|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
3-498 |
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: 714.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 3 LGRAFSVAVRGLDGEIVEIEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSVYD 82
Cdd:COG0606 2 LARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 83 IALAAAVLSAQQKKPWERLENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADNLPEASLVDGIDVRGVRTLG 162
Cdd:COG0606 82 LPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 163 QLQSWLRGSTGLA-GRITTADTTPESAADLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPSLSGS 241
Cdd:COG0606 162 EVVAFLRGEQPLPpAEPDAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 242 ESLEVTAIHSVAGLLSGDTPLITRPPFVAPHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEALRTPL 321
Cdd:COG0606 242 EALEVTAIHSVAGLLPPDGGLIRRRPFRAPHHTASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 322 EDGEIRLARRDGVACYPARFQLVLAANPCPCAPA-DP-QDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGAFS-A 398
Cdd:COG0606 321 EDGEVTISRANGSVTYPARFQLVAAMNPCPCGYLgDPdRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSsA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 399 ADGESTSQVRQRVALAREAAAQRWRPHGFRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAWSLAD 478
Cdd:COG0606 401 PPGESSAEVRERVAAARERQLERFGGTGIRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIAD 480
|
490 500
....*....|....*....|
gi 110826535 479 LAGRTSPGIDEVAAALSFRQ 498
Cdd:COG0606 481 LAGSERIEREHLAEALQYRR 500
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
7-497 |
5.86e-145 |
|
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: 425.03 E-value: 5.86e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 7 FSVAVRGLDGEIVEIEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSVYDIALA 86
Cdd:TIGR00368 2 YSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 87 AAVLSAQQKKPWERLENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADNLPEASLVDGIDVRGVRTLGQLQS 166
Cdd:TIGR00368 82 IGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAEEASLIDGLNIYGADHLKEVVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 167 WLRGSTGLAGRittADTTPESAA--------DLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPSL 238
Cdd:TIGR00368 162 FLEGSEKLPPR---TNTKPKSIInksyiidlDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 239 SGSESLEVTAIHSVAGLLSgDTPLITRPPFVAPHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEALR 318
Cdd:TIGR00368 239 TNEEAIETARIWSLVGKLI-DRKQIKQRPFRSPHHSASKPALVGGGP-IPLPGEISLAHNGVLFLDELPEFKRSVLDALR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 319 TPLEDGEIRLARRDGVACYPARFQLVLAANPCPCA--PADPQDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGAF 396
Cdd:TIGR00368 317 EPIEDGSISISRASAKIFYPARFQLVAAMNPCPCGhyGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 397 -SAADGESTSQVRQRVALAREAAAQRW-RPHGFRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAW 474
Cdd:TIGR00368 397 lSTGSGESSAEVKQRVIKAREIQNIRYeKFANINKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVAR 476
|
490 500
....*....|....*....|...
gi 110826535 475 SLADLAGRTSPGIDEVAAALSFR 497
Cdd:TIGR00368 477 TIADLKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
1-497 |
2.62e-116 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 351.97 E-value: 2.62e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 1 MALGRAFSVAVRGLDGEIVEIEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSV 80
Cdd:PRK09862 1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 81 YDIALAAAVLSAQQKKPWERLENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGwPAVVVPADNLPEASLVDGidvRGVRT 160
Cdd:PRK09862 81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSG-RKIIVAKDNEDEVGLING---EGCLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 161 LGQLQ---SWLRGSTGLAGRITTADTTPESAADLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPS 237
Cdd:PRK09862 157 ADHLQavcAFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 238 LSGSESLEVTAIHSVAGLLSGDTPLITRpPFVAPHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEAL 317
Cdd:PRK09862 237 LSNEEALESAAILSLVNAESVQKQWRQR-PFRSPHHSASLTAMVGGGA-IPGPGEISLAHNGVLFLDELPEFERRTLDAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 318 RTPLEDGEIRLARRDGVACYPARFQLVLAANPCPCAPADPQDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGAFS 397
Cdd:PRK09862 315 REPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 398 --AADGESTSQVRQRVALAREAAAQRWRphgfRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAWS 475
Cdd:PRK09862 395 ktVVPGESSATVKQRVMAARERQFKRQN----KLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVART 470
|
490 500
....*....|....*....|..
gi 110826535 476 LADLAGRTSPGIDEVAAALSFR 497
Cdd:PRK09862 471 IADIDQSDIITRQHLQEAVSYR 492
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
190-395 |
1.24e-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: 334.12 E-value: 1.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 190 DLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPSLSGSESLEVTAIHSVAGLLsGDTPLITRPPFV 269
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLG-GDGGLIRRRPFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 270 APHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDGVACYPARFQLVLAANP 349
Cdd:pfam01078 80 APHHSASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110826535 350 CPCAPAD--PQDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGA 395
Cdd:pfam01078 159 CPCGYLGdpNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEE 206
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
213-388 |
7.14e-08 |
|
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: 51.76 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 213 HLMLTGPPGVGKTMLAQRLPGLLpSLSGSESLEVTAIHSVAGLLsgdtplitrppfvaphhsssVAALVGGGSGMARPGA 292
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIANEL-FRPGAPFLYLNASDLLEGLV--------------------VAELFGHFLVRLLFEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 293 VSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDgvacyparfqlvlaanpcpcapadpqDCICAAATKRRYLG 372
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE--------------------------NVRVIGATNRPLLG 133
|
170
....*....|....*.
gi 110826535 373 KLSGPLLDRVDLRVQM 388
Cdd:cd00009 134 DLDRALYDRLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
212-349 |
1.33e-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: 45.06 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 212 HHLMLTGPPGVGKTMLAQRLPGLLPSLSGSeSLEVTAIHSVAGLLSGDTPLITRPPFvaphHSSSVAALVGGGSGMARpg 291
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGG-VIYIDGEDILEEVLDQLLLIIVGGKK----ASGSGELRLRLALALAR-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 110826535 292 avsRAHRGVLFLDECAEISLSALEALRTPLEDgeirlARRDGVACYPARFQLVLAANP 349
Cdd:smart00382 76 ---KLKPDVLILDEITSLLDAEQEALLLLLEE-----LRLLLLLKSEKNLTVILTTND 125
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
3-498 |
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: 714.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 3 LGRAFSVAVRGLDGEIVEIEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSVYD 82
Cdd:COG0606 2 LARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 83 IALAAAVLSAQQKKPWERLENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADNLPEASLVDGIDVRGVRTLG 162
Cdd:COG0606 82 LPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGIRRLIVPAANAAEAALVPGIEVYGASSLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 163 QLQSWLRGSTGLA-GRITTADTTPESAADLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPSLSGS 241
Cdd:COG0606 162 EVVAFLRGEQPLPpAEPDAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 242 ESLEVTAIHSVAGLLSGDTPLITRPPFVAPHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEALRTPL 321
Cdd:COG0606 242 EALEVTAIHSVAGLLPPDGGLIRRRPFRAPHHTASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 322 EDGEIRLARRDGVACYPARFQLVLAANPCPCAPA-DP-QDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGAFS-A 398
Cdd:COG0606 321 EDGEVTISRANGSVTYPARFQLVAAMNPCPCGYLgDPdRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSsA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 399 ADGESTSQVRQRVALAREAAAQRWRPHGFRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAWSLAD 478
Cdd:COG0606 401 PPGESSAEVRERVAAARERQLERFGGTGIRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIAD 480
|
490 500
....*....|....*....|
gi 110826535 479 LAGRTSPGIDEVAAALSFRQ 498
Cdd:COG0606 481 LAGSERIEREHLAEALQYRR 500
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
7-497 |
5.86e-145 |
|
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: 425.03 E-value: 5.86e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 7 FSVAVRGLDGEIVEIEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSVYDIALA 86
Cdd:TIGR00368 2 YSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 87 AAVLSAQQKKPWERLENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADNLPEASLVDGIDVRGVRTLGQLQS 166
Cdd:TIGR00368 82 IGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKFIIVPKENAEEASLIDGLNIYGADHLKEVVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 167 WLRGSTGLAGRittADTTPESAA--------DLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPSL 238
Cdd:TIGR00368 162 FLEGSEKLPPR---TNTKPKSIInksyiidlDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 239 SGSESLEVTAIHSVAGLLSgDTPLITRPPFVAPHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEALR 318
Cdd:TIGR00368 239 TNEEAIETARIWSLVGKLI-DRKQIKQRPFRSPHHSASKPALVGGGP-IPLPGEISLAHNGVLFLDELPEFKRSVLDALR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 319 TPLEDGEIRLARRDGVACYPARFQLVLAANPCPCA--PADPQDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGAF 396
Cdd:TIGR00368 317 EPIEDGSISISRASAKIFYPARFQLVAAMNPCPCGhyGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 397 -SAADGESTSQVRQRVALAREAAAQRW-RPHGFRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAW 474
Cdd:TIGR00368 397 lSTGSGESSAEVKQRVIKAREIQNIRYeKFANINKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVAR 476
|
490 500
....*....|....*....|...
gi 110826535 475 SLADLAGRTSPGIDEVAAALSFR 497
Cdd:TIGR00368 477 TIADLKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
1-497 |
2.62e-116 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 351.97 E-value: 2.62e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 1 MALGRAFSVAVRGLDGEIVEIEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSV 80
Cdd:PRK09862 1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 81 YDIALAAAVLSAQQKKPWERLENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGwPAVVVPADNLPEASLVDGidvRGVRT 160
Cdd:PRK09862 81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSG-RKIIVAKDNEDEVGLING---EGCLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 161 LGQLQ---SWLRGSTGLAGRITTADTTPESAADLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPS 237
Cdd:PRK09862 157 ADHLQavcAFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 238 LSGSESLEVTAIHSVAGLLSGDTPLITRpPFVAPHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEAL 317
Cdd:PRK09862 237 LSNEEALESAAILSLVNAESVQKQWRQR-PFRSPHHSASLTAMVGGGA-IPGPGEISLAHNGVLFLDELPEFERRTLDAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 318 RTPLEDGEIRLARRDGVACYPARFQLVLAANPCPCAPADPQDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGAFS 397
Cdd:PRK09862 315 REPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 398 --AADGESTSQVRQRVALAREAAAQRWRphgfRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAWS 475
Cdd:PRK09862 395 ktVVPGESSATVKQRVMAARERQFKRQN----KLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVART 470
|
490 500
....*....|....*....|..
gi 110826535 476 LADLAGRTSPGIDEVAAALSFR 497
Cdd:PRK09862 471 IADIDQSDIITRQHLQEAVSYR 492
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
190-395 |
1.24e-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: 334.12 E-value: 1.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 190 DLADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRLPGLLPSLSGSESLEVTAIHSVAGLLsGDTPLITRPPFV 269
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLG-GDGGLIRRRPFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 270 APHHSSSVAALVGGGSgMARPGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDGVACYPARFQLVLAANP 349
Cdd:pfam01078 80 APHHSASAAALVGGGS-IPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110826535 350 CPCAPAD--PQDCICAAATKRRYLGKLSGPLLDRVDLRVQMHRLRAGA 395
Cdd:pfam01078 159 CPCGYLGdpNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEE 206
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
21-143 |
1.01e-46 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 158.38 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 21 IEADITSGLPGVHLVGLPDAALQESRDRVRAAVTNCGNSWPMARLTLALSPATLPKMGSVYDIALAAAVLSAQQKKPWEr 100
Cdd:pfam13541 1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFEFPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQIPVL- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 110826535 101 lENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADN 143
Cdd:pfam13541 80 -EETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| Mg_chelatase_C |
pfam13335 |
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative ... |
401-497 |
2.34e-30 |
|
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: 113.25 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 401 GESTSQVRQRVALAREAAAQRWRphgfRTNAEVSGPLLRRKFRPSSAAMLPLRTALDRGLLSIRGVDRTLRVAWSLADLA 480
Cdd:pfam13335 1 GESSAEVRERVAAARERQAERFG----GENAQLPGRELRRFCRLDAAARALLERALERLGLSARAYDRILRVARTIADLA 76
|
90
....*....|....*..
gi 110826535 481 GRTSPGIDEVAAALSFR 497
Cdd:pfam13335 77 GSERIGREHLAEALQYR 93
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
213-369 |
4.85e-10 |
|
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: 57.69 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 213 HLMLTGPPGVGKTMLAQRLPGLlpsLSGSESLEVtaihsvagLLSGDTpliTRPPFVAPHHsssvaalVGGGSGMARPGA 292
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAA---LSNRPVFYV--------QLTRDT---TEEDLFGRRN-------IDPGGASWVDGP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 293 VSRAHR--GVLFLDECAEISLSALEALRTPLEDGEIRLARRDG-VACYPARFQLVLAANPCPC--APADPqdcicaaATK 367
Cdd:pfam07728 60 LVRAARegEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGElVKAAPDGFRLIATMNPLDRglNELSP-------ALR 132
|
..
gi 110826535 368 RR 369
Cdd:pfam07728 133 SR 134
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
213-388 |
7.14e-08 |
|
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: 51.76 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 213 HLMLTGPPGVGKTMLAQRLPGLLpSLSGSESLEVTAIHSVAGLLsgdtplitrppfvaphhsssVAALVGGGSGMARPGA 292
Cdd:cd00009 21 NLLLYGPPGTGKTTLARAIANEL-FRPGAPFLYLNASDLLEGLV--------------------VAELFGHFLVRLLFEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 293 VSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDgvacyparfqlvlaanpcpcapadpqDCICAAATKRRYLG 372
Cdd:cd00009 80 AEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE--------------------------NVRVIGATNRPLLG 133
|
170
....*....|....*.
gi 110826535 373 KLSGPLLDRVDLRVQM 388
Cdd:cd00009 134 DLDRALYDRLDIRIVI 149
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
16-163 |
1.06e-06 |
|
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: 49.54 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 16 GEIVEIEADITSGLPGVHLVG-LPDAaLQES----RDRVRAAVTNCGNSWPM---ARLTLALSPATLPKMGSVYDIALAA 87
Cdd:pfam05362 40 GDLLTIEAVIMPGKGKLTLTGqLGDV-MKESaqaaLSYVRSRAEELGIDPDFfekKDIHIHVPEGATPKDGPSAGVTMAT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 88 AVLSAQQKKPWERleNTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADN------LPEaSLVDGIDVRGVRTL 161
Cdd:pfam05362 119 ALVSALTGIPVRK--DVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVIIPKENekdledIPE-NVREGLEIIPVEHV 195
|
..
gi 110826535 162 GQ 163
Cdd:pfam05362 196 DE 197
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
194-493 |
2.98e-06 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 49.36 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 194 VVGQSQARFAVEVAAA--GAHHLMLTGPPGVGKTMLAQRLPGLLPslsgseslEVTAI------------------HSVA 253
Cdd:COG1239 11 IVGQEEMKLALLLNAVdpGIGGVLIRGEKGTAKSTAVRALAALLP--------PIEVVkgcpyncdpddpdelcpdCRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 254 GLLSGDTPLITRP-PFVAPHHSSSVAALVGG-------GSGMAR--PGAVSRAHRGVLFLDecaEISLsalealrtpLED 323
Cdd:COG1239 83 LAAGEELPTETRPvPVVELPLGATEDRVVGSldlekalKEGEKAfePGLLARAHRGILYVD---EVNL---------LDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 324 ------------GEIRLaRRDGVA-CYPARFQLVLAANPCPcapadpqdcicaaatkrrylGKLSGPLLDRVDLRVQMHR 390
Cdd:COG1239 151 hlvdvlldaaamGRNTV-EREGVSvSHPARFVLVGTMNPEE--------------------GELRPQLLDRFGLSVEVEG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 391 LR------------------AGAFSAADGESTSQVRQRVALAREAAAQrwrphgfrtnAEVSGPLLRRkfrpssAAmlpl 452
Cdd:COG1239 210 PRdpeerveivrrrlafeadPEAFAAEYAEEQAELRERIAAARELLPE----------VTIPDELLRY------IA---- 269
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 110826535 453 RTALDRGLLSIRGVDRTLRVAWSLADLAGRTSPGIDEVAAA 493
Cdd:COG1239 270 ELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRA 310
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
194-327 |
6.96e-06 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 46.24 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 194 VVGQS----QARFAVEVAAAGAHHLMLTGPPGVGKTMLAQrlpgllpslsgseslevtAIHSVAGLLSGdtplitrpPFV 269
Cdd:pfam00158 1 IIGESpamqEVLEQAKRVAPTDAPVLITGESGTGKELFAR------------------AIHQLSPRADG--------PFV 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110826535 270 AphhsssV--AAL------------VGG---GSGMARPGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIR 327
Cdd:pfam00158 55 A------VncAAIpeelleselfghEKGaftGADSDRKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFE 123
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
212-349 |
1.33e-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: 45.06 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 212 HHLMLTGPPGVGKTMLAQRLPGLLPSLSGSeSLEVTAIHSVAGLLSGDTPLITRPPFvaphHSSSVAALVGGGSGMARpg 291
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGG-VIYIDGEDILEEVLDQLLLIIVGGKK----ASGSGELRLRLALALAR-- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 110826535 292 avsRAHRGVLFLDECAEISLSALEALRTPLEDgeirlARRDGVACYPARFQLVLAANP 349
Cdd:smart00382 76 ---KLKPDVLILDEITSLLDAEQEALLLLLEE-----LRLLLLLKSEKNLTVILTTND 125
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
139-349 |
1.96e-05 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 47.20 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 139 VPADNLPEASLVDGIDVRGVRTLGQLQSWLRGSTGLAGR-ITTADTTPESAADLADVVGQSQA-RFAVEVAAAGAHH--- 213
Cdd:COG3284 267 LDLEALPDGARRAPASPRPLRLRDGRRLGALLRLRPARRaARAAPAGAPAPAALAALAGGDPAmRRALRRARRLADRdip 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 214 LMLTGPPGVGKTMLAQrlpgllpslsgseslevtAIHSVAGLLSGdtplitrpPFVA------PHhSSSVAALVG----- 282
Cdd:COG3284 347 VLILGETGTGKELFAR------------------AIHAASPRADG--------PFVAvncaaiPE-ELIESELFGyepga 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110826535 283 --GGSGMARPGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRlaRRDGVACYPARFQLVLAANP 349
Cdd:COG3284 400 ftGARRKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVT--PLGGTKPIPVDVRLIAATHR 466
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
191-327 |
1.64e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 43.33 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 191 LADVVGQSQARFAVE-----------VAAAG---AHHLMLTGPPGVGKTMLAQRLPGLLpslsgseslevtaihsvagll 256
Cdd:COG1223 1 LDDVVGQEEAKKKLKliikelrrrenLRKFGlwpPRKILFYGPPGTGKTMLAEALAGEL--------------------- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110826535 257 sgDTPLITrppfVAPHhsSSVAALVGGGSGMARpgAV---SRAHRGVLFLDECaeislSALEALRTPLED-GEIR 327
Cdd:COG1223 60 --KLPLLT----VRLD--SLIGSYLGETARNLR--KLfdfARRAPCVIFFDEF-----DAIAKDRGDQNDvGEVK 119
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
213-329 |
1.70e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.56 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 213 HLMLTGPPGVGKTMLAQRLPGLLPSLsGSESLEVTAIH--SVAGLLSGDTPLITRPPfVAPHHSSSVAALVgggsgmaRP 290
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEV-RDSVVFVDLPSgtSPKDLLRALLRALGLPL-SGRLSKEELLAAL-------QQ 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 110826535 291 GAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLA 329
Cdd:pfam13401 78 LLLALAVAVVLIIDEAQHLSLEALEELRDLLNLSSKLLQ 116
|
|
| ruvB |
PRK00080 |
Holliday junction branch migration DNA helicase RuvB; |
191-381 |
4.90e-04 |
|
Holliday junction branch migration DNA helicase RuvB;
Pssm-ID: 234619 [Multi-domain] Cd Length: 328 Bit Score: 42.43 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 191 LADVVGQSQARFAVEVAAAGAH-------HLMLTGPPGVGKTMLAQRLpgllpslsgSESLEVTaIHSVAGllsgdtPLI 263
Cdd:PRK00080 24 LDEFIGQEKVKENLKIFIEAAKkrgealdHVLLYGPPGLGKTTLANII---------ANEMGVN-IRITSG------PAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 264 TRPpfvaphhsSSVAALVgggsgmarpgaVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDGVAcypAR--- 340
Cdd:PRK00080 88 EKP--------GDLAAIL-----------TNLEEGDVLFIDEIHRLSPVVEEILYPAMEDFRLDIMIGKGPA---ARsir 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 110826535 341 -----FQLVlaanpcpcapadpqdcicaAATKRryLGKLSGPLLDR 381
Cdd:PRK00080 146 ldlppFTLI-------------------GATTR--AGLLTSPLRDR 170
|
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
191-381 |
5.68e-04 |
|
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.
Pssm-ID: 398900 [Multi-domain] Cd Length: 159 Bit Score: 40.56 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 191 LADVVGQSQARFAVEVAAAGAH-------HLMLTGPPGVGKTMLAQRLpgllpslsgSESLEVtAIHSVAGllsgdtPLI 263
Cdd:pfam05496 6 LDEYIGQEKVKENLKIFIEAAKqrgealdHVLLYGPPGLGKTTLANII---------ANEMGV-NIRITSG------PAI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 264 TRPpfvaphhsSSVAALVgggsgmarpgaVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDGVACYP----- 338
Cdd:pfam05496 70 ERP--------GDLAAIL-----------TNLEPGDVLFIDEIHRLNRAVEEILYPAMEDFRLDIVIGKGPSARSirldl 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110826535 339 ARFQLVlaanpcpcapadpqdcicaAATKRryLGKLSGPLLDR 381
Cdd:pfam05496 131 PPFTLV-------------------GATTR--AGLLTSPLRDR 152
|
|
| MCM8 |
cd17759 |
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a ... |
210-349 |
7.02e-04 |
|
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a complex with Mcm9 that is required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).
Pssm-ID: 350665 [Multi-domain] Cd Length: 289 Bit Score: 41.75 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 210 GAHHLMLTGPPGVGKTMLAQRLPGLLPS---LSGSeslevtaihsvAGLLSGDTPLITRPPFvaphhsssvaalvgGGSG 286
Cdd:cd17759 42 GDPHVLIVGDPGLGKSQMLQAACNIAPRgvyVCGN-----------TTTTSGLTVTLTKDGR--------------SGDF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110826535 287 MARPGAVSRAHRGVLFLDECAEISlSALEALRTPLEDGEIRLARRDGVACYPARFQLVLAANP 349
Cdd:cd17759 97 ALEAGALVLGDQGICGIDEFDKMG-SQHQALLEAMEQQSVSLAKAGVVCSLPARTSVIAAANP 158
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
213-349 |
1.50e-03 |
|
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: 40.79 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 213 HLMLTGPPGVGKTMLAQRLPGLLPslsgsESLEVTAIHSVAgllSGDTPLITRPPfvaphhsssvaalvGGGSGMARPGA 292
Cdd:cd17706 43 HILLVGDPGTAKSQILKYVLKIAP-----RGVYTSGKGSSG---AGLTAAVVRDS--------------ETGEWYLEAGA 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 110826535 293 VSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDGVACYPARFQLVLAANP 349
Cdd:cd17706 101 LVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANP 157
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
192-237 |
1.70e-03 |
|
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: 40.54 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 192 ADVVGQSQARFAVEVAAAGAHHLMLTGPPGVGKTMLAQRL--------------PGLLPS 237
Cdd:COG0714 12 KVYVGQEELIELVLIALLAGGHLLLEGVPGVGKTTLAKALaralglpfiriqftPDLLPS 71
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
75-166 |
1.73e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 41.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 75 PKMGSVYDIALAAAVLSAQQKKPWErlENTLLLGELSLDGRVRPVRGVLPAVLAAKRDGWPAVVVPADN------LPEAS 148
Cdd:PRK10787 674 PKDGPSAGIAMCTALVSCLTGNPVR--ADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENkrdleeIPDNV 751
|
90
....*....|....*...
gi 110826535 149 LVDgIDVRGVRTLGQLQS 166
Cdd:PRK10787 752 IAD-LDIHPVKRIEEVLT 768
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
191-229 |
1.89e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 40.45 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 110826535 191 LADVVGQSQA-------RFAVEvaAAGAHHLMLTGPPGVGKTMLAQ 229
Cdd:PRK13342 11 LDEVVGQEHLlgpgkplRRMIE--AGRLSSMILWGPPGTGKTTLAR 54
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
188-327 |
4.17e-03 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 39.56 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 188 AADLADVVGQSQA----RFAVEVAAAGAHHLMLTGPPGVGKTMLAQrlpgllpslsgseslevtAIHSVAGLLSGdtpli 263
Cdd:COG2204 127 NAEDSGLIGRSPAmqevRRLIEKVAPSDATVLITGESGTGKELVAR------------------AIHRLSPRADG----- 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110826535 264 trpPFVAPHHSSSVAALVG-----------GGSGMARPGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIR 327
Cdd:COG2204 184 ---PFVAVNCAAIPEELLEselfghekgafTGAVARRIGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFE 255
|
|
| PRK15424 |
PRK15424 |
propionate catabolism operon regulatory protein PrpR; Provisional |
183-326 |
4.79e-03 |
|
propionate catabolism operon regulatory protein PrpR; Provisional
Pssm-ID: 237963 [Multi-domain] Cd Length: 538 Bit Score: 39.32 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 183 TTPESAADLADVVGQS----QARFAVEVAAAGAHHLMLTGPPGVGKTMLAQrlpgllpslsgseslevtAIHSVAGLLSG 258
Cdd:PRK15424 210 NALRTRYVLGDLLGQSpqmeQVRQTILLYARSSAAVLIQGETGTGKELAAQ------------------AIHREYFARHD 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 259 DTPLITRPPFVAPH-----HSSSVAALVGGGSGM-------ARPGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEI 326
Cdd:PRK15424 272 ARQGKKSHPFVAVNcgaiaESLLEAELFGYEEGAftgsrrgGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEV 351
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
191-228 |
5.31e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.13 E-value: 5.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 110826535 191 LADVVGQSQARFAVEV-AAAGAHH-----LMLTGPPGVGKTMLA 228
Cdd:PRK04195 13 LSDVVGNEKAKEQLREwIESWLKGkpkkaLLLYGPPGVGKTSLA 56
|
|
| RuvB |
COG2255 |
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ... |
177-229 |
6.66e-03 |
|
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];
Pssm-ID: 441856 [Multi-domain] Cd Length: 337 Bit Score: 38.52 E-value: 6.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110826535 177 RITTADTTPESAAD-------LADVVGQSQARFAVEVAAAGA-------HHLMLTGPPGVGKTMLAQ 229
Cdd:COG2255 6 RLSSSASEEEDALErslrpkrLDEYIGQEKVKENLKIFIEAAkkrgealDHVLLYGPPGLGKTTLAH 72
|
|
| MCM |
pfam00493 |
MCM P-loop domain; |
213-384 |
7.70e-03 |
|
MCM P-loop domain;
Pssm-ID: 459830 [Multi-domain] Cd Length: 224 Bit Score: 37.89 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 213 HLMLTGPPGVGKTMLAQRLPGLLP---SLSGSESlevtaihSVAGLlsgdTPLITRPPFvaphhsssvaalvgGGSGMAR 289
Cdd:pfam00493 59 NVLLVGDPGTAKSQLLKYVEKIAPravYTSGKGS-------SAAGL----TAAVVRDPV--------------TGEFVLE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 290 PGAVSRAHRGVLFLDECAEISLSALEALRTPLEDGEIRLARRDGVACYPARFQLVLAANPcpcapadpqdcicaaaTKRR 369
Cdd:pfam00493 114 AGALVLADGGVCCIDEFDKMNDEDRVALHEAMEQQTISIAKAGIVATLNARCSILAAANP----------------IFGR 177
|
170 180
....*....|....*....|...
gi 110826535 370 YLGK--------LSGPLLDRVDL 384
Cdd:pfam00493 178 YDPKksiaeninLPPPLLSRFDL 200
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
215-305 |
8.30e-03 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 37.17 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110826535 215 MLTGPPGVGKTMLAQRLPGLL----PSLSGSESLEVTAIHSVAGLLsgdtplitrppfVAPhhsssvAALVGGGSGMARP 290
Cdd:pfam07724 7 LFLGPTGVGKTELAKALAELLfgdeRALIRIDMSEYMEEHSVSRLI------------GAP------PGYVGYEEGGQLT 68
|
90
....*....|....*
gi 110826535 291 GAVSRAHRGVLFLDE 305
Cdd:pfam07724 69 EAVRRKPYSIVLIDE 83
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
191-228 |
9.94e-03 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 37.93 E-value: 9.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110826535 191 LADVVGQSQ--ARFAVEVAAAGAHHLMLTGPPGVGKTMLA 228
Cdd:PRK00440 16 LDEIVGQEEivERLKSYVKEKNMPHLLFAGPPGTGKTTAA 55
|
|
| |
