|
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: 847.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 1 MAKRKTKFVCQDCGYEVAKWLGKCPGCNNWNTFVEEIEITGGRQKQAFQTGNRSVgKPEKITAIKSQQEPRVTTDMKEFN 80
Cdd:COG1066 1 MAKTKTVYVCQECGYESPKWLGRCPECGAWNTLVEEVVAKAKKGRAASGAAGRAS-KPVPLSEVEAEEEPRISTGIGELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 81 RVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYVLAETNLLDIAN 160
Cdd:COG1066 80 RVLGGGLVPGSVVLIGGEPGIGKSTLLLQVAARLAKKGGKVLYVSGEESASQIKLRAERLGLLSDNLYLLAETDLEAILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 161 QIEAIKPSFVVIDSIQTVYREEITSAPGSVSQVRECTSELMKIAKTNGIPIFIVGHVTKEGTIAGPRLLEHMVDAVLYFE 240
Cdd:COG1066 160 TIEELKPDLLVIDSIQTMYSEELESAPGSVSQVRECAAELIRLAKETGIAVFLVGHVTKEGSIAGPRVLEHMVDTVLYFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 241 GERHHTYRILRGVKNRFGSTNEMGIFEMKEAGLREVLNPSEIFLEERSQGASGSTVVASMEGTRPVLVEIQALISPTAFG 320
Cdd:COG1066 240 GDRHSRYRILRAVKNRFGSTNEIGVFEMTEKGLREVSNPSELFLSERDEPVPGSAVTVTMEGTRPLLVEVQALVSPSSFG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 321 NPRRMATGVDQNRVPLLMAVLEKRVGLMLQNQDAYIKVAGGVRLDEPAIDLAIAVSIASSFRDQPTKPEDIFIGEVGLTG 400
Cdd:COG1066 320 NPRRTAVGLDSNRLAMLLAVLEKRAGLPLGDQDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGEVGLTG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1318755049 401 EIRRVSRIEQRVQEAAKLGFKRVICPKNNLGGWtTPNNIEIIGVNTVQEALQI 453
Cdd:COG1066 400 EIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKL-KPKGIEIIGVSTLEEALEA 451
|
|
| sms |
TIGR00416 |
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved ... |
1-451 |
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: 700.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 1 MAKRKTKFVCQDCGYEVAKWLGKCPGCNNWNTFVEEIEI-TGGRQKQ---AFQTGNRSVGKPEKITAIKSQQEPRVTTDM 76
Cdd:TIGR00416 1 MAKAKSKFVCQHCGADSPKWQGKCPACHAWNTITEERLHrSLGAQKNrrnSGKAGIPQAQKSQTISAIELEEVPRFSSGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 77 KEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYVLAETNLL 156
Cdd:TIGR00416 81 GELDRVLGGGIVPGSLILIGGDPGIGKSTLLLQVACQLAKNQMKVLYVSGEESLQQIKMRAIRLGLPEPNLYVLSETNWE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 157 DIANQIEAIKPSFVVIDSIQTVYREEITSAPGSVSQVRECTSELMKIAKTNGIPIFIVGHVTKEGTIAGPRLLEHMVDAV 236
Cdd:TIGR00416 161 QICANIEEENPQACVIDSIQTLYSPDISSAPGSVSQVRECTAELMRLAKTRGIAIFIVGHVTKEGSIAGPKVLEHMVDTV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 237 LYFEGERHHTYRILRGVKNRFGSTNEMGIFEMKEAGLREVLNPSEIFLEERSQGASGSTVVASMEGTRPVLVEIQALISP 316
Cdd:TIGR00416 241 LYFEGDRDSRFRILRSVKNRFGATNEIGIFEMTEQGLREVLNPSAIFLSRREEPMSGSSITVTWEGTRPLLVEIQALVSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 317 TAFGNPRRMATGVDQNRVPLLMAVLEKRVGLMLQNQDAYIKVAGGVRLDEPAIDLAIAVSIASSFRDQPTKPEDIFIGEV 396
Cdd:TIGR00416 321 TSFANPRRVATGLDQNRLALLLAVLEKRLGLPLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFLGEV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1318755049 397 GLTGEIRRVSRIEQRVQEAAKLGFKRVICPKNNLGGwTTPNNIEIIGVNTVQEAL 451
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 ... |
8-276 |
1.94e-174 |
|
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: 489.35 E-value: 1.94e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 8 FVCQDCGYEVAKWLGKCPGCNNWNTFVEEIEITGGRqKQAFQTGNRSVGKPEKITAIKSQQEPRVTTDMKEFNRVLGGGI 87
Cdd:cd01121 1 YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSS-ASRRASASPSPSKPLPLSDVEAEEEERISTGIGELDRVLGGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 88 VPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYVLAETNLLDIANQIEAIKP 167
Cdd:cd01121 80 VPGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIKLRAERLGLGSDNLYLLAETNLEAILAEIEELKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 168 SFVVIDSIQTVYREEITSAPGSVSQVRECTSELMKIAKTNGIPIFIVGHVTKEGTIAGPRLLEHMVDAVLYFEGERHHTY 247
Cdd:cd01121 160 SLVVIDSIQTVYSPELTSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVTKDGAIAGPKVLEHMVDTVLYFEGDRGSSY 239
|
250 260
....*....|....*....|....*....
gi 1318755049 248 RILRGVKNRFGSTNEMGIFEMKEAGLREV 276
Cdd:cd01121 240 RILRSVKNRFGPTNEIGVFEMTENGLREV 268
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
71-274 |
2.73e-24 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 100.38 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 71 RVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLG--------- 141
Cdd:COG0467 1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRAESLGldleeyies 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 142 -------VTSDELYVLAETNLLDIANQIEAIKPSFVVIDSIqtvyrEEITSAPGSVSQVRECTSELMKIAKTNGIPIFIV 214
Cdd:COG0467 81 gllriidLSPEELGLDLEELLARLREAVEEFGAKRVVIDSL-----SGLLLALPDPERLREFLHRLLRYLKKRGVTTLLT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1318755049 215 GHVTKEGTIAGPRLLEHMVDAVLYF-----EGERHHTYRILrgvKNRfGSTNEMGIFEMK--EAGLR 274
Cdd:COG0467 156 SETGGLEDEATEGGLSYLADGVILLryvelGGELRRALSVL---KMR-GSAHDRTIREFEitDGGIE 218
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
86-346 |
3.57e-18 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 84.95 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 86 GIVP-GSLVLVGGDPGIGKSTLLLQISSQLAD---------KSLSVLYISGEESTRQTKLRADRLG--------VTSDEL 147
Cdd:COG3598 8 GLLPeGGVTLLAGPPGTGKSFLALQLAAAVAAggpwlgrrvPPGKVLYLAAEDDRGELRRRLKALGadlglpfaDLDGRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 148 YVLAETNLLD-------IANQIEAIKPSFVVIDSIQTVYR-EEITSApgsvsQVRECTSELMKIAKTNGIPIFIVGHVTK 219
Cdd:COG3598 88 RLLSLAGDLDdtddleaLERAIEEEGPDLVVIDPLARVFGgDENDAE-----EMRAFLNPLDRLAERTGAAVLLVHHTGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 220 EG----TIAGPR---LLEHMVDAVLYFEGERHHTYRILRGVKNRFGSTNEMGIFEMKEAGLREVLNPSEIFLEERSQGAS 292
Cdd:COG3598 163 GGagkdSGDRARgssALRGAARSVLVLSREKGEDLRVLTRAKSNYGPEIALRWDNGGRLALEEVAALTAGAGEVELKELV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1318755049 293 GSTVVASMEGTRPVLVEIQALISPTAFGNPRRMATGVDQNRVPLLMAVLEKRVG 346
Cdd:COG3598 243 GGVARTGTDSELEEGLLEVPLAEAESAGEDAELAAKAVADEKDAARAVARLKAG 296
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
72-269 |
4.89e-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: 79.62 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQ-ISSQLADKSlSVLYISGEESTRQTKLRADRLG------VTS 144
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQfLYAGAKNGE-PGLFFTFEESPERLLRNAKSFGwdfdemEDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 145 DELYVLAETN-----------LLDIANQIEAIKPSFVVIDSIQTVYREEITSapgsvSQVRECTSELMKIAKTNGIPIFI 213
Cdd:cd01124 80 GKLIIVDAPPteagrfsldelLSRILSIIKSFKAKRVVIDSLSGLRRAKEDQ-----MRARRIVIALLNELRAAGVTTIF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318755049 214 VG--HVTKEGTIAGPRLLEHMVDAV--LYF---EGERHhtyRILRGVKNRFGStNEMGIFEMK 269
Cdd:cd01124 155 TSemRSFLSSESAGGGDVSFIVDGVilLRYveiEGELR---RTIRVLKMRGTG-HDTGTHPFE 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
89-240 |
2.60e-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: 64.32 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 89 PGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYVLAETNLLDIANQIEAIKPS 168
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1318755049 169 FVVIDsiqtvyreEITSAPGSVS----QVRECTSELMKIAKTNGIPIFIVGHvtkEGTIAGPRLLEHMVDAVLYFE 240
Cdd:smart00382 81 VLILD--------EITSLLDAEQeallLLLEELRLLLLLKSEKNLTVILTTN---DEKDLGPALLRRRFDRRIVLL 145
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
82-221 |
7.52e-12 |
|
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: 63.94 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 82 VLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLAD-----------KSLSVLYISGEESTRQTKLRADRLGVT---SDEL 147
Cdd:pfam13481 25 LIKGLLPAGGLGLLAGAPGTGKTTLALDLAAAVATgkpwlggprvpEQGKVLYVSAEGPADELRRRLRAAGADldlPARL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 148 YVL--------------AETNLLDIANQIEAIK----PSFVVIDSIQTVYREEITSApgsvSQVRECTSELMKIAKTNGI 209
Cdd:pfam13481 105 LFLslveslplffldrgGPLLDADVDALEAALEevedPDLVVIDPLARALGGDENSN----SDVGRLVKALDRLARRTGA 180
|
170
....*....|..
gi 1318755049 210 PIFIVGHVTKEG 221
Cdd:pfam13481 181 TVLLVHHVGKDG 192
|
|
| Rubredoxin_2 |
pfam18073 |
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ... |
8-35 |
8.62e-12 |
|
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: 59.09 E-value: 8.62e-12
10 20
....*....|....*....|....*...
gi 1318755049 8 FVCQDCGYEVAKWLGKCPGCNNWNTFVE 35
Cdd:pfam18073 1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
72-274 |
1.69e-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: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQ-ISSQLADKSLSVLYISGEESTRQTKLRADRLG--------- 141
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLEEPPEDLRENARSFGwdlekleee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 142 --------VTSDELYVLAETN------LLDIANQIEAIKPSFVVIDSIQTVYREEitsapgSVSQVRECTSELMKIAKTN 207
Cdd:pfam06745 81 gklaiidaSTSGIGIAEVEDRfdleelIERLREAIREIGAKRVVIDSITTLFYLL------KPAVAREILRRLKRVLKGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1318755049 208 GI-PIFIVGHVTKEGTIAGPRLLEHMVDAV--LYFEGERHHTYRILRGVKNRfGSTNEMG--IFEMKEAGLR 274
Cdd:pfam06745 155 GVtAIFTSEKPSGEGGIGGYGVEEFIVDGVirLDLKEIEEERVRTIEIVKMR-GTPHSMKryPFEITDNGIV 225
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
72-175 |
3.06e-11 |
|
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: 63.14 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYVL- 150
Cdd:cd19488 1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELRAVALSHGWSLDGIHIFe 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1318755049 151 -------------------AETNLLDIANQI----EAIKPSFVVIDSI 175
Cdd:cd19488 81 lspsesaldaaqqytilhpSELELSETTRLIfervERLKPSRVVIDSL 128
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
367-429 |
2.22e-10 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 57.84 E-value: 2.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318755049 367 PAIDLAIAVSIASSFRDQPTKPEDIFIGEVGLTGEIRRVSRIEQRVQEAAKLGFKRVICPKNN 429
Cdd:pfam13541 59 SSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
72-274 |
3.46e-10 |
|
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: 59.64 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGE--ESTRQTKLRADRLGVTSDELYV 149
Cdd:cd01394 1 LSTGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEglSPERFQQIAGERFESIASNIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 150 LAETnllDIANQIEAIKPSF----------VVIDSIQTVYREEITSAPGSVSQVRECTSELMKIAKTNGIPIFIVGHV-- 217
Cdd:cd01394 81 FEPY---SFDEQGVAIQEAEkllksdkvdlVVVDSATALYRLELGDDSEANRELSRQMSKLLSIARKYDIPVVITNQVys 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318755049 218 -TKEGTIA--GPRLLEHMVDAVLYFE----GERHHTYRilrgvKNRFGSTNEMGIFEMKEAGLR 274
Cdd:cd01394 158 dIDDDRLKpvGGTLLEHWSKAIIRLEksppGLRRATLE-----KHRSRPEGQSAGFRITDRGIR 216
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
367-452 |
1.85e-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: 59.67 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 367 PAIDLAIAVSI-ASSFRDQPTKPED-IFIGEVGLTGEIRRVSRIEQRVQEAAKLGFKRVICPKNNLG--GWttPNNIEII 442
Cdd:COG0606 78 SRFDLPIALGIlAASGQIPAEALEDyVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAeaAL--VPGIEVY 155
|
90
....*....|
gi 1318755049 443 GVNTVQEALQ 452
Cdd:COG0606 156 GASSLLEVVA 165
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
71-131 |
2.19e-09 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 57.53 E-value: 2.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1318755049 71 RVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTR 131
Cdd:COG2874 2 IISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTTK 62
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
72-218 |
2.19e-09 |
|
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic proteins RAD51, RAD55/57 and the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as RAD55/57 .
Pssm-ID: 410868 [Multi-domain] Cd Length: 234 Bit Score: 57.54 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQL----ADKSLSVLYISGEESTRQTKLR--ADRLGVT 143
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLchTLAVTCQLpidrGGGEGKAIYIDTEGTFRPERLRaiAQRFGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 144 SDE-----LYVLA-----ETNLLDIANQ-IEAIKPSFVVIDSIQTVYREEItSAPGSVS----QVRECTSELMKIAKTNG 208
Cdd:cd01123 81 PDDvldnvAYARAfnsdhQTQLLDQAAAmMVESRFKLLIVDSATALYRTDY-SGRGELSarqmHLAKFLRMLQRLADEFG 159
|
170
....*....|
gi 1318755049 209 IPIFIVGHVT 218
Cdd:cd01123 160 VAVVVTNQVV 169
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
68-276 |
7.45e-09 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 56.02 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 68 QEPRVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEestrqtklradrlGVTSDEL 147
Cdd:PRK09361 1 MDERLPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTE-------------GLSPERF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 148 YVLAETNLLDIAN------------QIEAIKP---------SFVVIDSIQTVYREEITSAPGSVSQVRECTSE---LMKI 203
Cdd:PRK09361 68 KQIAGEDFEELLSniiifepssfeeQSEAIRKaeklakenvGLIVLDSATSLYRLELEDEEDNSKLNRELGRQlthLLKL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1318755049 204 AKTNGIPIFIVGHV---TKEGTI--AGPRLLEHMVDAVLYFEGERhHTYRILRGVKNRFGSTNEMGIFEMKEAGLREV 276
Cdd:PRK09361 148 ARKHDLAVVITNQVysdIDSDGLrpLGGHTLEHWSKTILRLEKFR-NGKRRATLEKHRSRPEGESAEFRITDRGIEII 224
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
72-242 |
1.27e-08 |
|
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: 55.00 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVtsdELYVLA 151
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERSEALGI---DLRAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 152 ETNLLDIAN-----------------QIEAIKPSFVVIDSIqTVYREEITSAPGSVSQVRectsELMKIAKTNGIPIFIV 214
Cdd:cd19487 78 EKGLLSIEQidpaelspgefaqrvrtSVEQEDARVVVIDSL-NGYLNAMPDERFLILQMH----ELLSYLNNQGVTTLLI 152
|
170 180 190
....*....|....*....|....*....|...
gi 1318755049 215 G--HVTKEGTIAGPRLLEHMVDAVL---YFEGE 242
Cdd:cd19487 153 VaqHGLLGGDMGTPVDISYLADTVVllrYFEAE 185
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
61-209 |
2.68e-08 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 56.04 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 61 ITAIKSQQ---EPRVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLllqiSSQLADKSLS----VLYISGEESTRQT 133
Cdd:PRK09302 241 LTAMRLTQrssNERISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLL----ASKFAEAACRrgerCLLFAFEESRAQL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 134 KLRADRLGV---------------TSDELYVLaETNLLDIANQIEAIKPSFVVIDSIQTVYReeitsaPGSVSQVRECTS 198
Cdd:PRK09302 317 IRNARSWGIdlekmeekgllkiicARPESYGL-EDHLIIIKREIEEFKPSRVAIDPLSALAR------GGSLNEFRQFVI 389
|
170
....*....|.
gi 1318755049 199 ELMKIAKTNGI 209
Cdd:PRK09302 390 RLTDYLKSEEI 400
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
81-249 |
8.99e-08 |
|
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells 3) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC3, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410899 [Multi-domain] Cd Length: 250 Bit Score: 53.06 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 81 RVLGGGIVPGSLVLVGGDPGIGKSTLLLQIS--SQLADK----SLSVLYISGE-----------ESTRQTKLRADRLGVT 143
Cdd:cd19491 3 ELLGGGIPVGGITEIAGESGAGKTQLCLQLAltVQLPRElgglGGGAVYICTEssfpskrlqqlASSLPKRYHLEKAKNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 144 SDELYVlaeTNLLDIANQIEAIK---PSF--------VVIDSIQTVYR-EEITSAPGSVSQVRECT---SELMKIAKTNG 208
Cdd:cd19491 83 LDNIFV---EHVADLETLEHCLNyqlPALlergpirlVVIDSIAALFRsEFDTSRSDLVERAKYLRrlaDHLKRLADKYN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1318755049 209 IPIFIVGHVT---KEGTIAGPRLLEHMVDAVLYFEGERHHTYRI 249
Cdd:cd19491 160 LAVVVVNQVTdrfDSSSDASGLGVLDYLSQFSSFSGGVSGNRKV 203
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
72-212 |
1.73e-07 |
|
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: 52.13 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGgIVPGSLVLVGGDPGIGKSTLLLQISSQLA-DKSLSVLYISGEESTRQ--------------TKLR 136
Cdd:cd00984 2 LPTGFTDLDKLTGG-LQPGDLIIIAARPSMGKTAFALNIAENIAlDEGLPVLFFSLEMSAEQlaerllssesgvslSKLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 137 ADRLgvTSDELYVLAET-----------------NLLDIANQIEAIK-----PSFVVIDSIQTvyreeITSAPGSVS--- 191
Cdd:cd00984 81 TGRL--DDEDWERLTAAmgelselplyiddtpglTVDEIRAKARRLKrehggLGLIVIDYLQL-----IRGSKRAENrqq 153
|
170 180
....*....|....*....|.
gi 1318755049 192 QVRECTSELMKIAKTNGIPIF 212
Cdd:cd00984 154 EVAEISRSLKALAKELNVPVI 174
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
71-217 |
4.44e-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: 51.15 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 71 RVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQLAdKSLS-----VLYISGEESTRQTKLR--ADRLG 141
Cdd:pfam08423 18 QITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLchTLCVTCQLP-LEMGggegkALYIDTEGTFRPERLVaiAERYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 142 VTSDE-----LYVLAET-----NLLDIANQIEAIKP-SFVVIDSIQTVYREEItSAPGSVS----QVRECTSELMKIAKT 206
Cdd:pfam08423 97 LDPEDvldnvAYARAYNsehqmQLLQQAAAMMSESRfALLIVDSATALYRTDF-SGRGELAerqqHLAKFLRTLQRLADE 175
|
170
....*....|.
gi 1318755049 207 NGIPIFIVGHV 217
Cdd:pfam08423 176 FGVAVVITNQV 186
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
93-220 |
4.89e-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: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 93 VLVGGDPGIGKSTLLLQISSQLADKSLSVLYIsgeeSTRQTKLRAdrlgvtsdeLYVLAETNLLDIanqieaikpsfVVI 172
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFI----SFLDTILEA---------IEDLIEEKKLDI-----------III 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1318755049 173 DSIQTVYREEItsaPGSVSQVRECTSELMKIAKTNGIPIFIVGHVTKE 220
Cdd:cd01120 57 DSLSSLARASQ---GDRSSELLEDLAKLLRAARNTGITVIATIHSDKF 101
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
72-184 |
7.82e-07 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 49.97 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELY--- 148
Cdd:PRK06067 7 ISTGNEELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKSYLKQMESVKIDISDFFlwg 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1318755049 149 --VLAETN-------------LLD-IANQIEAIKPSFVVIDS--IQTVYREEIT 184
Cdd:PRK06067 87 ylRIFPLNtegfewnstlankLLElIIEFIKSKREDVIIIDSltIFATYAEEDD 140
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
47-217 |
3.93e-06 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 48.84 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 47 AFQTGNRSVGKPEKITaiksqqepRVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQLADKSLS---- 120
Cdd:PTZ00035 83 GFISATEYLEARKNII--------RITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLchTLCVTCQLPIEQGGgegk 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 121 VLYISGEESTRQTKLR--ADRLGVTSDE-----LYVLAETN------LLDIANQIEAIKPSFVVIDSIQTVYREEItSAP 187
Cdd:PTZ00035 155 VLYIDTEGTFRPERIVqiAERFGLDPEDvldniAYARAYNHehqmqlLSQAAAKMAEERFALLIVDSATALFRVDY-SGR 233
|
170 180 190
....*....|....*....|....*....|....
gi 1318755049 188 GSVS--QVRECT--SELMKIAKTNGIPIFIVGHV 217
Cdd:PTZ00035 234 GELAerQQHLGKflRALQKLADEFNVAVVITNQV 267
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
72-218 |
6.74e-06 |
|
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: 47.35 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQLAdKSLS-----VLYISGEESTRQTKLR--ADRLGV 142
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLshTLCVTAQLP-GSMGggggkVAYIDTEGTFRPDRIRpiAERFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 143 TSDE-----LYVLAET-----NLLDI--ANQIEAIKPSFVVIDSIQTVYREEItSAPGSVSQ----VRECTSELMKIAKT 206
Cdd:cd19514 80 DHDAvldniLYARAYTsehqmELLDYvaAKFHEEAVFRLLIIDSIMALFRVDF-SGRGELAErqqkLAQMLSRLQKISEE 158
|
170
....*....|..
gi 1318755049 207 NGIPIFIVGHVT 218
Cdd:cd19514 159 YNVAVFITNQVT 170
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
90-218 |
7.57e-06 |
|
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: 46.19 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 90 GSLVLVGGDPGIGKSTLLLQ--ISSQLADKSlsVLYISGEEStrqtkLRADRLgVTSDELYVLAETNLLDIANQIEAIKP 167
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQlaANALLLGGG--VVWIDTEGA-----FPPSRL-VQILEASPSSELELAEALSRLLYFRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 168 -----------------------SFVVIDSIQTVYREEITSAPGSVSQVRE-------CTSELMKIAKTNGIPIFIVGHV 217
Cdd:cd01393 73 pdtlahllaldslpeslfpppntSLVVVDSVSALFRKAFPRGGDGDSSSSLrarllsqLARALQKLAAQFNLAVVVTNQV 152
|
.
gi 1318755049 218 T 218
Cdd:cd01393 153 T 153
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
72-212 |
1.89e-05 |
|
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: 45.78 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVL-GGGIVPGSLVLVGGDPGIGKSTLllqiSSQLADKSL----SVLYISGEESTRQTKLRADRLG----- 141
Cdd:cd19484 1 ISTGIPRLDAMLgGGGFFRGSSILVSGATGTGKTLL----AASFADAACrrgeRCLYFAFEESPAQLIRNAKSIGidleq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 142 -VTSDELYVLA--------ETNLLDIANQIEAIKPSFVVIDSIQTVYReeitsaPGSVSQVRECTSELMKIAKTNGIPIF 212
Cdd:cd19484 77 mERKGLLKIICarpelyglEDHLIIIKSEINEFKPSRVIVDPLSALAR------GGSLNEVKEFVIRLIDYLKSQEITGL 150
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
79-137 |
3.14e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.78 E-value: 3.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1318755049 79 FNRVLGGGivpGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRA 137
Cdd:COG3899 303 LERARAGR---GELVLVSGEAGIGKSRLVRELARRARARGGRVLRGKCDQLERGVPYAP 358
|
|
| PRK08533 |
PRK08533 |
flagellar accessory protein FlaH; Reviewed |
78-214 |
6.93e-05 |
|
flagellar accessory protein FlaH; Reviewed
Pssm-ID: 181459 Cd Length: 230 Bit Score: 43.90 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 78 EFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLG-------VTSDELYV- 149
Cdd:PRK08533 12 ELHKRLGGGIPAGSLILIEGDESTGKSILSQRLAYGFLQNGYSVSYVSTQLTTTEFIKQMMSLGydinkklISGKLLYIp 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318755049 150 ---------LAETNLLDIANQIEAIKPSFVVIDSIQTVYREEItsapgSVSQVRECTSELMKIAKTNGIPIFIV 214
Cdd:PRK08533 92 vypllsgnsEKRKFLKKLMNTRRFYEKDVIIIDSLSSLISNDA-----SEVAVNDLMAFFKRISSLNKVIILTA 160
|
|
| PRK05973 |
PRK05973 |
replicative DNA helicase; Provisional |
87-176 |
7.96e-05 |
|
replicative DNA helicase; Provisional
Pssm-ID: 168322 [Multi-domain] Cd Length: 237 Bit Score: 43.87 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 87 IVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYVLAEtnlLDIANQI---- 162
Cdd:PRK05973 61 LKPGDLVLLGARPGHGKTLLGLELAVEAMKSGRTGVFFTLEYTEQDVRDRLRALGADRAQFADLFE---FDTSDAIcady 137
|
90 100
....*....|....*....|
gi 1318755049 163 ------EAIKPSFVVIDSIQ 176
Cdd:PRK05973 138 iiarlaSAPRGTLVVIDYLQ 157
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
38-132 |
1.50e-04 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 43.91 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 38 EITGGRQKQAFQTGNRSVGK-PEKITAIKSQQEP--RVTTDMKEFNRVLGGgIVPGSLVLVGGDPGIGKSTLLLQISSQL 114
Cdd:COG0305 137 EIAEKRSSKGFVSISDILKEaLERIEELYKNGGGitGVPTGFTDLDKLTGG-LQPGDLIILAARPSMGKTAFALNIARNA 215
|
90
....*....|....*....
gi 1318755049 115 ADKS-LSVLYISGEESTRQ 132
Cdd:COG0305 216 AIKEgKPVAIFSLEMSAEQ 234
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
80-205 |
1.63e-04 |
|
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: 42.69 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 80 NRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLA------DKSLSVLYISGE---------ESTRQTKLRADRLGVTS 144
Cdd:cd19493 1 DTALAGGLPLGAITEITGASGSGKTQFALTLASSAAmparkgGLDGGVLYIDTEskfsaerlaEIAEARFPEAFSGFMEE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1318755049 145 DE--------LYVLAETNLLDIANQIEAIKPS-------FVVIDSIQTVYREEITSAPGSVSQVRECTSELMKIAK 205
Cdd:cd19493 81 NEraeemlkrVAVVRVTTLAQLLERLPNLEEHilssgvrLVVIDSIAALVRREFGGSDGEVTERHNALAREASSLK 156
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
89-182 |
2.74e-04 |
|
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: 41.36 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 89 PGSLVLVGgDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLgvtsdelyvlaETNLLDIANQIEAIKPS 168
Cdd:cd00009 19 PKNLLLYG-PPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFG-----------HFLVRLLFELAEKAKPG 86
|
90
....*....|....
gi 1318755049 169 FVVIDSIQTVYREE 182
Cdd:cd00009 87 VLFIDEIDSLSRGA 100
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
348-453 |
2.98e-04 |
|
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: 41.84 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 348 MLQNQDAYIKV-AGGVRLDEPAIDLAIAVSIASSFRDQPTKPEDIFIGEVGLTGEIRRVSRIEQRVQEAAKLGFKRVICP 426
Cdd:pfam05362 90 FFEKKDIHIHVpEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIP 169
|
90 100 110
....*....|....*....|....*....|..
gi 1318755049 427 KNNLGGWT-TPNNI----EIIGVNTVQEALQI 453
Cdd:pfam05362 170 KENEKDLEdIPENVreglEIIPVEHVDEVLKH 201
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
48-218 |
3.83e-04 |
|
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: 42.46 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 48 FQTGNRSVGKPEKITAIksqqeprvTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQLAdKSLS----- 120
Cdd:TIGR02238 62 FITAFEISQKRKKVLKI--------TTGSQALDGILGGGIESMSITEVFGEFRCGKTQLshTLCVTAQLP-REMGggngk 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 121 VLYISGEESTRQTKLR--ADRLGVTSDE-----LYVLAET-----NLLDIANQIEAIKP-SFVVIDSIQTVYREEItSAP 187
Cdd:TIGR02238 133 VAYIDTEGTFRPDRIRaiAERFGVDPDAvldniLYARAYTsehqmELLDYLAAKFSEEPfRLLIVDSIMALFRVDF-SGR 211
|
170 180 190
....*....|....*....|....*....|....*
gi 1318755049 188 GSVSQ----VRECTSELMKIAKTNGIPIFIVGHVT 218
Cdd:TIGR02238 212 GELSErqqkLAQMLSRLNKISEEFNVAVFVTNQVQ 246
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
72-218 |
3.97e-04 |
|
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: 41.92 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLL--LQISSQLADKSL----SVLYISGEESTRQTKLR--ADRLGVT 143
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLPIDQGggegKALYIDTEGTFRPERLLaiAERYGLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 144 SDEL-----YVLA-----ETNLLDIANQIEA-IKPSFVVIDSIQTVYREEItSAPGSVS--QVRECT--SELMKIAKTNG 208
Cdd:cd19513 81 GEDVldnvaYARAyntdhQMQLLIQASAMMAeSRYALLIVDSATALYRTDY-SGRGELSarQMHLAKflRMLQRLADEFG 159
|
170
....*....|
gi 1318755049 209 IPIFIVGHVT 218
Cdd:cd19513 160 VAVVITNQVV 169
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
74-266 |
5.85e-04 |
|
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: 41.20 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 74 TDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQ-ISSQLADKSLSVLYISGEESTRQTKLRADRLG----------- 141
Cdd:cd19485 3 TGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQfLVNGIKEFGEPGVFVTFEESPEDIIKNMASFGwdlpklvaegk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 142 -------VTSDELYVLAETNL----LDIANQIEAIKPSFVVIDSIQTVYreeitSAPGSVSQVRectSELMKIA---KTN 207
Cdd:cd19485 83 llildasPEPSEEEVTGEYDLeallIRIEYAIRKIGAKRVSLDSLEAVF-----SGLSDSAVVR---AELLRLFawlKQK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318755049 208 GIPIFIVGHVTKEGTIAGPRLLEHMVDAVLYF----EGERhhTYRILRGVKNRfGSTNEMGIF 266
Cdd:cd19485 155 GVTAIMTGERGEDGPLTRYGVEEYVSDCVVILrnvlEGER--RRRTLEILKYR-GSSHGKGEY 214
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
90-222 |
6.86e-04 |
|
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: 41.21 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 90 GSLVLVGGDPGIGKSTLLLQISSQLA----------DKSLSVLYISGEESTR--QTKLRA--DRLGVTSDELY------- 148
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVAtgrdwlgerrVKQGRVVYLAAEDPRDglRRRLKAigAHLGDEDAALAenlvien 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1318755049 149 -----VLAETNLLDIANQIEAIKPSFVVIdsIQTVYREEITSAPGSVSQVRECTSELMKIAKTNGIPIFIVGHVTKEGT 222
Cdd:cd01125 81 lrgkpVSIDAEAPELERIIEELEGVRLII--IDTLARVLHGGDENDAADMGAFVAGLDRIARETGAAVLLVHHTGKDAA 157
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
93-238 |
1.25e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 40.00 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 93 VLVGGDPGIGKSTLLLQISsqladkslSVLYISGEESTRqtKLRADRLGVTSDelyVLAETNLLDIANQIEAIKP---SF 169
Cdd:pfam13479 5 ILIYGPSGIGKTTFAKTLP--------KPLFLDTEKGSK--ALDGDRFPDIVI---RDSWQDFLDAIDELTAAELadyKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 170 VVIDSIQTVYR-------------EEITSAPGSV--SQVRECTSELMKIAKTNGIPIFIVGHVTKE-----GTIAGPR-- 227
Cdd:pfam13479 72 IVIDTVDWLERlclayickqngkgSSIEDGGYGKgyGELGEEFRRLLDALQELGKNVIFTAHAKTRkdedpDGEKYTRye 151
|
170 180
....*....|....*....|
gi 1318755049 228 ---------LLEHMVDAVLY 238
Cdd:pfam13479 152 pklgkktanELPGEVDLVLR 171
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
72-218 |
1.62e-03 |
|
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: 40.48 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQLadkSLS-------VLYISGEESTRQTKLR--ADRL 140
Cdd:TIGR02239 78 LTTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLchTLAVTCQL---PIDqgggegkALYIDTEGTFRPERLLaiAERY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 141 GVTSDEL-----YVLA-----ETNLLDIANQIEA-IKPSFVVIDSIQTVYREEItSAPGSVSqVREC-----TSELMKIA 204
Cdd:TIGR02239 155 GLNPEDVldnvaYARAyntdhQLQLLQQAAAMMSeSRFALLIVDSATALYRTDF-SGRGELS-ARQMhlarfLRSLQRLA 232
|
170
....*....|....
gi 1318755049 205 KTNGIPIFIVGHVT 218
Cdd:TIGR02239 233 DEFGVAVVITNQVV 246
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
79-130 |
1.63e-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: 39.02 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1318755049 79 FNRVLGGGivpGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEEST 130
Cdd:pfam13191 16 LDRVRSGR---PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENL 64
|
|
| FlaH |
cd19475 |
flagellar accessory protein FlaH; Flagellar accessory protein FlaH is part of the motor of the ... |
72-214 |
1.92e-03 |
|
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: 39.51 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 72 VTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQISSQLADKSLSVLYISGEESTRQTKLRADRLGVTSDELYV-- 149
Cdd:cd19475 1 ISLGRDDLDKRLGGGIPYPSSIMIEGEESTGKSVLSQRLVYGFLQNDYSGYYISTQQTTKEFLKQMKSLKYDINKKLLrg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 150 ---------------LAETNLLDIANQIEAIKPSFVVIDSIQTvyreeITSAPGSVSQVRECTSELMKIAKTNGIPIFIV 214
Cdd:cd19475 81 kllyipvyplifdnsLKDKFLKKIVNTRAFYEKDFIIFDSLSI-----LIANDASEVQVLDLMKFIKRIVNTGKIILFTI 155
|
|
| circ_KaiC |
TIGR02655 |
circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, ... |
71-180 |
2.24e-03 |
|
circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, part of the kaiABC operon that controls circadian rhythm. It may be universal in Cyanobacteria. Each member has two copies of the KaiC domain (pfam06745), which is also found in other proteins. KaiC performs autophosphorylation and acts as its own transcriptional repressor. [Cellular processes, Other]
Pssm-ID: 131703 [Multi-domain] Cd Length: 484 Bit Score: 40.32 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 71 RVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTLLLQ-ISSQLADKSLSVLYiSGEESTRQTKLRADRLGVTSDE--- 146
Cdd:TIGR02655 244 RVSSGVVRLDEMCGGGFFKDSIILATGATGTGKTLLVSKfLENACANKERAILF-AYEESRAQLLRNAYSWGIDFEEmeq 322
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1318755049 147 ---LYVLA--------ETNLLDIANQIEAIKPSFVVIDSIQTVYR 180
Cdd:TIGR02655 323 qglLKIICaypesaglEDHLQIIKSEIADFKPARIAIDSLSALAR 367
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
92-176 |
3.15e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 37.57 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 92 LVLVGgdP-GIGKSTLLLQISSQLaDKSLSVLYISGEEstrqtklradrlgvtsDELYVLAETNLLDIANQIEAIKPSFV 170
Cdd:pfam13173 5 LVITG--PrQVGKTTLLLQLIKEL-LPPENILYINLDD----------------PRLLKLADFELLELFLELLYPGKTYL 65
|
....*.
gi 1318755049 171 VIDSIQ 176
Cdd:pfam13173 66 FLDEIQ 71
|
|
| radA |
PRK04301 |
DNA repair and recombination protein RadA; Validated |
71-182 |
6.36e-03 |
|
DNA repair and recombination protein RadA; Validated
Pssm-ID: 235273 [Multi-domain] Cd Length: 317 Bit Score: 38.71 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 71 RVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKStlllQISSQLA----------DKSLSVLYISGEESTRQTKLR--AD 138
Cdd:PRK04301 83 KITTGSKELDELLGGGIETQSITEFYGEFGSGKT----QICHQLAvnvqlpeekgGLEGKAVYIDTEGTFRPERIEqmAE 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1318755049 139 RLGVTSDE----LYV-----------LAEtNLLDIANQIEAIKpsFVVIDSIQTVYREE 182
Cdd:PRK04301 159 ALGLDPDEvldnIHVaraynsdhqmlLAE-KAEELIKEGENIK--LVIVDSLTAHFRAE 214
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
92-174 |
9.09e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 37.09 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 92 LVLVGGDPGIGKSTLllqiSSQLADKsLSVLYISGEESTRQTklrADRLGVTSDELYVLAETN-----LLDiANQIE-AI 165
Cdd:PRK04182 2 IITISGPPGSGKTTV----ARLLAEK-LGLKHVSAGEIFREL---AKERGMSLEEFNKYAEEDpeidkEID-RRQLEiAE 72
|
....*....
gi 1318755049 166 KPSFVVIDS 174
Cdd:PRK04182 73 KEDNVVLEG 81
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
67-184 |
9.45e-03 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 38.17 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318755049 67 QQEPRVTTDMKEFNRVLGGGIVPGSLVLVGGDPGIGKSTL--LLQISSQLADKSL----SVLYISGEESTRQTKLR--AD 138
Cdd:PLN03186 100 QEIIQITTGSRELDKILEGGIETGSITEIYGEFRTGKTQLchTLCVTCQLPLDQGggegKAMYIDTEGTFRPQRLIqiAE 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1318755049 139 RLGVTSDEL-----YVLA-----ETNLLDIANQIEA-IKPSFVVIDSIQTVYREEIT 184
Cdd:PLN03186 180 RFGLNGADVlenvaYARAyntdhQSELLLEAASMMAeTRFALMIVDSATALYRTEFS 236
|
|
| |
