|
Name |
Accession |
Description |
Interval |
E-value |
| sms |
TIGR00416 |
DNA repair protein RadA; The gene protuct codes for a probable ATP-dependent protease involved ... |
1-454 |
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: 812.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 1 MAKApKRAFVCNECGADYPRWQGQCSACHAWNTITEMRIAASPQVARNERLSGYAGNAGVSKVQKLSDISLEALPRFSTG 80
Cdd:TIGR00416 1 MAKA-KSKFVCQHCGADSPKWQGKCPACHAWNTITEERLHRSLGAQKNRRNSGKAGIPQAQKSQTISAIELEEVPRFSSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 81 FKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAE-GMKTLYVTGEESLQQVAMRAHRLGLPTANLNMLSETSI 159
Cdd:TIGR00416 80 FGELDRVLGGGIVPGSLILIGGDPGIGKSTLLLQVACQLAKnQMKVLYVSGEESLQQIKMRAIRLGLPEPNLYVLSETNW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 160 EQICQIADEEKPQLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDC 239
Cdd:TIGR00416 160 EQICANIEEENPQACVIDSIQTLYSPDISSAPGSVSQVRECTAELMRLAKTRGIAIFIVGHVTKEGSIAGPKVLEHMVDT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 240 SVLLDGDADSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVSNPSAIFLSRGDEITSGSSVMVVWEGTRPLLVEIQALVD 319
Cdd:TIGR00416 240 VLYFEGDRDSRFRILRSVKNRFGATNEIGIFEMTEQGLREVLNPSAIFLSRREEPMSGSSITVTWEGTRPLLVEIQALVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 320 HSMMSNPRRVAVGLEQNRLAILLAVLHRHGGLQMADQDVFVNVVGGVKVTETSADLALLLAMVSSLRDRPLPQDLVVFGE 399
Cdd:TIGR00416 320 PTSFANPRRVATGLDQNRLALLLAVLEKRLGLPLADQDVFLNVAGGVKVSEPAADLALLIAIVSSFRDRPLDPDLVFLGE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1195217170 400 VGLAGEIRPVPSGQERISEAAKHGFRRAIVPAANVPKKVPEGMQIFGVKKLSDAL 454
Cdd:TIGR00416 400 VGLAGEIRPVPSLEERLKEAAKLGFKRAIVPKANSPKTAPEGIKVIGVKKVGDAL 454
|
|
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
1-457 |
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: 803.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 1 MAKApKRAFVCNECGADYPRWQGQCSACHAWNTITEMRIAASPQVARNerlSGYAGNAgvSKVQKLSDISLEALPRFSTG 80
Cdd:COG1066 1 MAKT-KTVYVCQECGYESPKWLGRCPECGAWNTLVEEVVAKAKKGRAA---SGAAGRA--SKPVPLSEVEAEEEPRISTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 81 FKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAE-GMKTLYVTGEESLQQVAMRAHRLGLPTANLNMLSETSI 159
Cdd:COG1066 75 IGELDRVLGGGLVPGSVVLIGGEPGIGKSTLLLQVAARLAKkGGKVLYVSGEESASQIKLRAERLGLLSDNLYLLAETDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 160 EQICQIADEEKPQLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDC 239
Cdd:COG1066 155 EAILATIEELKPDLLVIDSIQTMYSEELESAPGSVSQVRECAAELIRLAKETGIAVFLVGHVTKEGSIAGPRVLEHMVDT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 240 SVLLDGDADSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVSNPSAIFLSRGDEITSGSSVMVVWEGTRPLLVEIQALVD 319
Cdd:COG1066 235 VLYFEGDRHSRYRILRAVKNRFGSTNEIGVFEMTEKGLREVSNPSELFLSERDEPVPGSAVTVTMEGTRPLLVEVQALVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 320 HSMMSNPRRVAVGLEQNRLAILLAVLHRHGGLQMADQDVFVNVVGGVKVTETSADLALLLAMVSSLRDRPLPQDLVVFGE 399
Cdd:COG1066 315 PSSFGNPRRTAVGLDSNRLAMLLAVLEKRAGLPLGDQDVYVNVVGGLKITEPAADLAVALAIASSFRDRPLPPDTVFFGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195217170 400 VGLAGEIRPVPSGQERISEAAKHGFRRAIVPAANVPKKVPEGMQIFGVKKLSDALSVF 457
Cdd:COG1066 395 VGLTGEIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKLKPKGIEIIGVSTLEEALEAL 452
|
|
| RadA_SMS_N |
cd01121 |
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ... |
9-280 |
2.06e-156 |
|
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: 443.90 E-value: 2.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 9 FVCNECGADYPRWQGQCSACHAWNTITEMRIAASPQVARNERLSGyagnaGVSKVQKLSDISLEALPRFSTGFKEFDRVL 88
Cdd:cd01121 1 YVCQECGYESPKWLGRCPSCGEWNTFVEEVVSASSSASRRASASP-----SPSKPLPLSDVEAEEEERISTGIGELDRVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 89 GGGVVPGSAILIGGNPGAGKSTLLLQTLCKLA-EGMKTLYVTGEESLQQVAMRAHRLGLPTANLNMLSETSIEQICQIAD 167
Cdd:cd01121 76 GGGLVPGSVVLIGGDPGIGKSTLLLQVAARLAqRGGKVLYVSGEESLSQIKLRAERLGLGSDNLYLLAETNLEAILAEIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 168 EEKPQLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDCSVLLDGDA 247
Cdd:cd01121 156 ELKPSLVVIDSIQTVYSPELTSSPGSVSQVRECAAELLRLAKETGIPVFLVGHVTKDGAIAGPKVLEHMVDTVLYFEGDR 235
|
250 260 270
....*....|....*....|....*....|...
gi 1195217170 248 DSRFRTLRSHKNRFGAVNELGVFAMTEQGLREV 280
Cdd:cd01121 236 GSSYRILRSVKNRFGPTNEIGVFEMTENGLREV 268
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
76-278 |
1.90e-26 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 106.54 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 76 RFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCK-LAEGMKTLYVTGEESLQQVAMRAHRLGLPTANL--- 151
Cdd:COG0467 1 RVPTGIPGLDELLGGGLPRGSSTLLSGPPGTGKTTLALQFLAEgLRRGEKGLYVSFEESPEQLLRRAESLGLDLEEYies 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 152 NMLS-------------ETSIEQICQIADEEKPQLMVIDSIQVMHMADVQSspgsvAQVRETAAYLTRFAKTRGVAIVMV 218
Cdd:COG0467 81 GLLRiidlspeelgldlEELLARLREAVEEFGAKRVVIDSLSGLLLALPDP-----ERLREFLHRLLRYLKKRGVTTLLT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195217170 219 GHVTKDGSLAGPKVLEHCIDCSVLLD--GDADSRFRTLRSHKNRFGAV-NELGVFAMTEQGLR 278
Cdd:COG0467 156 SETGGLEDEATEGGLSYLADGVILLRyvELGGELRRALSVLKMRGSAHdRTIREFEITDGGIE 218
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
91-334 |
2.34e-19 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 88.42 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 91 GVVP-GSAILIGGNPGAGKSTLLLQTLCKLAEGM----------KTLYVTGEESLQQVAMRAHRLG--------LPTANL 151
Cdd:COG3598 8 GLLPeGGVTLLAGPPGTGKSFLALQLAAAVAAGGpwlgrrvppgKVLYLAAEDDRGELRRRLKALGadlglpfaDLDGRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 152 NMLSET-------SIEQICQIADEEKPQLMVIDSIQVMHMADVQSSpgsvAQVRETAAYLTRFAKTRGVAIVMVGHVTKD 224
Cdd:COG3598 88 RLLSLAgdlddtdDLEALERAIEEEGPDLVVIDPLARVFGGDENDA----EEMRAFLNPLDRLAERTGAAVLLVHHTGKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 225 G-------SLAGPKVLEHCIDCSVLLDGDADSRFRTLRSHKNRFGAVNELGVfaMTEQGLREVSNPSAIFLSRGDEITSG 297
Cdd:COG3598 164 GagkdsgdRARGSSALRGAARSVLVLSREKGEDLRVLTRAKSNYGPEIALRW--DNGGRLALEEVAALTAGAGEVELKEL 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 1195217170 298 SSVMVVWeGTRPLLVEIQALVDHSMMSNPRRVAVGLE 334
Cdd:COG3598 242 VGGVART-GTDSELEEGLLEVPLAEAESAGEDAELAA 277
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
78-262 |
6.16e-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: 85.39 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCK-LAEGMKTLYVTGEESLQQVAMRAHRLGL---------- 146
Cdd:cd01124 2 KTGIPGLDELLGGGIPKGSVTLLTGGPGTGKTLFGLQFLYAgAKNGEPGLFFTFEESPERLLRNAKSFGWdfdemedegk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 147 -------PTANLNMLSETSIEQICQIADEEKPQLMVIDSIQVMHMADVQSSpgsvaQVRETAAYLTRFAKTRGVAIVMVG 219
Cdd:cd01124 82 liivdapPTEAGRFSLDELLSRILSIIKSFKAKRVVIDSLSGLRRAKEDQM-----RARRIVIALLNELRAAGVTTIFTS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1195217170 220 HVTKDGS--LAGPKVLEHCIDCSVLLD---GDADSRfRTLRSHKNRFG 262
Cdd:cd01124 157 EMRSFLSseSAGGGDVSFIVDGVILLRyveIEGELR-RTIRVLKMRGT 203
|
|
| ATPase |
pfam06745 |
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ... |
78-260 |
7.85e-16 |
|
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: 76.52 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAE--GMKTLYVTGEESLQQVAMRAHRLG---------- 145
Cdd:pfam06745 2 KTGIPGLDEILKGGFPEGRVVLITGGPGTGKTIFGLQFLYNGALkyGEPGVFVTLEEPPEDLRENARSFGwdlekleeeg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 146 -------------LPTANLNMLSETSIEQICQIADEEKPQLMVIDSIQVMhmadVQSSpgSVAQVRETAAYLTRFAKTRG 212
Cdd:pfam06745 82 klaiidastsgigIAEVEDRFDLEELIERLREAIREIGAKRVVIDSITTL----FYLL--KPAVAREILRRLKRVLKGLG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1195217170 213 VAIVMVGHVTKD-GSLAGPKVLEHCIDCSVLLDGD--ADSRFRTLRSHKNR 260
Cdd:pfam06745 156 VTAIFTSEKPSGeGGIGGYGVEEFIVDGVIRLDLKeiEEERVRTIEIVKMR 206
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
78-260 |
3.46e-14 |
|
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: 71.58 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAE-GMKTLYVTGE----ESLQQVAmrAHRLGLPTANLN 152
Cdd:cd01394 2 STGSKSLDSLLGGGVERGTITQIYGPPGSGKTNICLQLAVEAAKqGKKVVYIDTEglspERFQQIA--GERFESIASNII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 153 MLSETSIEQ-------ICQIADEEKPQLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHV---T 222
Cdd:cd01394 80 VFEPYSFDEqgvaiqeAEKLLKSDKVDLVVVDSATALYRLELGDDSEANRELSRQMSKLLSIARKYDIPVVITNQVysdI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1195217170 223 KDGSLA--GPKVLEHCIDCSVLLD-GDADSRFRTLRSHKNR 260
Cdd:cd01394 160 DDDRLKpvGGTLLEHWSKAIIRLEkSPPGLRRATLEKHRSR 200
|
|
| KaiC-like_N |
cd19488 |
N-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
78-179 |
4.51e-13 |
|
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: 68.53 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCK-LAEGMKTLYVTGEESLQQVAMRAHRLGL---------- 146
Cdd:cd19488 2 STGIPGLDDILRGGLPPRRLYLVEGAPGTGKTTLALQFLLEgAANGETGLYITLSETEQELRAVALSHGWsldgihifel 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1195217170 147 --------PTANLNMLSETSIE------QICQIADEEKPQLMVIDSI 179
Cdd:cd19488 82 spsesaldAAQQYTILHPSELElsettrLIFERVERLKPSRVVIDSL 128
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
88-226 |
2.90e-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: 65.48 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 88 LGGGVVP-GSAILIGGNPGAGKSTLLLQTLCKLAEG------------MKTLYVTGEESLQQVAMRAHRLGL-------- 146
Cdd:pfam13481 25 LIKGLLPaGGLGLLAGAPGTGKTTLALDLAAAVATGkpwlggprvpeqGKVLYVSAEGPADELRRRLRAAGAdldlparl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 147 ----PTANLNMLSETS--------IEQICQIADE-EKPQLMVIDSIQVMHMADVQSSpgsvAQVRETAAYLTRFAKTRGV 213
Cdd:pfam13481 105 lflsLVESLPLFFLDRggplldadVDALEAALEEvEDPDLVVIDPLARALGGDENSN----SDVGRLVKALDRLARRTGA 180
|
170
....*....|...
gi 1195217170 214 AIVMVGHVTKDGS 226
Cdd:pfam13481 181 TVLLVHHVGKDGA 193
|
|
| KaiC_C |
cd19484 |
C-terminal domain of Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most ... |
78-217 |
9.63e-12 |
|
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: 64.27 E-value: 9.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVL-GGGVVPGSAILIGGNPGAGKSTL---LLQTLCklAEGMKTLYVTGEESLQQVA----------MRAHR 143
Cdd:cd19484 2 STGIPRLDAMLgGGGFFRGSSILVSGATGTGKTLLaasFADAAC--RRGERCLYFAFEESPAQLIrnaksigidlEQMER 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195217170 144 LGLPTANLNMLSETSIE----QICQIADEEKPQLMVIDSIQVMhmadvqSSPGSVAQVRETAAYLTRFAKTRGVAIVM 217
Cdd:cd19484 80 KGLLKIICARPELYGLEdhliIIKSEINEFKPSRVIVDPLSAL------ARGGSLNEVKEFVIRLIDYLKSQEITGLF 151
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
64-214 |
1.88e-11 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 66.06 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 64 QKLSDIslealpRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLL---LQTLCklAEGMKTLYVTGEESLQQVAMR 140
Cdd:PRK09302 248 QRSSNE------RISSGVPDLDEMLGGGFFRGSIILVSGATGTGKTLLAskfAEAAC--RRGERCLLFAFEESRAQLIRN 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 141 AHRLGL-----------------PT-ANLnmlsETSIEQICQIADEEKPQLMVIDSIQVMHmadvqsSPGSVAQVRETAA 202
Cdd:PRK09302 320 ARSWGIdlekmeekgllkiicarPEsYGL----EDHLIIIKREIEEFKPSRVAIDPLSALA------RGGSLNEFRQFVI 389
|
170
....*....|..
gi 1195217170 203 YLTRFAKTRGVA 214
Cdd:PRK09302 390 RLTDYLKSEEIT 401
|
|
| Rubredoxin_2 |
pfam18073 |
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ... |
9-36 |
2.59e-11 |
|
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: 57.94 E-value: 2.59e-11
10 20
....*....|....*....|....*...
gi 1195217170 9 FVCNECGADYPRWQGQCSACHAWNTITE 36
Cdd:pfam18073 1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
|
|
| KaiC-N |
cd19485 |
N-terminal domain of Circadian Clock Protein Kaic; KaiC is a circadian clock protein, most ... |
79-260 |
7.13e-11 |
|
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: 62.00 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 79 TGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTlckLAEGMKT-----LYVTGEESLQQVAMRAHRLGLPTANLNM 153
Cdd:cd19485 3 TGIEGFDDITHGGLPKGRPTLICGTAGTGKTLFAAQF---LVNGIKEfgepgVFVTFEESPEDIIKNMASFGWDLPKLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 154 LSETSIEQICQIADEE----------------------KPQLMVIDSIQV--MHMADvqsspgsVAQVRETAAYLTRFAK 209
Cdd:cd19485 80 EGKLLILDASPEPSEEevtgeydleallirieyairkiGAKRVSLDSLEAvfSGLSD-------SAVVRAELLRLFAWLK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1195217170 210 TRGVAIVMVGHVTKDGSLAGPKVLEHCIDCSVLLDG--DADSRFRTLRSHKNR 260
Cdd:cd19485 153 QKGVTAIMTGERGEDGPLTRYGVEEYVSDCVVILRNvlEGERRRRTLEILKYR 205
|
|
| KaiC-like_C |
cd19487 |
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock ... |
78-278 |
1.28e-10 |
|
C-terminal domain of KaiC family protein; uncharacterized subfamily; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410895 [Multi-domain] Cd Length: 219 Bit Score: 61.16 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQ-TLCKLAEGMKTLYVTGEESLQQVAMRAHRLGLPTANLNMLSE 156
Cdd:cd19487 2 SSGVPELDELLGGGLERGTSTLLIGPAGVGKSTLALQfAKAAAARGERSVLFSFDESIGTLFERSEALGIDLRAMVEKGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 157 TSIEQI-----------CQI---ADEEKPQLMVIDSI----QVMHMADVqsspgSVAQVRETAAYLTRfaktRGVAIVMV 218
Cdd:cd19487 82 LSIEQIdpaelspgefaQRVrtsVEQEDARVVVIDSLngylNAMPDERF-----LILQMHELLSYLNN----QGVTTLLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 219 ghVTKDGSLAGPKVLEhcIDCSVLLDG-------DADSRFR-TLRSHKNRFGAvNELGV--FAMTEQGLR 278
Cdd:cd19487 153 --VAQHGLLGGDMGTP--VDISYLADTvvllryfEAEGEVRkAISVLKKRTGD-HERTIreFRITRSGLK 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
94-244 |
2.51e-10 |
|
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: 58.54 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 94 PGSAILIGGNPGAGKSTLLLQTLCKL-AEGMKTLYVTGEESLQQVAMRAHRLGLPTANLNMLSETSIEQICQIADEEKPQ 172
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195217170 173 LMVIDSIQVMHMADVQSSpgsvAQVRETAAYLTRFAKTRGVAIVMVGHVTKDgslAGPKVLEHCIDCSVLLD 244
Cdd:smart00382 81 VLILDEITSLLDAEQEAL----LLLLEELRLLLLLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIVLL 145
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
99-227 |
2.16e-09 |
|
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: 57.78 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 99 LIGGNPGAGKSTLLLQTLCKLAEGM-----------KTLYVTGEESLQQVAMRAHRLGL-----PTANLNMLS------- 155
Cdd:cd01125 5 MLVGPPGSGKSFLALDLAVAVATGRdwlgerrvkqgRVVYLAAEDPRDGLRRRLKAIGAhlgdeDAALAENLVienlrgk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 156 -------ETSIEQIcqIADEEKPQLMVIDSIQ-VMHMADvQSSPGSVAQVretAAYLTRFAKTRGVAIVMVGHVTKDGSL 227
Cdd:cd01125 85 pvsidaeAPELERI--IEELEGVRLIIIDTLArVLHGGD-ENDAADMGAF---VAGLDRIARETGAAVLLVHHTGKDAAG 158
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
371-433 |
3.04e-09 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 54.76 E-value: 3.04e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195217170 371 TSADLALLLAMVSSLRDRPLPQDLVVFGEVGLAGEIRPVPSGQERISEAAKHGFRRAIVPAAN 433
Cdd:pfam13541 59 SSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| PRK09302 |
PRK09302 |
circadian clock protein KaiC; Reviewed |
67-277 |
7.47e-09 |
|
circadian clock protein KaiC; Reviewed
Pssm-ID: 236461 [Multi-domain] Cd Length: 509 Bit Score: 57.58 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 67 SDISLEALPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTlckLAEGMKT-----LYVTGEESLQQVAMRA 141
Cdd:PRK09302 3 QPSASPGIEKLPTGIEGFDDITHGGLPKGRPTLVSGTAGTGKTLFALQF---LVNGIKRfdepgVFVTFEESPEDIIRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 142 HRLGLPTANLNMLSETSIEQICQIADEE----------------------KPQLMVIDSIQVmhmadVQSSPGSVAQVRE 199
Cdd:PRK09302 80 ASFGWDLQKLIDEGKLFILDASPDPSEQeeageydlealfirieyaidkiGAKRVVLDSIEA-----LFSGFSNEAVVRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 200 TAAYLTRFAKTRGVAIVMVGHVTKD-GSLAGPKVLEHCIDCSVLLDG--DADSRFRTLRSHKNRfGAVNELG--VFAMTE 274
Cdd:PRK09302 155 ELRRLFAWLKQKGVTAVITGERGDEyGPLTRYGVEEFVSDCVIILRNrlEGEKRTRTLRILKYR-GTTHGKNeyPFTITE 233
|
...
gi 1195217170 275 QGL 277
Cdd:PRK09302 234 DGI 236
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
375-457 |
2.35e-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: 56.20 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 375 LALLLAMvSSLRDRPLpQDLVVFGEVGLAGEIRPV----PSgqerISEAAKHGFRRAIVPAANVPK-KVPEGMQIFGVKK 449
Cdd:COG0606 86 LGILAAS-GQIPAEAL-EDYVFLGELSLDGSLRPVrgvlPA----ALAAREAGIRRLIVPAANAAEaALVPGIEVYGASS 159
|
....*...
gi 1195217170 450 LSDALSVF 457
Cdd:COG0606 160 LLEVVAFL 167
|
|
| DnaB_C |
cd00984 |
C-terminal domain of DnaB helicase; DnaB helicase C-terminal domain. The hexameric helicase ... |
78-190 |
1.28e-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: 52.51 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGgVVPGSAILIGGNPGAGKSTLLLQTLCKLA--EGMKTLYVTGEESLQQVAMR---------AHRLGL 146
Cdd:cd00984 3 PTGFTDLDKLTGG-LQPGDLIIIAARPSMGKTAFALNIAENIAldEGLPVLFFSLEMSAEQLAERllssesgvsLSKLRT 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195217170 147 P----------TANLNMLSE----------TSIEQICQIA-----DEEKPQLMVIDSIQVMHMADVQSS 190
Cdd:cd00984 82 GrlddedwerlTAAMGELSElplyiddtpgLTVDEIRAKArrlkrEHGGLGLIVIDYLQLIRGSKRAEN 150
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
98-224 |
2.48e-07 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 49.42 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 98 ILIGGNPGAGKSTLLLQT-LCKLAEGMKTLYVTGEESLqqvamrahrlglptanlnmlsetsIEQICQIADEEKPQLMVI 176
Cdd:cd01120 1 ILITGPPGSGKTTLLLQFaEQALLSDEPVIFISFLDTI------------------------LEAIEDLIEEKKLDIIII 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1195217170 177 DSIQVMHMAdvqSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKD 224
Cdd:cd01120 57 DSLSSLARA---SQGDRSSELLEDLAKLLRAARNTGITVIATIHSDKF 101
|
|
| Rad51_DMC1_archRadA |
cd01123 |
recombinase Rad51, DMC1, and archaeal RadA; This group of recombinases includes the eukaryotic ... |
78-224 |
2.81e-07 |
|
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: 51.38 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTLCKLAE--------GMKTLYVTGEESLQQVAMR--AHRLGL- 146
Cdd:cd01123 2 TTGSKELDKLLGGGIETGSITEMFGEFRTGK-TQLCHTLAVTCQlpidrgggEGKAIYIDTEGTFRPERLRaiAQRFGLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 147 PTANLNML-------SETSIEQICQIAD---EEKPQLMVIDSIQVMHMADVqSSPGSVAQVRETAAY----LTRFAKTRG 212
Cdd:cd01123 81 PDDVLDNVayarafnSDHQTQLLDQAAAmmvESRFKLLIVDSATALYRTDY-SGRGELSARQMHLAKflrmLQRLADEFG 159
|
170
....*....|..
gi 1195217170 213 VAIVMVGHVTKD 224
Cdd:cd01123 160 VAVVVTNQVVAQ 171
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
372-456 |
9.82e-07 |
|
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: 49.16 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 372 SADLALLLAMVSSLRDRPLPQDLVVFGEVGLAGEIRPVPSGQERISEAAKHGFRRAIVPAAN------VPKKVPEGMQIF 445
Cdd:pfam05362 111 SAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENekdledIPENVREGLEII 190
|
90
....*....|.
gi 1195217170 446 GVKKLSDALSV 456
Cdd:pfam05362 191 PVEHVDEVLKH 201
|
|
| FlaH |
COG2874 |
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility]; |
76-131 |
1.05e-06 |
|
Archaellum biogenesis ATPase ArlH/FlaH [Cell motility];
Pssm-ID: 442121 Cd Length: 230 Bit Score: 49.45 E-value: 1.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195217170 76 RFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQtLCK--LAEGMKTLYVTGE 131
Cdd:COG2874 2 IISTGNDELDKRLGGGIPLGSLVLIEGENGTGKSVLSQQ-FAYgaLENGLSVTYISTE 58
|
|
| radB |
PRK09361 |
DNA repair and recombination protein RadB; Provisional |
76-281 |
1.09e-06 |
|
DNA repair and recombination protein RadB; Provisional
Pssm-ID: 236482 [Multi-domain] Cd Length: 225 Bit Score: 49.48 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 76 RFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAE-GMKTLYVTGE----ESLQQVAmrahrlglpTAN 150
Cdd:PRK09361 4 RLPTGCKMLDELLGGGFERGTITQIYGPPGSGKTNICLQLAVEAAKnGKKVIYIDTEglspERFKQIA---------GED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 151 LNMLSETSI--------EQICQIADEEK-----PQLMVIDSIQVMHMADVQSSPGSVAQVRETAA---YLTRFAKTRGVA 214
Cdd:PRK09361 75 FEELLSNIIifepssfeEQSEAIRKAEKlakenVGLIVLDSATSLYRLELEDEEDNSKLNRELGRqltHLLKLARKHDLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1195217170 215 IVMVGHVTKD---GSL--AGPKVLEHCIDCSVLLDGDADS-RFRTLRSHknRFGAVNELGVFAMTEQGLREVS 281
Cdd:PRK09361 155 VVITNQVYSDidsDGLrpLGGHTLEHWSKTILRLEKFRNGkRRATLEKH--RSRPEGESAEFRITDRGIEIID 225
|
|
| Rad51 |
pfam08423 |
Rad51; Rad51 is a DNA repair and recombination protein and is a homolog of the bacterial ... |
76-224 |
1.10e-06 |
|
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: 49.99 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 76 RFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTLCKLAE------GM--KTLYVTGE-----ESLQQVamrAH 142
Cdd:pfam08423 18 QITTGSKELDKLLGGGIETGSITEIFGEFRTGK-TQLCHTLCVTCQlplemgGGegKALYIDTEgtfrpERLVAI---AE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 143 RLGL-PTANLNMLS----------ETSIEQICQIADEEKPQLMVIDSIQVMHMADVqSSPGSVA----QVRETAAYLTRF 207
Cdd:pfam08423 94 RYGLdPEDVLDNVAyaraynsehqMQLLQQAAAMMSESRFALLIVDSATALYRTDF-SGRGELAerqqHLAKFLRTLQRL 172
|
170
....*....|....*..
gi 1195217170 208 AKTRGVAIVMVGHVTKD 224
Cdd:pfam08423 173 ADEFGVAVVITNQVVAQ 189
|
|
| DnaB |
COG0305 |
Replicative DNA helicase [Replication, recombination and repair]; |
60-218 |
1.34e-06 |
|
Replicative DNA helicase [Replication, recombination and repair];
Pssm-ID: 440074 [Multi-domain] Cd Length: 429 Bit Score: 50.46 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 60 VSKVQKLSDISlEALPRFSTGFKEFDRVLgGGVVPGSAILIGGNPGAGKSTLLLQTLCKLA--EGMKTLYVTGEESLQQV 137
Cdd:COG0305 158 LERIEELYKNG-GGITGVPTGFTDLDKLT-GGLQPGDLIILAARPSMGKTAFALNIARNAAikEGKPVAIFSLEMSAEQL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 138 AMRahrlglptanlnMLS-ETSIEQ--IC--QIADEEKPQLMviDSIQVMHMAD--VQSSPG-SVAQVRETAaylTRFAK 209
Cdd:COG0305 236 VMR------------LLSsEARIDSskLRtgKLSDEDWERLS--SAAGELSEAPiyIDDTPGlTIAEIRAKA---RRLKR 298
|
....*....
gi 1195217170 210 TRGVAIVMV 218
Cdd:COG0305 299 EHGLGLIVI 307
|
|
| XRCC3 |
cd19491 |
XRCC3 recombinase; XRCC3 (X-ray repair complementing defective repair in Chinese hamster cells ... |
84-222 |
4.26e-06 |
|
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: 48.06 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 84 FDRVLGGGVVPGSAILIGGNPGAGKSTLLLQtLC---KLAE---GM--KTLYVTGEES-----LQQVAMRAHRLGLPTAN 150
Cdd:cd19491 1 LDELLGGGIPVGGITEIAGESGAGKTQLCLQ-LAltvQLPRelgGLggGAVYICTESSfpskrLQQLASSLPKRYHLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 151 LNMLSETSIEQICQIAD-------------EEKP-QLMVIDSIQVMHMADVQSSPGSVAQ----VRETAAYLTRFAKTRG 212
Cdd:cd19491 80 KNFLDNIFVEHVADLETlehclnyqlpallERGPiRLVVIDSIAALFRSEFDTSRSDLVErakyLRRLADHLKRLADKYN 159
|
170
....*....|
gi 1195217170 213 VAIVMVGHVT 222
Cdd:cd19491 160 LAVVVVNQVT 169
|
|
| PRK05973 |
PRK05973 |
replicative DNA helicase; Provisional |
92-221 |
5.26e-06 |
|
replicative DNA helicase; Provisional
Pssm-ID: 168322 [Multi-domain] Cd Length: 237 Bit Score: 47.72 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 92 VVPGSAILIGGNPGAGKSTLLLQTLCKLAE-GMKTLYVTGEESLQQVAMRAHRLGLPTANLNMLSE--TSiEQIC----- 163
Cdd:PRK05973 61 LKPGDLVLLGARPGHGKTLLGLELAVEAMKsGRTGVFFTLEYTEQDVRDRLRALGADRAQFADLFEfdTS-DAICadyii 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 164 -QIADEEKPQLMVIDSIQVMhmaDVQ-SSPGSVAQVREtaayLTRFAKTRGVAIVMVGHV 221
Cdd:PRK05973 140 aRLASAPRGTLVVIDYLQLL---DQRrEKPDLSVQVRA----LKSFARERGLIIVFISQI 192
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
356-456 |
1.07e-05 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 48.01 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 356 QDVFVNVVGGVKVTE-TSADLALLLAMVSSLRDRPLPQDLVVFGEVGLAGEIRPVPSGQERISEAAKHGFRRAIVPAAN- 433
Cdd:PRK10787 662 RDIHVHVPEGATPKDgPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENk 741
|
90 100
....*....|....*....|....*...
gi 1195217170 434 -----VPKKVPEGMQIFGVKKLSDALSV 456
Cdd:PRK10787 742 rdleeIPDNVIADLDIHPVKRIEEVLTL 769
|
|
| Rad51 |
cd19513 |
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous ... |
77-222 |
1.24e-05 |
|
RAD51D recombinase; RAD51 recombinase plays an essential role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51 is recruited to the break site with the help of its paralogs, RAD51D, RAD51B, RAD51C, XRCC3, and XRCC2, where it forms long helical polymers which wrap around the ssDNA tail at the break which leads to pairing and strand invasion.
Pssm-ID: 410921 [Multi-domain] Cd Length: 235 Bit Score: 46.54 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 77 FSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLL--LQTLCKL------AEGmKTLYVTGE-----ESLQQVamrAHR 143
Cdd:cd19513 1 ITTGSKELDKLLGGGIETGSITELFGEFRTGKTQLChtLAVTCQLpidqggGEG-KALYIDTEgtfrpERLLAI---AER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 144 LGL-PTANLNMLSETS----------IEQICQIADEEKPQLMVIDSIQVMHMADVqSSPGSVAQvRET--AAYL---TRF 207
Cdd:cd19513 77 YGLnGEDVLDNVAYARayntdhqmqlLIQASAMMAESRYALLIVDSATALYRTDY-SGRGELSA-RQMhlAKFLrmlQRL 154
|
170
....*....|....*
gi 1195217170 208 AKTRGVAIVMVGHVT 222
Cdd:cd19513 155 ADEFGVAVVITNQVV 169
|
|
| PTZ00035 |
PTZ00035 |
Rad51 protein; Provisional |
76-224 |
1.60e-05 |
|
Rad51 protein; Provisional
Pssm-ID: 185407 [Multi-domain] Cd Length: 337 Bit Score: 46.91 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 76 RFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTLCKLA---------EGmKTLYVTGE-----ESLQQVamrA 141
Cdd:PTZ00035 99 RITTGSTQLDKLLGGGIETGSITELFGEFRTGK-TQLCHTLCVTCqlpieqgggEG-KVLYIDTEgtfrpERIVQI---A 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 142 HRLGL-PTANL-NML------SETSIEQICQIAD---EEKPQLMVIDSIQVMHMADVqSSPGSVAQvRETA-----AYLT 205
Cdd:PTZ00035 174 ERFGLdPEDVLdNIAyaraynHEHQMQLLSQAAAkmaEERFALLIVDSATALFRVDY-SGRGELAE-RQQHlgkflRALQ 251
|
170
....*....|....*....
gi 1195217170 206 RFAKTRGVAIVMVGHVTKD 224
Cdd:PTZ00035 252 KLADEFNVAVVITNQVMAD 270
|
|
| PRK06067 |
PRK06067 |
flagellar accessory protein FlaH; Validated |
78-133 |
1.90e-05 |
|
flagellar accessory protein FlaH; Validated
Pssm-ID: 180381 Cd Length: 234 Bit Score: 45.73 E-value: 1.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKStLLLQTLCK--LAEGMKTLYVTGEES 133
Cdd:PRK06067 8 STGNEELDRKLGGGIPFPSLILIEGDHGTGKS-VLSQQFVYgaLKQGKKVYVITTENT 64
|
|
| DnaB_C |
pfam03796 |
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at ... |
78-218 |
4.93e-05 |
|
DnaB-like helicase C terminal domain; The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli 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: 427509 [Multi-domain] Cd Length: 254 Bit Score: 44.71 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGgVVPGSAILIGGNPGAGKSTLLLqTLCK---LAEGMKTLYVTGEESLQQVAMRahrlglptanlnML 154
Cdd:pfam03796 3 PTGFTDLDRLTGG-LQPGDLIIIAARPSMGKTAFAL-NIARnaaVKHKKPVAIFSLEMSAEQLVMR------------LL 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195217170 155 S-ETSIEQ----ICQIADEEKPQLMviDSIQVMHMAD--VQSSPG-SVAQVRetaAYLTRFAKTRGVAIVMV 218
Cdd:pfam03796 69 AsEAGVDSqklrTGQLTDEDWEKLA--KAAGRLSEAPlyIDDTPGlSIAEIR---AKARRLKREHGLGLIVI 135
|
|
| DMC1 |
cd19514 |
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in ... |
78-224 |
5.58e-05 |
|
homologous-pairing protein DMC1; DMC1 has a central role in homologous recombination in meiosis. It assembles at the sites of programmed DNA double-strand breaks and carries out a search for allelic DNA sequences located on homologous chromatids. It forms octameric rings.
Pssm-ID: 410922 [Multi-domain] Cd Length: 236 Bit Score: 44.27 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTLCKLAE--------GMKTLYVTGE-----ESLQQVamrAHRL 144
Cdd:cd19514 2 STGSTELDKLLGGGIESMSITEVFGEFRTGK-TQLSHTLCVTAQlpgsmgggGGKVAYIDTEgtfrpDRIRPI---AERF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 145 GL-PTANL-NML------SETSIEQICQIAD---EEKP-QLMVIDSIQVMHMADVqSSPGSVAQVRETAAY----LTRFA 208
Cdd:cd19514 78 GVdHDAVLdNILyaraytSEHQMELLDYVAAkfhEEAVfRLLIIDSIMALFRVDF-SGRGELAERQQKLAQmlsrLQKIS 156
|
170
....*....|....*.
gi 1195217170 209 KTRGVAIVMVGHVTKD 224
Cdd:cd19514 157 EEYNVAVFITNQVTAD 172
|
|
| PRK04328 |
PRK04328 |
hypothetical protein; Provisional |
73-137 |
1.35e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235281 Cd Length: 249 Bit Score: 43.53 E-value: 1.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1195217170 73 ALPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCK-LAEGMKTLYVTGEESLQQV 137
Cdd:PRK04328 1 MVKRVKTGIPGMDEILYGGIPERNVVLLSGGPGTGKSIFSQQFLWNgLQMGEPGVYVALEEHPVQV 66
|
|
| GvpD_P-loop |
pfam07088 |
GvpD gas vesicle protein, P-loop domain; This family consists of several archaeal GvpD gas ... |
94-256 |
2.37e-04 |
|
GvpD gas vesicle protein, P-loop domain; This family consists of several archaeal GvpD gas vesicle regulatory proteins. GvpD is involved in the regulation of gas vesicle formation and functions as a repressor through the interaction and the breakdown induction of the transcriptional activator GvpE. This domain includes the P-loop and the basic region 1 (bR1, an arginine-rich region) which are essential for GvpD repressive function.
Pssm-ID: 462087 Cd Length: 189 Bit Score: 41.87 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 94 PGSAILIGGNPGAGKSTLLLQTLCKLA--------------EGMKTLYVTGEESLQQVA---MRAHRLGLP--------T 148
Cdd:pfam07088 9 FGKTLLINGAPGTGKTLFTIRGLDVLRrhhdvlyvstrvdqETVSEMYFSGHGELDKTAfldLLQDPFGLPidvdvpfeK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 149 ANLNMLSETsIEQICQIAdeEKPqLMVIDSIQVM--HMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVmvghvtkdgS 226
Cdd:pfam07088 89 LDLHSLLEW-VDAINAIG--TRL-TIAFDSWDLIyeYLALRHDDPPDIETVTNQLAALARGSGARLVLVL---------E 155
|
170 180 190
....*....|....*....|....*....|
gi 1195217170 227 LAGPKVLEHCIDCSVLLDGDADSRFRTLRS 256
Cdd:pfam07088 156 TAQNSRLEYIVDGVVTLNVKNDDRGRTRRS 185
|
|
| recomb_RAD51 |
TIGR02239 |
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein ... |
78-226 |
2.84e-04 |
|
DNA repair protein RAD51; This eukaryotic sequence family consists of RAD51, a protein involved in DNA homologous recombination and repair. It is similar in sequence the exclusively meiotic recombinase DMC1 (TIGR02238), to archaeal families RadA (TIGR02236) and RadB (TIGR02237), and to bacterial RecA (TIGR02012).
Pssm-ID: 274048 [Multi-domain] Cd Length: 316 Bit Score: 42.79 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTL---CKL------AEGmKTLYVTGE-----ESLQQVamrAHR 143
Cdd:TIGR02239 79 TTGSKELDKLLGGGIETGSITEIFGEFRTGK-TQLCHTLavtCQLpidqggGEG-KALYIDTEgtfrpERLLAI---AER 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 144 LGL-PTANLNMLSETS----------IEQICQIADEEKPQLMVIDSIQVMHMADVQSSPGSVAQVRETAAY---LTRFAK 209
Cdd:TIGR02239 154 YGLnPEDVLDNVAYARayntdhqlqlLQQAAAMMSESRFALLIVDSATALYRTDFSGRGELSARQMHLARFlrsLQRLAD 233
|
170
....*....|....*....
gi 1195217170 210 TRGVAIVMVGHVTK--DGS 226
Cdd:TIGR02239 234 EFGVAVVITNQVVAqvDGA 252
|
|
| recomb_DMC1 |
TIGR02238 |
meiotic recombinase Dmc1; This model describes DMC1, a subfamily of a larger family of DNA ... |
78-280 |
4.07e-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: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTLCKLAE--------GMKTLYVTGEESLQQVAMR--AHRLGL- 146
Cdd:TIGR02238 79 TTGSQALDGILGGGIESMSITEVFGEFRCGK-TQLSHTLCVTAQlpremgggNGKVAYIDTEGTFRPDRIRaiAERFGVd 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 147 PTANL-NML------SETSIEQICQIAD---EEKPQLMVIDSIQVMHMADVqSSPGSVAQ----VRETAAYLTRFAKTRG 212
Cdd:TIGR02238 158 PDAVLdNILyaraytSEHQMELLDYLAAkfsEEPFRLLIVDSIMALFRVDF-SGRGELSErqqkLAQMLSRLNKISEEFN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 213 VAIVMVGHVTKDGS-----LAGPK------VLEHCIDCSVLL-DGDADSRFRTLRSHKNRfgAVNElGVFAMTEQGLREV 280
Cdd:TIGR02238 237 VAVFVTNQVQADPGatmtfIADPKkpigghVLAHASTTRILLrKGRGEERVAKLYDSPDM--PEAE-ASFQITEGGIADA 313
|
|
| RecA |
pfam00154 |
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA ... |
59-179 |
4.41e-04 |
|
recA bacterial DNA recombination protein; RecA is a DNA-dependent ATPase and functions in DNA repair systems. RecA protein catalyzes an ATP-dependent DNA strand-exchange reaction that is the central step in the repair of dsDNA breaks by homologous recombination.
Pssm-ID: 425488 [Multi-domain] Cd Length: 262 Bit Score: 42.00 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 59 GVSKVQKLSDISLEALPRFSTGFKEFDRVLG-GGVVPGSAILIGGNPGAGKSTLLLQTLCKL-AEGMKTLYVTGEESLQQ 136
Cdd:pfam00154 15 GKGSIMKLGDEKKLDVETISTGSLALDIALGiGGYPKGRIIEIYGPESSGKTTLALHAIAEAqKAGGTAAFIDAEHALDP 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1195217170 137 VamRAHRLGLPTANLNMLSETSIEQICQIAD----EEKPQLMVIDSI 179
Cdd:pfam00154 95 V--YAKKLGVDIDNLLVSQPDTGEQALEIADmlvrSGAIDLIVVDSV 139
|
|
| Rad51C |
cd19492 |
RAD51C recombinase; RAD51C recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
100-222 |
6.43e-04 |
|
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: 40.29 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 100 IGGNPGAGKSTLLLQtLC------KLAEGM--KTLYVTGEESLQQVAMRAHRLGLPTANLNMLSEtsieqicQIADEEKP 171
Cdd:cd19492 6 ICGVPGVGKTQLCMQ-LAvnvqipKCFGGLagEAIYIDTEGSFNIHYFRVHDYVELLALINSLPK-------FLEDHPKV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1195217170 172 QLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVT 222
Cdd:cd19492 78 KLIVVDSIAFPFRHDFDDLAQRTRLLNGLAQLLHSLARQHNLAVVLTNQVT 128
|
|
| circ_KaiC |
TIGR02655 |
circadian clock protein KaiC; Members of this family are the circadian clock protein KaiC, ... |
76-182 |
7.56e-04 |
|
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: 41.86 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 76 RFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLL---LQTLCKLAEgmKTLYVTGEESLQQVAMRAHRLGLPTANL- 151
Cdd:TIGR02655 244 RVSSGVVRLDEMCGGGFFKDSIILATGATGTGKTLLVskfLENACANKE--RAILFAYEESRAQLLRNAYSWGIDFEEMe 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1195217170 152 --NML-------SETSIEQICQIADEE----KPQLMVIDSIQVM 182
Cdd:TIGR02655 322 qqGLLkiicaypESAGLEDHLQIIKSEiadfKPARIAIDSLSAL 365
|
|
| KaiC_arch |
cd19486 |
KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284; KaiC ... |
78-137 |
3.28e-03 |
|
KaiC family protein; uncharacterized subfamily similar to Pyrococcus horikoshii PH0284; 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: 410894 Cd Length: 230 Bit Score: 38.99 E-value: 3.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1195217170 78 STGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCK-LAEGMKTLYVTGEESLQQV 137
Cdd:cd19486 2 KTGIPGMDEILHGGIPERNVVLLSGGPGTGKSIFSQQFLWNgLKEGEPGVFVALEEHPVQV 62
|
|
| PLN03186 |
PLN03186 |
DNA repair protein RAD51 homolog; Provisional |
64-232 |
4.89e-03 |
|
DNA repair protein RAD51 homolog; Provisional
Pssm-ID: 178728 [Multi-domain] Cd Length: 342 Bit Score: 38.95 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 64 QKLSDISLealprfSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKsTLLLQTLCKLA---------EGmKTLYVTGE--- 131
Cdd:PLN03186 98 QRQEIIQI------TTGSRELDKILEGGIETGSITEIYGEFRTGK-TQLCHTLCVTCqlpldqgggEG-KAMYIDTEgtf 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195217170 132 --ESLQQVamrAHRLGL-PTANLNML-------SETSIEQICQIAD---EEKPQLMVIDSIQVMHMADVQSSPGSVAQVR 198
Cdd:PLN03186 170 rpQRLIQI---AERFGLnGADVLENVayaraynTDHQSELLLEAASmmaETRFALMIVDSATALYRTEFSGRGELSARQM 246
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1195217170 199 ETAAYL---TRFAKTRGVAIVMVGHVTK--DGS--LAGPKV 232
Cdd:PLN03186 247 HLGKFLrslQRLADEFGVAVVITNQVVAqvDGSafFAGPQL 287
|
|
| Elp4 |
cd19494 |
Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex ... |
73-122 |
6.96e-03 |
|
Elongator subcomplex subunit Elp4; Elongator is a highly conserved multiprotein complex involved in RNA polymerase II-mediated transcriptional elongation and many other processes, including cytoskeleton organization, exocytosis, and tRNA modification. It is composed of two subcomplexes, Elp1-3 and Elp4-6. Elp4-6 forms a heterohexameric RecA-like ring structure, although they lack the key sequence signatures of ATPases.
Pssm-ID: 410902 Cd Length: 259 Bit Score: 38.06 E-value: 6.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1195217170 73 ALPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLqtlcK--LAEG 122
Cdd:cd19494 9 SQLLTSTGIASLDDLLGGGLPLGSLLLIEEDSHSSYAKLLL----KyfLAEG 56
|
|
| |
