|
Name |
Accession |
Description |
Interval |
E-value |
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
10-464 |
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: 825.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 10 MAKKsKVQFVCQNCGYVSPKFLGRCPNCGKWNTMVEEIEQDTTDRRTRTSLTGEKAKPTKIADVVPKKEPRIKTKLEELN 89
Cdd:COG1066 1 MAKT-KTVYVCQECGYESPKWLGRCPECGAWNTLVEEVVAKAKKGRAASGAAGRASKPVPLSEVEAEEEPRISTGIGELD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 90 RVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGSINTEFYLYAETDMNEISR 169
Cdd:COG1066 80 RVLGGGLVPGSVVLIGGEPGIGKSTLLLQVAARLAKKGGKVLYVSGEESASQIKLRAERLGLLSDNLYLLAETDLEAILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 170 AIEHISPDYVIIDSIQTMTQPDITSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTKEGSIAGPRMLEHMVDTVLYFE 249
Cdd:COG1066 160 TIEELKPDLLVIDSIQTMYSEELESAPGSVSQVRECAAELIRLAKETGIAVFLVGHVTKEGSIAGPRVLEHMVDTVLYFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 250 GEQHHSFRILRAVKNRFGSTNEIGIFEMHEHGLEEVANPSQIFLEERLDGATGSAIVVAMEGTRPILVEIQALVTPTMFG 329
Cdd:COG1066 240 GDRHSRYRILRAVKNRFGSTNEIGVFEMTEKGLREVSNPSELFLSERDEPVPGSAVTVTMEGTRPLLVEVQALVSPSSFG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 330 NAKRTTTGLDFNRVSLIMAVLEKRAGLLLQNQDAYLKAAGGVKLNEPAIDLAIAVSIASSYKEKGTQPTECFIGEIGLTG 409
Cdd:COG1066 320 NPRRTAVGLDSNRLAMLLAVLEKRAGLPLGDQDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGEVGLTG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1821249106 410 EIRRVSHIEQRVKEVQKLGFTKVYLPKNNLGNWeAPKGIEIVGVATLAETLKRVF 464
Cdd:COG1066 400 EIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKL-KPKGIEIIGVSTLEEALEALF 453
|
|
| sms |
TIGR00416 |
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved ... |
10-460 |
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: 624.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 10 MAKKsKVQFVCQNCGYVSPKFLGRCPNCGKWNTMVEEIEQDTTDRRTRTSLTGEK-----AKPTKIADVVPKKEPRIKTK 84
Cdd:TIGR00416 1 MAKA-KSKFVCQHCGADSPKWQGKCPACHAWNTITEERLHRSLGAQKNRRNSGKAgipqaQKSQTISAIELEEVPRFSSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 85 LEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGSINTEFYLYAETDM 164
Cdd:TIGR00416 80 FGELDRVLGGGIVPGSLILIGGDPGIGKSTLLLQVACQLAKNQMKVLYVSGEESLQQIKMRAIRLGLPEPNLYVLSETNW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 165 NEISRAIEHISPDYVIIDSIQTMTQPDITSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTKEGSIAGPRMLEHMVDT 244
Cdd:TIGR00416 160 EQICANIEEENPQACVIDSIQTLYSPDISSAPGSVSQVRECTAELMRLAKTRGIAIFIVGHVTKEGSIAGPKVLEHMVDT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 245 VLYFEGEQHHSFRILRAVKNRFGSTNEIGIFEMHEHGLEEVANPSQIFLEERLDGATGSAIVVAMEGTRPILVEIQALVT 324
Cdd:TIGR00416 240 VLYFEGDRDSRFRILRSVKNRFGATNEIGIFEMTEQGLREVLNPSAIFLSRREEPMSGSSITVTWEGTRPLLVEIQALVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 325 PTMFGNAKRTTTGLDFNRVSLIMAVLEKRAGLLLQNQDAYLKAAGGVKLNEPAIDLAIAVSIASSYKEKGTQPTECFIGE 404
Cdd:TIGR00416 320 PTSFANPRRVATGLDQNRLALLLAVLEKRLGLPLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFLGE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821249106 405 IGLTGEIRRVSHIEQRVKEVQKLGFTKVYLPKNNLGNwEAPKGIEIVGVATLAETL 460
Cdd:TIGR00416 400 VGLAGEIRPVPSLEERLKEAAKLGFKRAIVPKANSPK-TAPEGIKVIGVKKVGDAL 454
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
18-285 |
1.18e-172 |
|
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: 485.11 E-value: 1.18e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 18 FVCQNCGYVSPKFLGRCPNCGKWNTMVEEIEQDTTDRRTRTSLTGEKAKPTKIADVVPKKEPRIKTKLEELNRVLGGGVV 97
Cdd:cd01121 1 YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSSASRRASASPSPSKPLPLSDVEAEEEERISTGIGELDRVLGGGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 98 PGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGSINTEFYLYAETDMNEISRAIEHISPD 177
Cdd:cd01121 81 PGSVVLIGGDPGIGKSTLLLQVAARLAQRGGKVLYVSGEESLSQIKLRAERLGLGSDNLYLLAETNLEAILAEIEELKPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 178 YVIIDSIQTMTQPDITSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTKEGSIAGPRMLEHMVDTVLYFEGEQHHSFR 257
Cdd:cd01121 161 LVVIDSIQTVYSPELTSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVTKDGAIAGPKVLEHMVDTVLYFEGDRGSSYR 240
|
250 260
....*....|....*....|....*...
gi 1821249106 258 ILRAVKNRFGSTNEIGIFEMHEHGLEEV 285
Cdd:cd01121 241 ILRSVKNRFGPTNEIGVFEMTENGLREV 268
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
80-283 |
7.22e-29 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 113.09 E-value: 7.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGsIN------ 153
Cdd:COG0467 1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSFEESPEQLLRRAESLG-LDleeyie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 154 -----------TEFYLYAETDMNEISRAIEHISPDYVIIDSIQTmtqpdITSVAGSVSQVRETTAELLKTAKTNGIAIFI 222
Cdd:COG0467 80 sgllriidlspEELGLDLEELLARLREAVEEFGAKRVVIDSLSG-----LLLALPDPERLREFLHRLLRYLKKRGVTTLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821249106 223 VGHVTKEGSIAGPRMLEHMVDTVLYFEGEQHHSF--RILRAVKNRfGS--TNEIGIFEMHEHGLE 283
Cdd:COG0467 155 TSETGGLEDEATEGGLSYLADGVILLRYVELGGElrRALSVLKMR-GSahDRTIREFEITDGGIE 218
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
81-283 |
3.00e-19 |
|
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: 86.16 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGS--------- 151
Cdd:cd01124 1 VKTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAGAKNGEPGLFFTFEESPERLLRNAKSFGWdfdemedeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 152 ------INTEFYLYAETD--MNEISRAIEHISPDYVIIDSIQT--MTQPDITSVagsVSQVRETTAELlktAKTNGIAIF 221
Cdd:cd01124 81 kliivdAPPTEAGRFSLDelLSRILSIIKSFKAKRVVIDSLSGlrRAKEDQMRA---RRIVIALLNEL---RAAGVTTIF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821249106 222 IVG-HVTKEGSIAGPRMLEHMVDTV--LYFEGEQHHSFRILRAVKNRFGStNEIGIFEMH--EHGLE 283
Cdd:cd01124 155 TSEmRSFLSSESAGGGDVSFIVDGVilLRYVEIEGELRRTIRVLKMRGTG-HDTGTHPFEitDKGIV 220
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
95-314 |
1.79e-18 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 85.72 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 95 GVVP-GSMVLIGGDPGIGKSTLLLQVSQQLAA---------IGGKVLYVSGEESAEQIKLRAERLGS------------- 151
Cdd:COG3598 8 GLLPeGGVTLLAGPPGTGKSFLALQLAAAVAAggpwlgrrvPPGKVLYLAAEDDRGELRRRLKALGAdlglpfadldgrl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 152 --INTEFYLYAETDMNEISRAIEHISPDYVIIDSIQTMTQPDitsvAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTKE 229
Cdd:COG3598 88 rlLSLAGDLDDTDDLEALERAIEEEGPDLVVIDPLARVFGGD----ENDAEEMRAFLNPLDRLAERTGAAVLLVHHTGKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 230 G-------SIAGPRMLEHMVDTVLYFEGEQHHSFRILRAVKNRFGSTNEIgIFEMHEHGLEEVANPSQIFLEERLDGATG 302
Cdd:COG3598 164 GagkdsgdRARGSSALRGAARSVLVLSREKGEDLRVLTRAKSNYGPEIAL-RWDNGGRLALEEVAALTAGAGEVELKELV 242
|
250
....*....|..
gi 1821249106 303 SAIVVAMEGTRP 314
Cdd:COG3598 243 GGVARTGTDSEL 254
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
80-231 |
2.01e-16 |
|
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: 77.42 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVS-----------QQLAAIGGKVLYVSGEESAEQIKLRAER 148
Cdd:pfam13481 14 GLAAPPPPRRWLIKGLLPAGGLGLLAGAPGTGKTTLALDLAaavatgkpwlgGPRVPEQGKVLYVSAEGPADELRRRLRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 149 LG----SINTEFYLYAET----------------DMNEISRAIEHI-SPDYVIIDSIQTMTQPDITsvagSVSQVRETTA 207
Cdd:pfam13481 94 AGadldLPARLLFLSLVEslplffldrggplldaDVDALEAALEEVeDPDLVVIDPLARALGGDEN----SNSDVGRLVK 169
|
170 180
....*....|....*....|....
gi 1821249106 208 ELLKTAKTNGIAIFIVGHVTKEGS 231
Cdd:pfam13481 170 ALDRLARRTGATVLLVHHVGKDGA 193
|
|
| Rubredoxin_2 |
pfam18073 |
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ... |
18-45 |
5.64e-13 |
|
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: 62.56 E-value: 5.64e-13
10 20
....*....|....*....|....*...
gi 1821249106 18 FVCQNCGYVSPKFLGRCPNCGKWNTMVE 45
Cdd:pfam18073 1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
81-184 |
1.28e-12 |
|
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: 66.99 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLG-SIN------ 153
Cdd:cd19488 1 ISTGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQFLLEGAANGETGLYITLSETEQELRAVALSHGwSLDgihife 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1821249106 154 --------------TEFYlYAETDMNEISRAI----EHISPDYVIIDSI 184
Cdd:cd19488 81 lspsesaldaaqqyTILH-PSELELSETTRLIfervERLKPSRVVIDSL 128
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
98-249 |
2.61e-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: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 98 PGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGSINTEFYLYAETDMNEISRAIEHISPD 177
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821249106 178 YVIIDSIQTMTQPDITSVAgsvsQVRETTAELLKTAKTNGIAIFIVGHVTKegsIAGPRMLEHMVDTVLYFE 249
Cdd:smart00382 81 VLILDEITSLLDAEQEALL----LLLEELRLLLLLKSEKNLTVILTTNDEK---DLGPALLRRRFDRRIVLL 145
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
81-278 |
2.95e-12 |
|
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: 66.12 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQ-VSQQLAAIGGKVLYVSGEESAEQIKLRAERLGsINTE---- 155
Cdd:pfam06745 1 VKTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQfLYNGALKYGEPGVFVTLEEPPEDLRENARSFG-WDLEklee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 156 ----FYLYAETDMNE----------------ISRAIEHISPDYVIIDSIQTMTQPDITSVAgsvsqvRETTAELLKTAKT 215
Cdd:pfam06745 80 egklAIIDASTSGIGiaevedrfdleelierLREAIREIGAKRVVIDSITTLFYLLKPAVA------REILRRLKRVLKG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821249106 216 NGI-AIFIVGHVTKEGSIAGPRMLEHMVDTV--LYFEGEQHHSFRILRAVKNRfGSTNEIGIFEMH 278
Cdd:pfam06745 154 LGVtAIFTSEKPSGEGGIGGYGVEEFIVDGVirLDLKEIEEERVRTIEIVKMR-GTPHSMKRYPFE 218
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
81-283 |
6.88e-12 |
|
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: 64.63 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGsINTEFYL-- 158
Cdd:cd19487 1 VSSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQFAKAAAARGERSVLFSFDESIGTLFERSEALG-IDLRAMVek 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 159 ----YAETDMNEIS---------RAIEHISPDYVIIDSIqtmtqpditsvAGSVSQVRETTA------ELLKTAKTNGIA 219
Cdd:cd19487 80 gllsIEQIDPAELSpgefaqrvrTSVEQEDARVVVIDSL-----------NGYLNAMPDERFlilqmhELLSYLNNQGVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821249106 220 IFIVG--HVTKEGSIAGPRMLEHMVDTVL---YFEgeqhHSFRILRA---VKNRFGsTNEIGI--FEMHEHGLE 283
Cdd:cd19487 149 TLLIVaqHGLLGGDMGTPVDISYLADTVVllrYFE----AEGEVRKAisvLKKRTG-DHERTIreFRITRSGLK 217
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
102-229 |
4.39e-11 |
|
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: 59.82 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 102 VLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSgeesaeqiklraerlgsintefylYAETDMNEISRAIEHISPDYVII 181
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFIS------------------------FLDTILEAIEDLIEEKKLDIIII 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1821249106 182 DSIQTMTQPditSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTKE 229
Cdd:cd01120 57 DSLSSLARA---SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKF 101
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
85-285 |
5.68e-11 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 62.19 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 85 LEELnrvLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEE-SAEQIK-LRAERLGSINTEFYLYAET 162
Cdd:PRK09361 12 LDEL---LGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKNGKKVIYIDTEGlSPERFKqIAGEDFEELLSNIIIFEPS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 163 DMNEISRAIEHISP------DYVIIDSIQTMTQPDITSVAGSVSQVRETTAE---LLKTAKTNGIAIFIVGHV---TKEG 230
Cdd:PRK09361 89 SFEEQSEAIRKAEKlakenvGLIVLDSATSLYRLELEDEEDNSKLNRELGRQlthLLKLARKHDLAVVITNQVysdIDSD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821249106 231 SI--AGPRMLEHMVDTVLYFEGEQhHSFRILRAVKNRFGSTNEIGIFEMHEHGLEEV 285
Cdd:PRK09361 169 GLrpLGGHTLEHWSKTILRLEKFR-NGKRRATLEKHRSRPEGESAEFRITDRGIEII 224
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
81-196 |
5.69e-10 |
|
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: 59.83 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGgVVPGSMVLIGGDPGIGKSTLLLQVSQQLAA-IGGKVLYVSGEESAEQIklrAERL----GSINTE 155
Cdd:cd00984 2 LPTGFTDLDKLTGG-LQPGDLIIIAARPSMGKTAFALNIAENIALdEGLPVLFFSLEMSAEQL---AERLlsseSGVSLS 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1821249106 156 F----YLYAEtDMNEISRAIEHISPDYVIIDSIQTMTQPDITSVA 196
Cdd:cd00984 78 KlrtgRLDDE-DWERLTAAMGELSELPLYIDDTPGLTVDEIRAKA 121
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
80-320 |
1.86e-09 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 59.51 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIkLRAERlgSINTEFYLY 159
Cdd:PRK09302 254 RISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLASKFAEAACRRGERCLLFAFEESRAQL-IRNAR--SWGIDLEKM 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 160 A-----------------ETDMNEISRAIEHISPDYVIIDSIQTMTQpditsvAGSVSQVRETTAELLKTAKTNGIAIF- 221
Cdd:PRK09302 331 EekgllkiicarpesyglEDHLIIIKREIEEFKPSRVAIDPLSALAR------GGSLNEFRQFVIRLTDYLKSEEITGLf 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 222 -------IVGHVTKEGSIAGprmlehMVDTVL---YFE--GEQHhsfRILRAVKNRfGS--TNEIGIFEMHEHGLEEVA- 286
Cdd:PRK09302 405 tnltpdfMGSHSITESHISS------LTDTWIllqYVEinGEMN---RALYVLKMR-GSwhSNQIREFVITDKGIHIKDp 474
|
250 260 270
....*....|....*....|....*....|....*.
gi 1821249106 287 --NPSQIFleerldgaTGSAIVVAMEGTRPILVEIQ 320
Cdd:PRK09302 475 frGFEGIL--------SGSPRRAQEAEERRELSRRF 502
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
88-268 |
2.72e-09 |
|
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: 56.94 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 88 LNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEE-SAEQIKLRA-ERLGSINTEFYLYAETDMN 165
Cdd:cd01394 8 LDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDTEGlSPERFQQIAgERFESIASNIIVFEPYSFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 166 EISRAIEHI-------SPDYVIIDSIQTMTQPDITSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTkegSIAGPRML 238
Cdd:cd01394 88 EQGVAIQEAekllksdKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLSIARKYDIPVVITNQVY---SDIDDDRL 164
|
170 180 190
....*....|....*....|....*....|
gi 1821249106 239 EHMVDTVLyfegeQHHSFRILRAVKNRFGS 268
Cdd:cd01394 165 KPVGGTLL-----EHWSKAIIRLEKSPPGL 189
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
80-184 |
1.50e-08 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 55.22 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESA----EQIK---------LRA 146
Cdd:COG2874 2 IISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQFAYGALENGLSVTYISTELTTkefiKQMKslsydisdyLLR 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1821249106 147 ERLG--SINTEFYLYAETDMNE-ISRAIEHISP-----DYVIIDSI 184
Cdd:COG2874 82 GRLLflPVHPLGFEWNSKQRKDlLKRLMKYIASnlweaDVIIIDSL 127
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
376-458 |
2.69e-08 |
|
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: 55.82 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 376 PAIDLAIAVSI-ASSYKEKGTQPTEC-FIGEIGLTGEIRRVSHIEQRVKEVQKLGFTKVYLPKNNLgnWEA--PKGIEIV 451
Cdd:COG0606 78 SRFDLPIALGIlAASGQIPAEALEDYvFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANA--AEAalVPGIEVY 155
|
....*..
gi 1821249106 452 GVATLAE 458
Cdd:COG0606 156 GASSLLE 162
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
376-438 |
1.34e-07 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 50.14 E-value: 1.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821249106 376 PAIDLAIAVSIASSYKEKGTQPTECFIGEIGLTGEIRRVSHIEQRVKEVQKLGFTKVYLPKNN 438
Cdd:pfam13541 59 SSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
81-283 |
1.56e-07 |
|
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: 51.94 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVL-GGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIkLRaeRLGSINTEFYLY 159
Cdd:cd19484 1 ISTGIPRLDAMLgGGGFFRGSSILVSGATGTGKTLLAASFADAACRRGERCLYFAFEESPAQL-IR--NAKSIGIDLEQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 160 A-----------------ETDMNEISRAIEHISPDYVIIDSIQTMTQPditsvaGSVSQVRETTAELLKTAKTNGIAIF- 221
Cdd:cd19484 78 ErkgllkiicarpelyglEDHLIIIKSEINEFKPSRVIVDPLSALARG------GSLNEVKEFVIRLIDYLKSQEITGLf 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821249106 222 ---IVGHVTKEGSIAGprmLEHMVDTVL---YFE--GEQHhsfRILRAVKNRfGS--TNEIGIFEMHEHGLE 283
Cdd:cd19484 152 tnlTPDGGSLEITEAG---ISSLTDTWIllrYVEinGERN---RGLYVLKMR-GMahSNQIREFSISDKGID 216
|
|
| RecA-like_Gp4D_helicase |
cd19483 |
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the ... |
102-279 |
1.31e-06 |
|
RecA-like domain of Escherichia coli bacteriophage T7 Gp4D helicase; This family includes the RecA-like domain of the Gp4D fragment of the Gene4 helicase-primase (Gp4) from bacteriophage T7. Gp4D (residues 241-566) is the minimal fragment of the Gp4 that forms hexameric rings, it contains the helicase domain and the linker connecting the helicase and primase domains. Helicases are ring-shaped oligomeric enzymes that unwind DNA at the replication fork; they couple NTP hydrolysis to the unwinding of nucleic acid duplexes into their component strands. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410891 [Multi-domain] Cd Length: 231 Bit Score: 49.49 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 102 VLIGGDPGIGKSTLLLQVSQQLAAI-GGKVLYVSGEESAEQ-------IKLRAERLGSINTE------------------ 155
Cdd:cd19483 1 VTIGAGSGIGKSTIVRELAYHLITEhGEKVGIISLEESVEEtakglagKHLGKPEPLELPRDditeeeeddafdnelgsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 156 -FYLY---AETDMNEISRAIEHISP----DYVIIDSIQTMTQPDitSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVT 227
Cdd:cd19483 81 rFFLYdhfGSLDWDNLKEKIRYMVKvlgcKVIVLDHLTILVSGL--DSSDERKELDEIMTELAALVKELGVTIILVSHLR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821249106 228 K--------------EGSIAGPRMLEHMVDTVLYFEGEQHHS------FRILRAVKNR-FGSTNEIGIFEMHE 279
Cdd:cd19483 159 RpgggkgheeggevsESDLRGSSAIAQLSDYVIGLERNKQADdpvernTTRVRVLKNRfTGETGIAGTLYYDE 231
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
85-146 |
3.16e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.86 E-value: 3.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821249106 85 LEELNRVLGGGvvpGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRA 146
Cdd:COG3899 300 LAALERARAGR---GELVLVSGEAGIGKSRLVRELARRARARGGRVLRGKCDQLERGVPYAP 358
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
81-225 |
4.44e-06 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 47.66 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLG---------- 150
Cdd:PRK06067 7 ISTGNEELDRKLGGGIPFPSLILIEGDHGTGKSVLSQQFVYGALKQGKKVYVITTENTSKSYLKQMESVKidisdfflwg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 151 -----SINTEFYLYAETDMNEI-SRAIEHISP---DYVIIDSIQTMTqpditsvagsVSQVRETTAELLKTAKT---NGI 218
Cdd:PRK06067 87 ylrifPLNTEGFEWNSTLANKLlELIIEFIKSkreDVIIIDSLTIFA----------TYAEEDDILNFLTEAKNlvdLGK 156
|
....*..
gi 1821249106 219 AIFIVGH 225
Cdd:PRK06067 157 TILITLH 163
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
81-223 |
6.44e-06 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 48.15 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGgVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGK-VLYVSGEESAEQIKLR---------AERL- 149
Cdd:COG0305 174 VPTGFTDLDKLTGG-LQPGDLIILAARPSMGKTAFALNIARNAAIKEGKpVAIFSLEMSAEQLVMRllssearidSSKLr 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821249106 150 -GSINtefylyaETDMNEISRAIEHIS--PDYvIIDSiqtmtqPDITsvagsVSQVReTTAELLKtaKTNGIAIFIV 223
Cdd:COG0305 253 tGKLS-------DEDWERLSSAAGELSeaPIY-IDDT------PGLT-----IAEIR-AKARRLK--REHGLGLIVI 307
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
99-238 |
8.68e-06 |
|
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: 46.99 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 99 GSMVLIGGDPGIGKSTLLLQVSQQLAAI----------GGKVLYVSGEESAEQIKLRAERLG-SINTE----------FY 157
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLAVAVATGrdwlgerrvkQGRVVYLAAEDPRDGLRRRLKAIGaHLGDEdaalaenlviEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 158 LYAETDMN-----EISRAI-EHISPDYVIIDsiqTMTQPDITSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVTKEGS 231
Cdd:cd01125 81 LRGKPVSIdaeapELERIIeELEGVRLIIID---TLARVLHGGDENDAADMGAFVAGLDRIARETGAAVLLVHHTGKDAA 157
|
....*..
gi 1821249106 232 IAGPRML 238
Cdd:cd01125 158 GDSQQAA 164
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
81-275 |
1.30e-05 |
|
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: 46.21 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQ-VSQQLAAIGGKVLYVSGEESAEQI------------KLRAE 147
Cdd:cd19485 1 LPTGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQfLVNGIKEFGEPGVFVTFEESPEDIiknmasfgwdlpKLVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 148 RLGSIN------TEFYLYAETDMN----EISRAIEHISPDYVIIDSIQTmtqpdITSVAGSVSQVRETTAELLKTAKTNG 217
Cdd:cd19485 81 GKLLILdaspepSEEEVTGEYDLEalliRIEYAIRKIGAKRVSLDSLEA-----VFSGLSDSAVVRAELLRLFAWLKQKG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 218 IAIFIVGHVTKEGSIAGPRMLEHMVDTV--LYFEGEQHHSFRILRAVKNRfGSTNEIGIF 275
Cdd:cd19485 156 VTAIMTGERGEDGPLTRYGVEEYVSDCVviLRNVLEGERRRRTLEILKYR-GSSHGKGEY 214
|
|
| PRK05973 |
PRK05973 |
replicative DNA helicase; Provisional |
82-203 |
2.49e-05 |
|
replicative DNA helicase; Provisional
Pssm-ID: 168322 [Multi-domain] Cd Length: 237 Bit Score: 45.41 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 82 KTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGSINTEFYLYAE 161
Cdd:PRK05973 47 KAAATTPAEELFSQLKPGDLVLLGARPGHGKTLLGLELAVEAMKSGRTGVFFTLEYTEQDVRDRLRALGADRAQFADLFE 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1821249106 162 TDM-NEISRA--IEHISP----DYVIIDSIQTMTQ----PDITsvagsvSQVR 203
Cdd:PRK05973 127 FDTsDAICADyiIARLASaprgTLVVIDYLQLLDQrrekPDLS------VQVR 173
|
|
| RecA-like |
cd01393 |
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ... |
99-227 |
5.01e-05 |
|
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: 43.88 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 99 GSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGE---------ESAEQIKLRAERLGSINTEFYLYAETDMNEISR 169
Cdd:cd01393 1 GKITEIYGPPGSGKTQLALQLAANALLLGGGVVWIDTEgafppsrlvQILEASPSSELELAEALSRLLYFRPPDTLAHLL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821249106 170 AIEHISP--------DYVIIDSIQTMTQPDITSVAGSVSQVRETTA-------ELLKTAKTNGIAIFIVGHVT 227
Cdd:cd01393 81 ALDSLPEslfpppntSLVVVDSVSALFRKAFPRGGDGDSSSSLRARllsqlarALQKLAAQFNLAVVVTNQVT 153
|
|
| PRK08506 |
PRK08506 |
replicative DNA helicase; Provisional |
81-175 |
1.01e-04 |
|
replicative DNA helicase; Provisional
Pssm-ID: 236278 [Multi-domain] Cd Length: 472 Bit Score: 44.62 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRvLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRA-ERLGSINTEFYLY 159
Cdd:PRK08506 175 LDTGFVELNK-MTKGFNKGDLIIIAARPSMGKTTLCLNMALKALNQDKGVAFFSLEMPAEQLMLRMlSAKTSIPLQNLRT 253
|
90
....*....|....*....
gi 1821249106 160 AETDMNEISR---AIEHIS 175
Cdd:PRK08506 254 GDLDDDEWERlsdACDELS 272
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
81-283 |
1.04e-04 |
|
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: 43.67 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTL--LLQVSQQL----AAIGGKVLYVSGEESAEQIKLR--AERLG-- 150
Cdd:cd01123 1 ITTGSKELDKLLGGGIETGSITEMFGEFRTGKTQLchTLAVTCQLpidrGGGEGKAIYIDTEGTFRPERLRaiAQRFGld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 151 ------------SINTEFYL----YAETDMNEISRAIehispdyVIIDSIQTMTQPDItSVAGSVSQVRETTAE----LL 210
Cdd:cd01123 81 pddvldnvayarAFNSDHQTqlldQAAAMMVESRFKL-------LIVDSATALYRTDY-SGRGELSARQMHLAKflrmLQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 211 KTAKTNGIAIFIVGHVTKE--GSIA---------GPRMLEHMVDTVLYF---EGEQhhsfRILRAVKNRFGSTNEiGIFE 276
Cdd:cd01123 153 RLADEFGVAVVVTNQVVAQvdGAMMfaadpkkpiGGNILAHASTTRLYLrkgRGET----RICKIYDSPCLPEAE-AVFA 227
|
....*..
gi 1821249106 277 MHEHGLE 283
Cdd:cd01123 228 ITADGVG 234
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
80-226 |
1.05e-04 |
|
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: 43.83 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTL--LLQVSQQL----AAIGGKVLYVSGEESaeqikLRAERLGSIN 153
Cdd:pfam08423 18 QITTGSKELDKLLGGGIETGSITEIFGEFRTGKTQLchTLCVTCQLplemGGGEGKALYIDTEGT-----FRPERLVAIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 154 TEFYLYAETDMNEIS--RA--IEH------------ISPDY--VIIDSIQTMTQPDItSVAGSVSQVRETTAELLKT--- 212
Cdd:pfam08423 93 ERYGLDPEDVLDNVAyaRAynSEHqmqllqqaaammSESRFalLIVDSATALYRTDF-SGRGELAERQQHLAKFLRTlqr 171
|
170
....*....|....*
gi 1821249106 213 -AKTNGIAIFIVGHV 226
Cdd:pfam08423 172 lADEFGVAVVITNQV 186
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
102-223 |
1.14e-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: 42.52 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 102 VLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLGSINTEFylyaetdmneiSRAIEHISPDYVII 181
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLL-----------FELAEKAKPGVLFI 90
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1821249106 182 DSIQTMTqpditsvAGSVSQVRETTAELLKTAKTNGIAIFIV 223
Cdd:cd00009 91 DEIDSLS-------RGAQNALLRVLETLNDLRIDRENVRVIG 125
|
|
| PRK08533 |
PRK08533 |
flagellar accessory protein FlaH; Reviewed |
80-223 |
1.25e-04 |
|
flagellar accessory protein FlaH; Reviewed
Pssm-ID: 181459 Cd Length: 230 Bit Score: 43.52 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTL-------LLQ-------VSQQLAA------------------IG 127
Cdd:PRK08533 5 KIELSRDELHKRLGGGIPAGSLILIEGDESTGKSILsqrlaygFLQngysvsyVSTQLTTtefikqmmslgydinkklIS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 128 GKVLYVSGEESAEQIKLRAERLGSINTEFYLYaetdmneisraiehiSPDYVIIDSIQTMTQPDItsvagSVSQVRETTA 207
Cdd:PRK08533 85 GKLLYIPVYPLLSGNSEKRKFLKKLMNTRRFY---------------EKDVIIIDSLSSLISNDA-----SEVAVNDLMA 144
|
170
....*....|....*.
gi 1821249106 208 ELLKTAKTNGIAIFIV 223
Cdd:PRK08533 145 FFKRISSLNKVIILTA 160
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
88-227 |
1.90e-04 |
|
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: 43.05 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 88 LNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVS------QQLAAIGGKVLYVSGEES----------AEQIKLRAERLGS 151
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQLAltvqlpRELGGLGGGAVYICTESSfpskrlqqlaSSLPKRYHLEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 152 INTE--FYLYAeTDMNEISRAIEHISPDY--------VIIDSI----QTMTQPDITSVAGSVSQVRETTAELLKTAKTNG 217
Cdd:cd19491 81 NFLDniFVEHV-ADLETLEHCLNYQLPALlergpirlVVIDSIaalfRSEFDTSRSDLVERAKYLRRLADHLKRLADKYN 159
|
170
....*....|
gi 1821249106 218 IAIFIVGHVT 227
Cdd:cd19491 160 LAVVVVNQVT 169
|
|
| PRK04328 |
PRK04328 |
hypothetical protein; Provisional |
79-255 |
2.66e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235281 Cd Length: 249 Bit Score: 42.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 79 PRIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQIKLRAERLG-------- 150
Cdd:PRK04328 3 KRVKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFSQQFLWNGLQMGEPGVYVALEEHPVQVRRNMRQFGwdvrkyee 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 151 ----------------SINTEFYLYAE-TDMNEIS----RAIEHISPDYVIIDSIQT--MTQPditSVAgsvsqvRETTA 207
Cdd:PRK04328 83 egkfaivdaftggigsAAKREKYVVKDpDDVRELIdvlrQAIKDIGAKRVVIDSVSTlyLTKP---AMA------RSIVM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821249106 208 ELLKTAKTNGIAIFIVGHVT-KEGSIAGPRmLEHMVDTVLY-----FEGEQHHS 255
Cdd:PRK04328 154 QLKRVLSGLGCTAIFVSQVSvGERGFGGPG-VEHAVDGIIRldldeIDGELKRS 206
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
78-155 |
3.40e-04 |
|
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: 41.34 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 78 EPRIKTKLEELNRVLGGGvvpGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAE-----QIKLRAERLGSI 152
Cdd:pfam13191 6 EEELEQLLDALDRVRSGR---PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPyspllEALTREGLLRQL 82
|
...
gi 1821249106 153 NTE 155
Cdd:pfam13191 83 LDE 85
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
80-226 |
1.10e-03 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 41.14 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 80 RIKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTL------LLQVSQQLAAIGGKVLYVSGEESaeqikLRAERLGSIN 153
Cdd:PTZ00035 99 RITTGSTQLDKLLGGGIETGSITELFGEFRTGKTQLchtlcvTCQLPIEQGGGEGKVLYIDTEGT-----FRPERIVQIA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 154 TEFYLYAETDMNEI--SRAIEH-------------ISPD---YVIIDSIQTMTQPDIT---SVAGSVSQVRETTAELLKT 212
Cdd:PTZ00035 174 ERFGLDPEDVLDNIayARAYNHehqmqllsqaaakMAEErfaLLIVDSATALFRVDYSgrgELAERQQHLGKFLRALQKL 253
|
170
....*....|....
gi 1821249106 213 AKTNGIAIFIVGHV 226
Cdd:PTZ00035 254 ADEFNVAVVITNQV 267
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
81-227 |
2.98e-03 |
|
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: 39.26 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 81 IKTKLEELNRVLGGGVVPGSMVLIGGDPGIGKSTL--LLQVSQQLAAI----GGKVLYVSGEESaeqikLRAERLGSINT 154
Cdd:cd19514 1 ISTGSTELDKLLGGGIESMSITEVFGEFRTGKTQLshTLCVTAQLPGSmgggGGKVAYIDTEGT-----FRPDRIRPIAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 155 EFYLYAETDMNEI--SRAI--EHI-------------SPDY--VIIDSIQTMTQPDITSvAGSVSQVRETTAELL----K 211
Cdd:cd19514 76 RFGVDHDAVLDNIlyARAYtsEHQmelldyvaakfheEAVFrlLIIDSIMALFRVDFSG-RGELAERQQKLAQMLsrlqK 154
|
170
....*....|....*.
gi 1821249106 212 TAKTNGIAIFIVGHVT 227
Cdd:cd19514 155 ISEEYNVAVFITNQVT 170
|
|
| COG2888 |
COG2888 |
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ... |
7-42 |
3.19e-03 |
|
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];
Pssm-ID: 442134 [Multi-domain] Cd Length: 52 Bit Score: 35.48 E-value: 3.19e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1821249106 7 GGTMAKKSKVQFVCQNCGYvspKFLGRCPNCGKWNT 42
Cdd:COG2888 7 GREIAPEGGVAFYCPNCGE---ALIIRCPKCRKQSN 39
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
98-169 |
3.37e-03 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 38.45 E-value: 3.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821249106 98 PGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLyVSGEESAEQIKLRAERLGSINTEFYLYAETDMNEISR 169
Cdd:cd03247 27 QGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDLEKALSSLISVLNQRPYLFDTTLRNNLGR 97
|
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
87-187 |
3.66e-03 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 39.14 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 87 ELNRVLGGgVVPGSMVLIGGDPGIGKSTLLLQVSQQLAAIGGKVLYVSGEESAEQI-KLRAERLGSIN-----TEFYLYA 160
Cdd:cd01122 32 SLNKLLKG-HRRGELTIFTGPTGSGKTTFLSEYSLDLCMQGVNTLWGSFEIKNVRLaKTMLTQFAGKNlednlREFDEWA 110
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1821249106 161 E---------------TDMNEISRAIEHISPDY----VIIDSIQTM 187
Cdd:cd01122 111 DkfellpmyfmkfhgsTDIDEVLDAMEHAVYVYdiqhIVIDNLQFM 156
|
|
| Nob1 |
COG1439 |
rRNA maturation endonuclease Nob1 [Translation, ribosomal structure and biogenesis]; |
2-38 |
5.08e-03 |
|
rRNA maturation endonuclease Nob1 [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441048 [Multi-domain] Cd Length: 155 Bit Score: 37.53 E-value: 5.08e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1821249106 2 IRIKGggtmAKKSKV-QFVCQNCGYVSPKFLGRCPNCG 38
Cdd:COG1439 113 IATKG----IKEVRKwRYRCTGCGREFDEPEEECPICG 146
|
|
| DUF2075 |
pfam09848 |
Schlafen group 3, DNA/RNA helicase domain; This domain is found in at the C terminus of group ... |
100-261 |
6.24e-03 |
|
Schlafen group 3, DNA/RNA helicase domain; This domain is found in at the C terminus of group 3 Schlafen proteins from mammals, and represents the DNA/RNA helicase domain. Schlafen proteins are involved in the control of cell proliferation, induction of immune responses, and in the regulation of viral replication. These proteins inhibit DNA replication and promote cell death in response to DNA damage. They play a role in genome surveillance to kill cells with defective replication. This domain is also found in various uncharacterized prokaryotic proteins fused to a DNA helicase, GIY-YIG or PD-(D/E)XK catalytic domain or HsdR-N(terminal) domain, which are similar to AAA DNA helicase, Type III restriction enzyme ATPase, RecD and RuvB helicase.
Pssm-ID: 430875 [Multi-domain] Cd Length: 355 Bit Score: 38.80 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 100 SMVLIGGDPGIGKSTLLLQVSQQLAAI--GGKVLYVSG---EESAEQIKLRAERLGSINTEFYLYAETDMNEISRAIEHI 174
Cdd:pfam09848 2 AVFLVTGGPGTGKTVIGLNLFAELEDSdlGRTAVYLSGnhpLVLVLYEALAGDLRKKRKKSAFQRPTSFINNLHKTHPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 175 spDYVIIDSIQTM-TQPDitsvagsvSQVRETTAELLKTA-KTNGIAIFIVGH--VTKEGSIAGPRMLEHMVDTV-LYFE 249
Cdd:pfam09848 82 --DVVIFDEAHRLwDKSD--------PYNNFSGPNQLKEImKRAKVIVFLVDEgqVLNTGEYGGIEELKKIAPKWpAEIR 151
|
170
....*....|....
gi 1821249106 250 GEQH--HSFRILRA 261
Cdd:pfam09848 152 EKYHlkSQFRSGGS 165
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
44-210 |
6.28e-03 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 39.12 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 44 VEEIEQDTTDRRTRTSLTGEKAKPTKIADVV--PKKEPRIKTKLeelnrvlggGVVPGSMVLIGGDPGIGKSTLLLQVSQ 121
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVelPMKHPELFEHL---------GIEPPKGVLLYGPPGTGKTLLAKAVAN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 122 QlaaIGGKVLYVSGEEsaeqiklraerlgsINTEFYLYAETDMNEISRAIEHISPDYVIIDSIQTMTqPDITSVAGSVSq 201
Cdd:TIGR01243 235 E---AGAYFISINGPE--------------IMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIA-PKREEVTGEVE- 295
|
....*....
gi 1821249106 202 vRETTAELL 210
Cdd:TIGR01243 296 -KRVVAQLL 303
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
99-227 |
6.77e-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: 37.59 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821249106 99 GSMVLIGGDPGIGKSTLLLQVS------QQLAAIGGKVLYVSGEesaeqiklraerlGSINTefYLYAETDMNEISRAIE 172
Cdd:cd19492 1 GKITEICGVPGVGKTQLCMQLAvnvqipKCFGGLAGEAIYIDTE-------------GSFNI--HYFRVHDYVELLALIN 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821249106 173 HIsPDY---------VIIDSIqtmTQP---DITSVAGSVSQVRETTAELLKTAKTNGIAIFIVGHVT 227
Cdd:cd19492 66 SL-PKFledhpkvklIVVDSI---AFPfrhDFDDLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVT 128
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
73-140 |
6.81e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 37.63 E-value: 6.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821249106 73 VVPKKEPRIKTKLEELnRVLGGGVVPGSMVLIGGDPGIGKSTLLLQVSQQL---AAIGGKVLYvSGEESAE 140
Cdd:cd03233 8 NISFTTGKGRSKIPIL-KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHY-NGIPYKE 76
|
|
| HybF |
COG0375 |
Hydrogenase maturation factor HypA/HybF, metallochaperone involved in Ni insertion ... |
8-46 |
6.86e-03 |
|
Hydrogenase maturation factor HypA/HybF, metallochaperone involved in Ni insertion [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440144 Cd Length: 113 Bit Score: 36.30 E-value: 6.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1821249106 8 GTMAKKSK-------VQFVCQNCGYVSP--KFLGRCPNCGKWNTMVEE 46
Cdd:COG0375 54 GTIAEGAEleieevpARARCRDCGKEFEleELFLRCPKCGSPDLEILS 101
|
|
| RPB9 |
COG1594 |
DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]; ... |
8-68 |
8.05e-03 |
|
DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS [Transcription]; DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS is part of the Pathway/BioSystem: RNA polymerase
Pssm-ID: 441202 [Multi-domain] Cd Length: 103 Bit Score: 36.08 E-value: 8.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821249106 8 GTMAKKSKVQFVCQNCGYVSPKflgrcpNCGKWNTMVEEIEQDTTDrRTRTSLTGEKAKPT 68
Cdd:COG1594 7 GSMMKPKDGVLVCPKCGYEEPR------DEEAEAKYVSTEEQEDKE-IIVVEEEEVEGLPT 60
|
|
| PRK11788 |
PRK11788 |
tetratricopeptide repeat protein; Provisional |
13-43 |
9.67e-03 |
|
tetratricopeptide repeat protein; Provisional
Pssm-ID: 236983 [Multi-domain] Cd Length: 389 Bit Score: 38.25 E-value: 9.67e-03
10 20 30
....*....|....*....|....*....|.
gi 1821249106 13 KSKVQFVCQNCGYVSPKFLGRCPNCGKWNTM 43
Cdd:PRK11788 350 KRKPRYRCRNCGFTARTLYWHCPSCKAWETI 380
|
|
| |
