NPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAE---LMKIAKTKGIPIFIVGHV---TK 220
Cdd:PRK09361 89 --SFEEQSEAIRKAeklakeNVGLIVLDSATSLYRLELEDEEDNSKLNRELGRQlthLLKLARKHDLAVVITNQVysdID 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238239004 221 EGSI--AGPRLLEHMVDTVLYFEGERhHTFRILRAVKNRFGSTNEMGIFEMREEGLTEV 277
Cdd:PRK09361 167 SDGLrpLGGHTLEHWSKTILRLEKFR-NGKRRATLEKHRSRPEGESAEFRITDRGIEII 224
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
73-267 |
5.52e-09 |
|
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410893 [Multi-domain] Cd Length: 226 Bit Score: 56.22 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 73 VKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQ-VSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSL--- 148
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQfLVNGIKEFGEPGVFVTFEESPEDIIKNMASFGWDLPKLvae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 149 ---------------HVLSETDME----YISSAIQEMNPSFVVVDSIQTVYQSdiTSAPgsvSQVRectAELMKIA---K 206
Cdd:cd19485 81 gkllildaspepseeEVTGEYDLEalliRIEYAIRKIGAKRVSLDSLEAVFSG--LSDS---AVVR---AELLRLFawlK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238239004 207 TKGIPIFIVGHVTKEGSIAGPRLLEHMVDTVLYF----EGERhhTFRILRAVKNRfGSTNEMGIF 267
Cdd:cd19485 153 QKGVTAIMTGERGEDGPLTRYGVEEYVSDCVVILrnvlEGER--RRRTLEILKYR-GSSHGKGEY 214
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
73-176 |
8.65e-09 |
|
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: 55.82 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 73 VKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHV-- 150
Cdd:cd19488 1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELRAVALSHGWSLDGIHIfe 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1238239004 151 -----------------------LSETdMEYISSAIQEMNPSFVVVDSI 176
Cdd:cd19488 81 lspsesaldaaqqytilhpseleLSET-TRLIFERVERLKPSRVVIDSL 128
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
368-430 |
8.80e-09 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 53.22 E-value: 8.80e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238239004 368 PAIDLAIVISIASSFRDTPPNPADCFIGEVGLTGEVRRVSRIEQRVKEAAKLGFKRMIIPAAN 430
Cdd:pfam13541 59 SSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
79-274 |
4.43e-08 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 53.69 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTL--LLQVSAQL----SGSSNSVLYISGEESVKQTKLR--ADRLGINNPSL-- 148
Cdd:cd01123 7 ELDKLLGGGIETGSITEMFGEFRTGKTQLchTLAVTCQLpidrGGGEGKAIYIDTEGTFRPERLRaiAQRFGLDPDDVld 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 149 HVLS----ETD-----MEYISSAIQEMNPSFVVVDSIQTVYQSDItSAPGSVSQVRECTAE----LMKIAKTKGIPIFIV 215
Cdd:cd01123 87 NVAYarafNSDhqtqlLDQAAAMMVESRFKLLIVDSATALYRTDY-SGRGELSARQMHLAKflrmLQRLADEFGVAVVVT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 216 GHVTKE--GSIA---------GPRLLEHMVDTVLYFEGERHHTfRILRAVKNRFGSTNEmGIFEMREEGL 274
Cdd:cd01123 166 NQVVAQvdGAMMfaadpkkpiGGNILAHASTTRLYLRKGRGET-RICKIYDSPCLPEAE-AVFAITADGV 233
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
82-243 |
6.36e-08 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 53.45 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 82 RVLGGGVVKGSLVLIGGDPGIGKSTLLLQ--VSAQLS----GSSNSVLYISGEESVKQTKLR--ADRLGINNPSLHVLSE 153
Cdd:cd19491 3 ELLGGGIPVGGITEIAGESGAGKTQLCLQlaLTVQLPrelgGLGGGAVYICTESSFPSKRLQqlASSLPKRYHLEKAKNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 154 TD---------MEYISSAIQEMNPSF--------VVVDSIQTVYQSDITSAPGSVSQ----VRECTAELMKIAKTKGIPI 212
Cdd:cd19491 83 LDnifvehvadLETLEHCLNYQLPALlergpirlVVIDSIAALFRSEFDTSRSDLVErakyLRRLADHLKRLADKYNLAV 162
|
170 180 190
....*....|....*....|....*....|....
gi 1238239004 213 FIVGHVT---KEGSIAGPRLLEHMVDTVLYFEGE 243
Cdd:cd19491 163 VVVNQVTdrfDSSSDASGLGVLDYLSQFSSFSGG 196
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
79-176 |
1.63e-07 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 52.14 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQ--TKLRADRLGINNP---------S 147
Cdd:COG2874 9 ELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTTKEfiKQMKSLSYDISDYllrgrllflP 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1238239004 148 LHVLSETD------------MEYISSAIQEMNpsFVVVDSI 176
Cdd:COG2874 89 VHPLGFEWnskqrkdllkrlMKYIASNLWEAD--VIIIDSL 127
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
91-219 |
3.90e-07 |
|
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: 50.04 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 91 GSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGE------------ESVKQTKLRADRLGinnPSLHVLSETD--- 155
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEgafppsrlvqilEASPSSELELAEAL---SRLLYFRPPDtla 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238239004 156 -MEYISSAIQEMNP----SFVVVDSIQTVYQSDITSAPGSVSQVRE-------CTAELMKIAKTKGIPIFIVGHVT 219
Cdd:cd01393 78 hLLALDSLPESLFPppntSLVVVDSVSALFRKAFPRGGDGDSSSSLrarllsqLARALQKLAAQFNLAVVVTNQVT 153
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
94-221 |
5.30e-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: 48.27 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 94 VLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKqtklradrlginnpslhvlsetdmEYISSAIQEMNPSFVVV 173
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL------------------------EAIEDLIEEKKLDIIII 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1238239004 174 DSIQTVYQSditSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVTKE 221
Cdd:cd01120 57 DSLSSLARA---SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKF 101
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
68-218 |
6.60e-07 |
|
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: 50.38 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 68 SEEPRVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTL--LLQVSAQL----SGSSNSVLYISGEESVKQTKLR--AD 139
Cdd:pfam08423 14 SELIQITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLchTLCVTCQLplemGGGEGKALYIDTEGTFRPERLVaiAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 140 RLGINnpSLHVL----------SETDMEYISSAIQEMNPS---FVVVDSIQTVYQSDItSAPGSVSQVRECTAELM---- 202
Cdd:pfam08423 94 RYGLD--PEDVLdnvayaraynSEHQMQLLQQAAAMMSESrfaLLIVDSATALYRTDF-SGRGELAERQQHLAKFLrtlq 170
|
170
....*....|....*.
gi 1238239004 203 KIAKTKGIPIFIVGHV 218
Cdd:pfam08423 171 RLADEFGVAVVITNQV 186
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
80-274 |
1.15e-06 |
|
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: 49.23 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 80 FNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGE----ESVKQ-----TKLRADRLGINNPSLHV 150
Cdd:cd01394 8 LDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEglspERFQQiagerFESIASNIIVFEPYSFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 151 LSETDMEYISSAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHV---TKEGSIA-- 225
Cdd:cd01394 88 EQGVAIQEAEKLLKSDKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLSIARKYDIPVVITNQVysdIDDDRLKpv 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1238239004 226 GPRLLEHMVDTVLYFE----GERHHTFRilravKNRFGSTNEMGIFEMREEGL 274
Cdd:cd01394 168 GGTLLEHWSKAIIRLEksppGLRRATLE-----KHRSRPEGQSAGFRITDRGI 215
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
81-256 |
7.50e-06 |
|
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: 46.93 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 81 NRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLS------GSSNSVLYISGEESVKQTKLRAD--------RLGINNP 146
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkgGLDGGVLYIDTESKFSAERLAEIaearfpeaFSGFMEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 147 S---------LHVLSETD-------MEYISSAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAELM----KIAK 206
Cdd:cd19493 81 NeraeemlkrVAVVRVTTlaqllerLPNLEEHILSSGVRLVVIDSIAALVRREFGGSDGEVTERHNALAREAsslkRLAE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 207 TKGIPIFIVGHVTKEGSIAGP----------RLLEHMVDTVLYFEGERHHTFRILRAVKN 256
Cdd:cd19493 161 EFRIAVLVTNQATTHFGDAGDgssgvtaalgDAWAHAVNTRLRLERCLLQLRRVLEIVKS 220
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
85-213 |
8.80e-06 |
|
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: 46.55 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 85 GGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGIN---------------NPSLH 149
Cdd:cd19484 14 GGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQLIRNAKSIGIDleqmerkgllkiicaRPELY 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238239004 150 VLsETDMEYISSAIQEMNPSFVVVDSIQTVyqsditSAPGSVSQVRECTAELMKIAKTKGIPIF 213
Cdd:cd19484 94 GL-EDHLIIIKSEINEFKPSRVIVDPLSAL------ARGGSLNEVKEFVIRLIDYLKSQEITGL 150
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
34-218 |
2.61e-05 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 46.14 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 34 VEEMIKKAPANRRAAFSHSVQTVQKPSPITSIETSEEprvktqlgEFNRVLGGGVVKGSLVLIGGDPGIGKSTL--LLQV 111
Cdd:PTZ00035 69 VEKIKEAASKLVPMGFISATEYLEARKNIIRITTGST--------QLDKLLGGGIETGSITELFGEFRTGKTQLchTLCV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 112 SAQL----SGSSNSVLYISGEESVKQTKLR--ADRLGINnpSLHVLS----------ETDMEYISSAIQEMNPS---FVV 172
Cdd:PTZ00035 141 TCQLpieqGGGEGKVLYIDTEGTFRPERIVqiAERFGLD--PEDVLDniayaraynhEHQMQLLSQAAAKMAEErfaLLI 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1238239004 173 VDSIQTVYQSDItSAPGSVS--QVRECT--AELMKIAKTKGIPIFIVGHV 218
Cdd:PTZ00035 219 VDSATALFRVDY-SGRGELAerQQHLGKflRALQKLADEFNVAVVITNQV 267
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
79-219 |
3.89e-05 |
|
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.
Pssm-ID: 410921 [Multi-domain] Cd Length: 235 Bit Score: 45.00 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTLL--LQVSAQL----SGSSNSVLYISGEESVKQTKLR--ADRLGINnpSLHV 150
Cdd:cd19513 7 ELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLpidqGGGEGKALYIDTEGTFRPERLLaiAERYGLN--GEDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 151 L----------SETDMEYISSAIQEMNPS---FVVVDSIQTVYQSDItSAPGSVSQVRECTAE----LMKIAKTKGIPIF 213
Cdd:cd19513 85 LdnvayaraynTDHQMQLLIQASAMMAESryaLLIVDSATALYRTDY-SGRGELSARQMHLAKflrmLQRLADEFGVAVV 163
|
....*.
gi 1238239004 214 IVGHVT 219
Cdd:cd19513 164 ITNQVV 169
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
64-290 |
4.06e-05 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 46.03 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 64 SIETSEEPRVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQ-VSAQLSGSSNSVLYISGEESVKQTKLRADRLG 142
Cdd:PRK09302 4 PSASPGIEKLPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQfLVNGIKRFDEPGVFVTFEESPEDIIRNVASFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 143 INNPSL---------HV---LSETDM--EY--------ISSAIQEMNPSFVVVDSIQTVYQSdiTSAPGsvsQVRectAE 200
Cdd:PRK09302 84 WDLQKLidegklfilDAspdPSEQEEagEYdlealfirIEYAIDKIGAKRVVLDSIEALFSG--FSNEA---VVR---RE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 201 LMKIA---KTKGIPIFIVGHVTKE-GSIAGPRLLEHMVDTVLY----FEGERhhTFRILRAVKNRfGS---TNEMGiFEM 269
Cdd:PRK09302 156 LRRLFawlKQKGVTAVITGERGDEyGPLTRYGVEEFVSDCVIIlrnrLEGEK--RTRTLRILKYR-GTthgKNEYP-FTI 231
|
250 260
....*....|....*....|.
gi 1238239004 270 REEGLTeVLNPSEIFLEERSA 290
Cdd:PRK09302 232 TEDGIS-VLPLTAMRLTQRSS 251
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
79-185 |
4.55e-05 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 44.58 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNP-----------S 147
Cdd:PRK06067 13 ELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKSYLKQMESVKIDISdfflwgylrifP 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1238239004 148 LHV--------LSETDMEYISSAIQEMNPSFVVVDS--IQTVYQSDIT 185
Cdd:PRK06067 93 LNTegfewnstLANKLLELIIEFIKSKREDVIIIDSltIFATYAEEDD 140
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
79-219 |
6.72e-05 |
|
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: 44.27 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTL--LLQVSAQLSGSSN----SVLYISGEESVKQTKLR--ADRLGINNPSL-- 148
Cdd:cd19514 7 ELDKLLGGGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSMGggggKVAYIDTEGTFRPDRIRpiAERFGVDHDAVld 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 149 HVL------SETDMEYISSAIQEM--NPSF--VVVDSIQTVYQSDItSAPGSVSQVRECTAE----LMKIAKTKGIPIFI 214
Cdd:cd19514 87 NILyaraytSEHQMELLDYVAAKFheEAVFrlLIIDSIMALFRVDF-SGRGELAERQQKLAQmlsrLQKISEEYNVAVFI 165
|
....*
gi 1238239004 215 VGHVT 219
Cdd:cd19514 166 TNQVT 170
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
34-219 |
7.56e-05 |
|
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA repair and recombination proteins. It is eukaryotic only and most closely related to eukaryotic RAD51. It also resembles archaeal RadA (TIGR02236) and RadB (TIGR02237) and bacterial RecA (TIGR02012). It has been characterized for human as a recombinase active only in meiosis.
Pssm-ID: 131292 [Multi-domain] Cd Length: 313 Bit Score: 44.38 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 34 VEEMIKKAPANRRAAFSHSVQTVQKPSPITSIETSEEprvktqlgEFNRVLGGGVVKGSLVLIGGDPGIGKSTL--LLQV 111
Cdd:TIGR02238 47 VDKIKEAASKIINPGFITAFEISQKRKKVLKITTGSQ--------ALDGILGGGIESMSITEVFGEFRCGKTQLshTLCV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 112 SAQL----SGSSNSVLYISGEESVKQTKLR--ADRLGINNPSL--HVL------SETDMEYISSAIQEMNPS---FVVVD 174
Cdd:TIGR02238 119 TAQLpremGGGNGKVAYIDTEGTFRPDRIRaiAERFGVDPDAVldNILyaraytSEHQMELLDYLAAKFSEEpfrLLIVD 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238239004 175 SIQTVYQSDItSAPGSVSQVRECTAELM----KIAKTKGIPIFIVGHVT 219
Cdd:TIGR02238 199 SIMALFRVDF-SGRGELSERQQKLAQMLsrlnKISEEFNVAVFVTNQVQ 246
|
|
| PRK08533 |
PRK08533 |
flagellar accessory protein FlaH; Reviewed |
79-215 |
2.02e-04 |
|
flagellar accessory protein FlaH; Reviewed
Pssm-ID: 181459 Cd Length: 230 Bit Score: 42.75 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGE----ESVKQTK----------LRADRLGIN 144
Cdd:PRK08533 12 ELHKRLGGGIPAGSLILIEGDESTGKSILSQRLAYGFLQNGYSVSYVSTQltttEFIKQMMslgydinkklISGKLLYIP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238239004 145 NPSLHVLSETDMEYISSAIQE---MNPSFVVVDSIQTVYQSDItsapgSVSQVRECTAELMKIAKTKGIPIFIV 215
Cdd:PRK08533 92 VYPLLSGNSEKRKFLKKLMNTrrfYEKDVIIIDSLSSLISNDA-----SEVAVNDLMAFFKRISSLNKVIILTA 160
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
80-129 |
2.59e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 2.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1238239004 80 FNRVLGGgvvKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEE 129
Cdd:COG3899 303 LERARAG---RGELVLVSGEAGIGKSRLVRELARRARARGGRVLRGKCDQ 349
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
79-219 |
3.88e-04 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 42.40 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTL--LLQVSAQLS----GSSNSVLYISGEESVKQTKLR--ADRLGInNPSlHV 150
Cdd:TIGR02239 84 ELDKLLGGGIETGSITEIFGEFRTGKTQLchTLAVTCQLPidqgGGEGKALYIDTEGTFRPERLLaiAERYGL-NPE-DV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 151 L----------SETDMEYISSAIQEMNPS---FVVVDSIQTVYQSDItSAPGSVSQVRECTAE----LMKIAKTKGIPIF 213
Cdd:TIGR02239 162 LdnvayaraynTDHQLQLLQQAAAMMSESrfaLLIVDSATALYRTDF-SGRGELSARQMHLARflrsLQRLADEFGVAVV 240
|
....*.
gi 1238239004 214 IVGHVT 219
Cdd:TIGR02239 241 ITNQVV 246
|
|
| FlaH |
cd19475 |
flagellar accessory protein FlaH; Flagellar accessory protein FlaH is part of the motor of the ... |
79-215 |
9.74e-04 |
|
flagellar accessory protein FlaH; Flagellar accessory protein FlaH is part of the motor of the archaellum membrane-anchored archaeal motility structure, together with FlaX and FlaI. FlaH forms a hexameric ring, and binds ATP which is essential for its interaction with FlaI and for archaellum assembly.
Pssm-ID: 410883 Cd Length: 220 Bit Score: 40.66 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 79 EFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGIN-NPSL--------- 148
Cdd:cd19475 7 DLDKRLGGGIPYPSSIMIEGEESTGKSVLSQRLVYGFLQNDYSGYYISTQQTTKEFLKQMKSLKYDiNKKLlrgkllyip 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238239004 149 -------HVLSETDMEYISSAIQEMNPSFVVVDSIQTVYQSDitsapGSVSQVRECTAELMKIAKTKGIPIFIV 215
Cdd:cd19475 87 vyplifdNSLKDKFLKKIVNTRAFYEKDFIIFDSLSILIAND-----ASEVQVLDLMKFIKRIVNTGKIILFTI 155
|
|
| PRK04328 |
PRK04328 |
hypothetical protein; Provisional |
71-235 |
1.14e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235281 Cd Length: 249 Bit Score: 40.45 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 71 PRVKTQLGEFNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEE---SVKQ---------TKLRA 138
Cdd:PRK04328 3 KRVKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLQMGEPGVYVALEEhpvQVRRnmrqfgwdvRKYEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 139 DRL---------GINNPS---LHVLSETD-----MEYISSAIQEMNPSFVVVDSIQTVYQSDITSAPGSVSQVRECTAEL 201
Cdd:PRK04328 83 EGKfaivdaftgGIGSAAkreKYVVKDPDdvrelIDVLRQAIKDIGAKRVVIDSVSTLYLTKPAMARSIVMQLKRVLSGL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1238239004 202 mkiaktkGIPIFIVGHVT-KEGSIAGPRlLEHMVD 235
Cdd:PRK04328 163 -------GCTAIFVSQVSvGERGFGGPG-VEHAVD 189
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
80-131 |
1.15e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 39.79 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1238239004 80 FNRVLGGGvvkGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESV 131
Cdd:pfam13191 16 LDRVRSGR---PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENL 64
|
|
| PRK05973 |
PRK05973 |
replicative DNA helicase; Provisional |
91-214 |
1.18e-03 |
|
replicative DNA helicase; Provisional
Pssm-ID: 168322 [Multi-domain] Cd Length: 237 Bit Score: 40.40 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 91 GSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADRLGINNPSLHVLSETDM-EYISSA--IQEMN 167
Cdd:PRK05973 64 GDLVLLGARPGHGKTLLGLELAVEAMKSGRTGVFFTLEYTEQDVRDRLRALGADRAQFADLFEFDTsDAICADyiIARLA 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1238239004 168 P----SFVVVDSIQTVYQSdiTSAPGSVSQVRectaELMKIAKTKG-IPIFI 214
Cdd:PRK05973 144 SaprgTLVVIDYLQLLDQR--REKPDLSVQVR----ALKSFARERGlIIVFI 189
|
|
| PRK11788 |
PRK11788 |
tetratricopeptide repeat protein; Provisional |
3-33 |
1.53e-03 |
|
tetratricopeptide repeat protein; Provisional
Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 40.56 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|.
gi 1238239004 3 KTKSKFICQSCGYESPKWMGKCPGCGAWNTM 33
Cdd:PRK11788 350 KRKPRYRCRNCGFTARTLYWHCPSCKAWETI 380
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
91-223 |
2.70e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 39.29 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 91 GSLVLIGGDPGIGKSTLLLQVSAQLSGSSN----------SVLYISGEE----------SVKQTKLRADRLGINNPSLHV 150
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVATGRDwlgerrvkqgRVVYLAAEDprdglrrrlkAIGAHLGDEDAALAENLVIEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 151 LSE---TDMEYISSAIQEM----NPSFVVVDSIQTVYQSDITSAPGSVSQVrecTAELMKIAKTKGIPIFIVGHVTKEGS 223
Cdd:cd01125 81 LRGkpvSIDAEAPELERIIeeleGVRLIIIDTLARVLHGGDENDAADMGAF---VAGLDRIARETGAAVLLVHHTGKDAA 157
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
91-219 |
3.72e-03 |
|
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: 38.36 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 91 GSLVLIGGDPGIGKSTLLLQ--VSAQL----SGSSNSVLYISGEESVKqtklradrlginnpsLHVLSETDMEYISSAIQ 164
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQlaVNVQIpkcfGGLAGEAIYIDTEGSFN---------------IHYFRVHDYVELLALIN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238239004 165 EMnPSF---------VVVDSIQTVYQSDITSAPGSVSQVRECTAELMKIAKTKGIPIFIVGHVT 219
Cdd:cd19492 66 SL-PKFledhpkvklIVVDSIAFPFRHDFDDLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVT 128
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
86-213 |
4.21e-03 |
|
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase DnaB unwinds the DNA duplex at the chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.
Pssm-ID: 410864 [Multi-domain] Cd Length: 256 Bit Score: 38.65 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 86 GGVVKGSLVLIGGDPGIGKSTLLLQVSAQ-LSGSSNSVLYISGEESVKQTKLR--ADRLGINNPSLH--VLSETDMEYIS 160
Cdd:cd00984 14 GGLQPGDLIIIAARPSMGKTAFALNIAENiALDEGLPVLFFSLEMSAEQLAERllSSESGVSLSKLRtgRLDDEDWERLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 161 SAIQEM------------------------------NPSFVVVDSIQTvyqsdITSAPGSVS---QVRECTAELMKIAKT 207
Cdd:cd00984 94 AAMGELselplyiddtpgltvdeirakarrlkrehgGLGLIVIDYLQL-----IRGSKRAENrqqEVAEISRSLKALAKE 168
|
....*.
gi 1238239004 208 KGIPIF 213
Cdd:cd00984 169 LNVPVI 174
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
94-180 |
4.46e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 37.51 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 94 VLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGEESVKQTKLRADrlgINNPSLHVLSEtdmeyissAIQEMNPSFVVV 173
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---FGHFLVRLLFE--------LAEKAKPGVLFI 90
|
....*..
gi 1238239004 174 DSIQTVY 180
Cdd:cd00009 91 DEIDSLS 97
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
360-458 |
7.07e-03 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 37.60 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 360 AGGVKLDEPAIDLAIVISIASSFRDTPPNPADCFIGEVGLTGEVRRVSRIEQRVKEAAKLGFKRMIIPAANLDGWTK-PK 438
Cdd:pfam05362 102 EGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDLEDiPE 181
|
90 100
....*....|....*....|....
gi 1238239004 439 ----GIEVIGVANVAEALRTSLGG 458
Cdd:pfam05362 182 nvreGLEIIPVEHVDEVLKHALVG 205
|
|
| 41 |
PHA02542 |
41 helicase; Provisional |
80-160 |
8.11e-03 |
|
41 helicase; Provisional
Pssm-ID: 222864 [Multi-domain] Cd Length: 473 Bit Score: 38.50 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238239004 80 FNRVLGGGVVKGSLVLIGGDPGIGKSTLLLQVSAQLSGSSNSVLYISGE--ESVKQTKLRADRLGINNPSLHVLSETdmE 157
Cdd:PHA02542 179 LNKITKGGAERKTLNVLLAGVNVGKSLGLCSLAADYLQQGYNVLYISMEmaEEVIAKRIDANLLDVSLDDIDDLSKA--E 256
|
...
gi 1238239004 158 YIS 160
Cdd:PHA02542 257 YKA 259
|
|
| |
