|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
1-491 |
0e+00 |
|
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: 653.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 1 MEGSMVEVEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAAD 80
Cdd:COG0606 13 IEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFDLPIALGILAAS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 81 GKVPQALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPV 160
Cdd:COG0606 93 GQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLLEVVAFLRGEQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 161 VPPEGPIVGSPDTDPGIgDLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTALHS 240
Cdd:COG0606 173 LPPAEPDAPPAEPPYEP-DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEEEALEVTAIHS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 241 LAGR--GSGRLMTRPPLAQPHHSVSMAAMVGGGvRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRS 318
Cdd:COG0606 252 VAGLlpPDGGLIRRRPFRAPHHTASAAALVGGG-SIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLEDGEVTISRA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 319 QAHTTFPARFQLVMALNPCPCGLADDPSGRCTCTPQQVRRYSGRLSGPILDRVDVTVRMRPLTSAHLLDAsalPAGESSS 398
Cdd:COG0606 331 NGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSA---PPGESSA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 399 AVHERVAQARERAAARWRGVPWRCNAEVPGKVLRQML-PANDATRIIEDALTTGRLTARGVDKVLRIAWTVADLEGKDEV 477
Cdd:COG0606 408 EVRERVAAARERQLERFGGTGIRLNAQLPGRELRKYCrLDAEARALLERALERLGLSARAYDRILRVARTIADLAGSERI 487
|
490
....*....|....
gi 313835016 478 DKACVAEAMGMRRG 491
Cdd:COG0606 488 EREHLAEALQYRRL 501
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
2-489 |
8.48e-142 |
|
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]
Pssm-ID: 129465 [Multi-domain] Cd Length: 499 Bit Score: 416.94 E-value: 8.48e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 2 EGSMVEVEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAADG 81
Cdd:TIGR00368 10 EAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPIAIGILAASE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 82 KVPQALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPVV 161
Cdd:TIGR00368 90 QLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAEEASLIDGLNIYGADHLKEVVKFLEGSEKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 162 PPEGPIVGSPDTD---PGIGDLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTAL 238
Cdd:TIGR00368 170 PPRTNTKPKSIINksyIIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLTNEEAIETARI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 239 HSLAGRGSGRLMTRP-PLAQPHHSVSMAAMVGGGVrIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGR 317
Cdd:TIGR00368 250 WSLVGKLIDRKQIKQrPFRSPHHSASKPALVGGGP-IPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIEDGSISISR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 318 SQAHTTFPARFQLVMALNPCPCGLADDPSGRCTCTPQQVRRYSGRLSGPILDRVDVTVRMRPLTSAHLLDASalpAGESS 397
Cdd:TIGR00368 329 ASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTG---SGESS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 398 SAVHERVAQA-RERAAARWRGVPWRCNAEVPGKVLRQM--LPANDAtRIIEDALTTGRLTARGVDKVLRIAWTVADLEGK 474
Cdd:TIGR00368 406 AEVKQRVIKArEIQNIRYEKFANINKNADLNSDEIEQFckLSAIDA-NDLEGALNKLGLSSRATHRILKVARTIADLKEE 484
|
490
....*....|....*
gi 313835016 475 DEVDKACVAEAMGMR 489
Cdd:TIGR00368 485 KNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
5-489 |
1.32e-114 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 347.35 E-value: 1.32e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 5 MVEVEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAADGKVP 84
Cdd:PRK09862 18 PITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGRYDLPIAIALLAASEQLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 85 QALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGfERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPVV--P 162
Cdd:PRK09862 98 ANKLDEYELVGELALTGALRGVPGAISSATEAIKSG-RKIIVAKDNEDEVGLINGEGCLIADHLQAVCAFLEGKHALerP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 163 PEGPIVGSPDTDpgigDLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTALHSLA 242
Cdd:PRK09862 177 KPTDAVSRALQH----DLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNEEALESAAILSLV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 243 GRGS-GRLMTRPPLAQPHHSVSMAAMVGGGVrIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRSQAH 321
Cdd:PRK09862 253 NAESvQKQWRQRPFRSPHHSASLTAMVGGGA-IPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 322 TTFPARFQLVMALNPCPCGLADDPSGRctCTPQQVRRYSGRLSGPILDRVDVTVRMrPLTSAHLLDASALPaGESSSAVH 401
Cdd:PRK09862 332 ITYPARFQLVAAMNPSPTGHYQGNHNR--CTPEQTLRYLNRLSGPFLDRFDLSLEI-PLPPPGILSKTVVP-GESSATVK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 402 ERVAQARERAAARWRgvpwRCNAEVPGKVLRQM--LPANDAtRIIEDALTTGRLTARGVDKVLRIAWTVADLEGKDEVDK 479
Cdd:PRK09862 408 QRVMAARERQFKRQN----KLNAWLDSPEIRQFckLESEDA-RWLEETLIHLGLSIRAWQRLLKVARTIADIDQSDIITR 482
|
490
....*....|
gi 313835016 480 ACVAEAMGMR 489
Cdd:PRK09862 483 QHLQEAVSYR 492
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
179-385 |
1.40e-113 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 333.73 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 179 DLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTALHSLAGRG-SGRLMTRPPLAQ 257
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLGgDGGLIRRRPFRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 258 PHHSVSMAAMVGGGvRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRSQAHTTFPARFQLVMALNPC 337
Cdd:pfam01078 81 PHHSASAAALVGGG-SIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPC 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 313835016 338 PCGLADDPSGRCTCTPQQVRRYSGRLSGPILDRVDVTVRMRPLTSAHL 385
Cdd:pfam01078 160 PCGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
184-379 |
8.19e-07 |
|
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: 48.68 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 184 IGQHEARRALEVAAAGRH--HILLRGAPGCGKSMLARRLPGILPRLDHRdALEVTAlHSLAGRGSGRLmtrpplaqphhs 261
Cdd:cd00009 1 VGQEEAIEALREALELPPpkNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNA-SDLLEGLVVAE------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 262 vsmaaMVGGGVRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIvigrsqaHTTFPARFQLVMALNpcpcgl 341
Cdd:cd00009 67 -----LFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLND-------LRIDRENVRVIGATN------ 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 313835016 342 addpsgrctctpqqvRRYSGRLSGPILDRVDVTVRMRP 379
Cdd:cd00009 129 ---------------RPLLGDLDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
200-305 |
7.25e-05 |
|
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: 43.13 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 200 RHHILLRGAPGCGKSMLARRLPGILPRlDHRDALEVTAlhslagrgsGRLMTRPPLAQPHHSVSMAAMVGGGVRIAQpGA 279
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGP-PGGGVIYIDG---------EDILEEVLDQLLLIIVGGKKASGSGELRLR-LA 70
|
90 100
....*....|....*....|....*....
gi 313835016 280 ISLAHR---GVLFLDEAPEFAPKVLDSLR 305
Cdd:smart00382 71 LALARKlkpDVLILDEITSLLDAEQEALL 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
1-491 |
0e+00 |
|
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: 653.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 1 MEGSMVEVEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAAD 80
Cdd:COG0606 13 IEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFDLPIALGILAAS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 81 GKVPQALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPV 160
Cdd:COG0606 93 GQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLLEVVAFLRGEQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 161 VPPEGPIVGSPDTDPGIgDLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTALHS 240
Cdd:COG0606 173 LPPAEPDAPPAEPPYEP-DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEEEALEVTAIHS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 241 LAGR--GSGRLMTRPPLAQPHHSVSMAAMVGGGvRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRS 318
Cdd:COG0606 252 VAGLlpPDGGLIRRRPFRAPHHTASAAALVGGG-SIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLEDGEVTISRA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 319 QAHTTFPARFQLVMALNPCPCGLADDPSGRCTCTPQQVRRYSGRLSGPILDRVDVTVRMRPLTSAHLLDAsalPAGESSS 398
Cdd:COG0606 331 NGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSA---PPGESSA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 399 AVHERVAQARERAAARWRGVPWRCNAEVPGKVLRQML-PANDATRIIEDALTTGRLTARGVDKVLRIAWTVADLEGKDEV 477
Cdd:COG0606 408 EVRERVAAARERQLERFGGTGIRLNAQLPGRELRKYCrLDAEARALLERALERLGLSARAYDRILRVARTIADLAGSERI 487
|
490
....*....|....
gi 313835016 478 DKACVAEAMGMRRG 491
Cdd:COG0606 488 EREHLAEALQYRRL 501
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
2-489 |
8.48e-142 |
|
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]
Pssm-ID: 129465 [Multi-domain] Cd Length: 499 Bit Score: 416.94 E-value: 8.48e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 2 EGSMVEVEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAADG 81
Cdd:TIGR00368 10 EAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPIAIGILAASE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 82 KVPQALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPVV 161
Cdd:TIGR00368 90 QLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAEEASLIDGLNIYGADHLKEVVKFLEGSEKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 162 PPEGPIVGSPDTD---PGIGDLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTAL 238
Cdd:TIGR00368 170 PPRTNTKPKSIINksyIIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLTNEEAIETARI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 239 HSLAGRGSGRLMTRP-PLAQPHHSVSMAAMVGGGVrIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGR 317
Cdd:TIGR00368 250 WSLVGKLIDRKQIKQrPFRSPHHSASKPALVGGGP-IPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIEDGSISISR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 318 SQAHTTFPARFQLVMALNPCPCGLADDPSGRCTCTPQQVRRYSGRLSGPILDRVDVTVRMRPLTSAHLLDASalpAGESS 397
Cdd:TIGR00368 329 ASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTG---SGESS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 398 SAVHERVAQA-RERAAARWRGVPWRCNAEVPGKVLRQM--LPANDAtRIIEDALTTGRLTARGVDKVLRIAWTVADLEGK 474
Cdd:TIGR00368 406 AEVKQRVIKArEIQNIRYEKFANINKNADLNSDEIEQFckLSAIDA-NDLEGALNKLGLSSRATHRILKVARTIADLKEE 484
|
490
....*....|....*
gi 313835016 475 DEVDKACVAEAMGMR 489
Cdd:TIGR00368 485 KNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
5-489 |
1.32e-114 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 347.35 E-value: 1.32e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 5 MVEVEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAADGKVP 84
Cdd:PRK09862 18 PITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGRYDLPIAIALLAASEQLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 85 QALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGfERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPVV--P 162
Cdd:PRK09862 98 ANKLDEYELVGELALTGALRGVPGAISSATEAIKSG-RKIIVAKDNEDEVGLINGEGCLIADHLQAVCAFLEGKHALerP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 163 PEGPIVGSPDTDpgigDLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTALHSLA 242
Cdd:PRK09862 177 KPTDAVSRALQH----DLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNEEALESAAILSLV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 243 GRGS-GRLMTRPPLAQPHHSVSMAAMVGGGVrIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRSQAH 321
Cdd:PRK09862 253 NAESvQKQWRQRPFRSPHHSASLTAMVGGGA-IPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 322 TTFPARFQLVMALNPCPCGLADDPSGRctCTPQQVRRYSGRLSGPILDRVDVTVRMrPLTSAHLLDASALPaGESSSAVH 401
Cdd:PRK09862 332 ITYPARFQLVAAMNPSPTGHYQGNHNR--CTPEQTLRYLNRLSGPFLDRFDLSLEI-PLPPPGILSKTVVP-GESSATVK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 402 ERVAQARERAAARWRgvpwRCNAEVPGKVLRQM--LPANDAtRIIEDALTTGRLTARGVDKVLRIAWTVADLEGKDEVDK 479
Cdd:PRK09862 408 QRVMAARERQFKRQN----KLNAWLDSPEIRQFckLESEDA-RWLEETLIHLGLSIRAWQRLLKVARTIADIDQSDIITR 482
|
490
....*....|
gi 313835016 480 ACVAEAMGMR 489
Cdd:PRK09862 483 QHLQEAVSYR 492
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
179-385 |
1.40e-113 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 333.73 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 179 DLTEVIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRLPGILPRLDHRDALEVTALHSLAGRG-SGRLMTRPPLAQ 257
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLGgDGGLIRRRPFRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 258 PHHSVSMAAMVGGGvRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRSQAHTTFPARFQLVMALNPC 337
Cdd:pfam01078 81 PHHSASAAALVGGG-SIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPC 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 313835016 338 PCGLADDPSGRCTCTPQQVRRYSGRLSGPILDRVDVTVRMRPLTSAHL 385
Cdd:pfam01078 160 PCGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
8-129 |
3.77e-36 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 129.88 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 8 VEAAISSGLPRTVLVGLPDAALHEARDRCRAAVCATGLSWPSNVLTINLTPAGLPKAGTHFDLAIAAATLAADGKVPQal 87
Cdd:pfam13541 1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFEFPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQIPV-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 313835016 88 LGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPAS 129
Cdd:pfam13541 79 LEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKE 120
|
|
| Mg_chelatase_C |
pfam13335 |
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative ... |
423-489 |
8.65e-19 |
|
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative bacterial magnesium chelatase subunit ChlI proteins. Most members have the associated pfam01078.
Pssm-ID: 433125 Cd Length: 93 Bit Score: 80.90 E-value: 8.65e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313835016 423 NAEVPGKVLRQMLPAND-ATRIIEDALTTGRLTARGVDKVLRIAWTVADLEGKDEVDKACVAEAMGMR 489
Cdd:pfam13335 26 NAQLPGRELRRFCRLDAaARALLERALERLGLSARAYDRILRVARTIADLAGSERIGREHLAEALQYR 93
|
|
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
85-155 |
8.02e-09 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 57.75 E-value: 8.02e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313835016 85 QALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDEASlVEGLMIWPVGHLGDVVDVL 155
Cdd:COG1066 383 RPLPPDTVFFGEVGLTGEIRPVSRIEQRLKEAAKLGFKRAIVPKGNKKKLK-PKGIEIIGVSTLEEALEAL 452
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
202-343 |
6.93e-07 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 48.44 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 202 HILLRGAPGCGKSMLARRLPGILPrldhRDALEVTALHslagrgsgRLMTRPPLAQPHH-SVSMAAMVGGG-VRIAQPGA 279
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALS----NRPVFYVQLT--------RDTTEEDLFGRRNiDPGGASWVDGPlVRAAREGE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313835016 280 IslahrgvLFLDEAPEFAPKVLDSLRGPLETGEIVI----GRSQAhttFPARFQLVMALNPCPCGLAD 343
Cdd:pfam07728 69 I-------AVLDEINRANPDVLNSLLSLLDERRLLLpdggELVKA---APDGFRLIATMNPLDRGLNE 126
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
184-379 |
8.19e-07 |
|
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: 48.68 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 184 IGQHEARRALEVAAAGRH--HILLRGAPGCGKSMLARRLPGILPRLDHRdALEVTAlHSLAGRGSGRLmtrpplaqphhs 261
Cdd:cd00009 1 VGQEEAIEALREALELPPpkNLLLYGPPGTGKTTLARAIANELFRPGAP-FLYLNA-SDLLEGLVVAE------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 262 vsmaaMVGGGVRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIvigrsqaHTTFPARFQLVMALNpcpcgl 341
Cdd:cd00009 67 -----LFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLND-------LRIDRENVRVIGATN------ 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 313835016 342 addpsgrctctpqqvRRYSGRLSGPILDRVDVTVRMRP 379
Cdd:cd00009 129 ---------------RPLLGDLDRALYDRLDIRIVIPL 151
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
180-336 |
2.02e-06 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 49.75 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 180 LTEVIGQHEARRALEVAAA----GrhHILLRGAPGCGKSMLARRLPGILPRL------------DHRDALEVTALHSLAG 243
Cdd:COG1239 8 FTAIVGQEEMKLALLLNAVdpgiG--GVLIRGEKGTAKSTAVRALAALLPPIevvkgcpyncdpDDPDELCPDCRERLAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 244 RGSGRLMTRP-PLAQ-PHH--------SVSMAAMVGGGVRIAQPGAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEI 313
Cdd:COG1239 86 GEELPTETRPvPVVElPLGatedrvvgSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRN 165
|
170 180
....*....|....*....|....*.
gi 313835016 314 VIGR---SQAHttfPARFQLVMALNP 336
Cdd:COG1239 166 TVERegvSVSH---PARFVLVGTMNP 188
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
180-249 |
7.67e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 47.19 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 180 LTEVIGQHEARRALE-----------VAAAG---RHHILLRGAPGCGKSMLAR------RLPGILPRLDhrdalevTALH 239
Cdd:COG1223 1 LDDVVGQEEAKKKLKliikelrrrenLRKFGlwpPRKILFYGPPGTGKTMLAEalagelKLPLLTVRLD-------SLIG 73
|
90
....*....|
gi 313835016 240 SLAGRGSGRL 249
Cdd:COG1223 74 SYLGETARNL 83
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
183-292 |
2.82e-05 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 44.31 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 183 VIGQ----HEARRALEVAAAGRHHILLRGAPGCGKSMLARrlpgilprldhrdalevtALHSLAGRGSGRLMtrpplaqp 258
Cdd:pfam00158 1 IIGEspamQEVLEQAKRVAPTDAPVLITGESGTGKELFAR------------------AIHQLSPRADGPFV-------- 54
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 313835016 259 hhSVSMAAM------------VGG---GVRIAQPGAISLAHRGVLFLDE 292
Cdd:pfam00158 55 --AVNCAAIpeelleselfghEKGaftGADSDRKGLFELADGGTLFLDE 101
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
199-336 |
2.96e-05 |
|
MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).
Pssm-ID: 350658 [Multi-domain] Cd Length: 311 Bit Score: 45.80 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 199 GRHHILLRGAPGCGKSMLARRLPGILPRldhrdALEVTALHSLAGRGSGRLMTRPplaqphhsvsmaamvGGGVRIAQPG 278
Cdd:cd17706 40 GDIHILLVGDPGTAKSQILKYVLKIAPR-----GVYTSGKGSSGAGLTAAVVRDS---------------ETGEWYLEAG 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 313835016 279 AISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRSQAHTTFPARFQLVMALNP 336
Cdd:cd17706 100 ALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANP 157
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
200-305 |
7.25e-05 |
|
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: 43.13 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 200 RHHILLRGAPGCGKSMLARRLPGILPRlDHRDALEVTAlhslagrgsGRLMTRPPLAQPHHSVSMAAMVGGGVRIAQpGA 279
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGP-PGGGVIYIDG---------EDILEEVLDQLLLIIVGGKKASGSGELRLR-LA 70
|
90 100
....*....|....*....|....*....
gi 313835016 280 ISLAHR---GVLFLDEAPEFAPKVLDSLR 305
Cdd:smart00382 71 LALARKlkpDVLILDEITSLLDAEQEALL 99
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
160-336 |
2.03e-04 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 43.74 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 160 VVPPEGPIVGSPDTDPGIGDLTEVIGQHEA-RRALEVA---AAGRHHILLRGAPGCGKSMLARrlpgilprldhrdalev 235
Cdd:COG3284 300 LRPARRAARAAPAGAPAPAALAALAGGDPAmRRALRRArrlADRDIPVLILGETGTGKELFAR----------------- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 236 tALHSLAGRGSGrlmtrpplaqPHHSVSMAAM----------------VGGGVRIAQPGAISLAHRGVLFLDEAPEFAPK 299
Cdd:COG3284 363 -AIHAASPRADG----------PFVAVNCAAIpeelieselfgyepgaFTGARRKGRPGKIEQADGGTLFLDEIGDMPLA 431
|
170 180 190
....*....|....*....|....*....|....*..
gi 313835016 300 VLDSLRGPLETGEIVigRSQAHTTFPARFQLVMALNP 336
Cdd:COG3284 432 LQARLLRVLQEREVT--PLGGTKPIPVDVRLIAATHR 466
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
183-220 |
2.31e-04 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 43.23 E-value: 2.31e-04
10 20 30
....*....|....*....|....*....|....*...
gi 313835016 183 VIGQHEARRALEVAAAGRHHILLRGAPGCGKSMLARRL 220
Cdd:COG0714 14 YVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKAL 51
|
|
| MCM3 |
cd17754 |
DNA replication licensing factor Mcm3; Mcm3 is a helicase that play an important role in ... |
202-336 |
1.71e-03 |
|
DNA replication licensing factor Mcm3; Mcm3 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases.
Pssm-ID: 350660 [Multi-domain] Cd Length: 299 Bit Score: 40.53 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 202 HILLRGAPGCGKSMLARRLPGILPRldhrdALEVTalhslaGRGSGrlmtrpplaqphhSVSMAAMVGG----GVRIAQP 277
Cdd:cd17754 43 NILLVGDPSVAKSQLLRYVLNTAPL-----AIATT------GRGSS-------------GVGLTAAVTTdqetGERRLEA 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 313835016 278 GAISLAHRGVLFLDEAPEFAPKVLDSLRGPLETGEIVIGRSQAHTTFPARFQLVMALNP 336
Cdd:cd17754 99 GAMVLADRGVVCIDEFDKMSDIDRVAIHEVMEQQTVTIAKAGIHASLNARCSVLAAANP 157
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
95-155 |
1.85e-03 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 39.53 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313835016 95 GELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDE-----ASLVEGLMIWPVGHLGDVVDVL 155
Cdd:pfam05362 137 GEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENEKDledipENVREGLEIIPVEHVDEVLKHA 202
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
83-224 |
7.26e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 38.74 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313835016 83 VPQALLGSTVLIGELGLDGRVRPVRGVLPALLAAREAGFERAVVPASQSDEASLVEGLMIWPVGHLGDVVDVLHGRPVVP 162
Cdd:COG0464 60 LLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYE 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313835016 163 PEGPIVGSPDTDPGIgDLTEVIGQHEARRALEVAAAG---------------RHHILLRGAPGCGKSMLARRLPGIL 224
Cdd:COG0464 140 DIGGLEEELLELREA-ILDDLGGLEEVKEELRELVALplkrpelreeyglppPRGLLLYGPPGTGKTLLARALAGEL 215
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
182-220 |
8.60e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 38.25 E-value: 8.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 313835016 182 EVIGQHEARRALEVA-AAGR-HH-ILLRGAPGCGKSMLARRL 220
Cdd:COG2812 11 DVVGQEHVVRTLKNAlASGRlAHaYLFTGPRGVGKTTLARIL 52
|
|
| |
