|
Name |
Accession |
Description |
Interval |
E-value |
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
17-336 |
0e+00 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 530.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 17 TRPVFPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVS-SPN--VEMIPD--- 90
Cdd:COG1239 2 MRTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNcDPDdpDELCPDcre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 91 -WATVLSTNVIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQ 169
Cdd:COG1239 82 rLAAGEELPTETRPVPVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 170 SGENVVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPKD 249
Cdd:COG1239 162 MGRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 250 MDIRNQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRR 329
Cdd:COG1239 242 AELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLRR 321
|
....*..
1G8P_A 330 DPLDEAG 336
Cdd:COG1239 322 DPFEEPG 328
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
21-350 |
0e+00 |
|
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria and other photosynthetic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 131085 [Multi-domain] Cd Length: 337 Bit Score: 505.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 21 FPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVS---SPNVEMIPDWATVLST 97
Cdd:TIGR02030 1 FPFTAIVGQDEMKLALLLNVIDPKIGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNsspSDPEMMCEEVRIRVDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 98 N----VIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGEN 173
Cdd:TIGR02030 81 QeplsIIKKPVPVVDLPLGATEDRVCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 174 VVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPKDMDIR 253
Cdd:TIGR02030 161 VVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 254 NQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDPLD 333
Cdd:TIGR02030 241 AKIVNAQNLLPQVTIPYDVLVKVAELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIRRVAVLALRHRLRKDPLE 320
|
330
....*....|....*..
1G8P_A 334 EAGSTARVARTVEETLP 350
Cdd:TIGR02030 321 SIDSGSRVERVVKEVLG 337
|
|
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
16-348 |
2.10e-148 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 422.09 E-value: 2.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 16 KTRPVFPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVSS--PNVEMIPDWAT 93
Cdd:CHL00081 9 KERPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNShpSDPELMSDEVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 94 VLSTN-----VIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVA 168
Cdd:CHL00081 89 EAIQNgetieTEKIKIPMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 169 QSGENVVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPK 248
Cdd:CHL00081 169 ASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEES 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 249 DMDIRNQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLR 328
Cdd:CHL00081 249 QEELRSKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRLR 328
|
330 340
....*....|....*....|
1G8P_A 329 RDPLDEAGSTARVARTVEET 348
Cdd:CHL00081 329 KDPLESIDSGDKVQKVFKEV 348
|
|
| AAA_lid_2 |
pfam17863 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
277-345 |
1.61e-16 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465538 [Multi-domain] Cd Length: 73 Bit Score: 73.40 E-value: 1.61e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1G8P_A 277 AALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDPLDEAGSTARVARTV 345
Cdd:pfam17863 5 AHLAIALGVSPRRADLALLRAARALAALEGRDYVTPEDVKEAAPLVLAHRLRREPEAEGETAEEILEEI 73
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
27-215 |
5.30e-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: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 27 VGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEavegcpvsspnvemipdwATVLSTNVirkptpv 106
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPG------------------APFLYLNA------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 107 vdlplgvseDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGENvverdgLSIRHPA 186
Cdd:cd00009 56 ---------SDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLND------LRIDREN 120
|
170 180
....*....|....*....|....*....
1G8P_A 187 RFVLVGSGNPEEGDLRPQLLDRFGLSVEV 215
Cdd:cd00009 121 VRVIGATNRPLLGDLDRALYDRLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-219 |
3.77e-03 |
|
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: 37.35 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 46 GGVLVFGDRGTGKSTAVRALAALLPeieavegcpvsspnvemiPDWATVLSTNVIRKPTPVVDLPLGVSEDRVVGALDIE 125
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELG------------------PPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 126 RAIskgEKAFEpgLLARANRGYLYIDECNLLEDHIVDLLLDVAQsgenvVERDGLSIRHPARFVLVGSGNPEEGDLRPQL 205
Cdd:smart00382 65 LRL---RLALA--LARKLKPDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
170
....*....|....
1G8P_A 206 LDRFGLSVEVLSPR 219
Cdd:smart00382 135 RRRFDRRIVLLLIL 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
17-336 |
0e+00 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 530.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 17 TRPVFPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVS-SPN--VEMIPD--- 90
Cdd:COG1239 2 MRTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNcDPDdpDELCPDcre 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 91 -WATVLSTNVIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQ 169
Cdd:COG1239 82 rLAAGEELPTETRPVPVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 170 SGENVVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPKD 249
Cdd:COG1239 162 MGRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 250 MDIRNQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRR 329
Cdd:COG1239 242 AELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLRR 321
|
....*..
1G8P_A 330 DPLDEAG 336
Cdd:COG1239 322 DPFEEPG 328
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
21-350 |
0e+00 |
|
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria and other photosynthetic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 131085 [Multi-domain] Cd Length: 337 Bit Score: 505.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 21 FPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVS---SPNVEMIPDWATVLST 97
Cdd:TIGR02030 1 FPFTAIVGQDEMKLALLLNVIDPKIGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNsspSDPEMMCEEVRIRVDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 98 N----VIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGEN 173
Cdd:TIGR02030 81 QeplsIIKKPVPVVDLPLGATEDRVCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 174 VVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPKDMDIR 253
Cdd:TIGR02030 161 VVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 254 NQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDPLD 333
Cdd:TIGR02030 241 AKIVNAQNLLPQVTIPYDVLVKVAELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIRRVAVLALRHRLRKDPLE 320
|
330
....*....|....*..
1G8P_A 334 EAGSTARVARTVEETLP 350
Cdd:TIGR02030 321 SIDSGSRVERVVKEVLG 337
|
|
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
16-348 |
2.10e-148 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 422.09 E-value: 2.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 16 KTRPVFPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVSS--PNVEMIPDWAT 93
Cdd:CHL00081 9 KERPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNShpSDPELMSDEVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 94 VLSTN-----VIRKPTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVA 168
Cdd:CHL00081 89 EAIQNgetieTEKIKIPMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 169 QSGENVVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPK 248
Cdd:CHL00081 169 ASGWNTVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEES 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 249 DMDIRNQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLR 328
Cdd:CHL00081 249 QEELRSKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRLR 328
|
330 340
....*....|....*....|
1G8P_A 329 RDPLDEAGSTARVARTVEET 348
Cdd:CHL00081 329 KDPLESIDSGDKVQKVFKEV 348
|
|
| Cob-chelat-sub |
TIGR02442 |
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ... |
21-337 |
1.47e-137 |
|
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the corrin ring of coenzyme B12 during its biosynthesis. Two versions have been well described. CbiK/CbiX is a monomeric, anaerobic version which acts early in the biosynthesis (pfam06180). CobNST is a trimeric, ATP-dependent, aerobic version which acts late in the biosynthesis (TIGR02257/TIGR01650/TIGR01651). A number of genomes (actinobacteria, cyanobacteria, betaproteobacteria and pseudomonads) which apparently biosynthesize B12, encode a cobN gene but are demonstrably lacking cobS and cobT. These genomes do, however contain a homolog (modelled here) of the magnesium chelatase subunits BchI/BchD family. Aside from the cyanobacteria (which have a separate magnesium chelatase trimer), these species do not make chlorins, so do not have any use for a magnesium chelatase. Furthermore, in nearly all cases the members of this family are proximal to either CobN itself or other genes involved in cobalt transport or B12 biosynthesis.
Pssm-ID: 274135 [Multi-domain] Cd Length: 633 Bit Score: 404.84 E-value: 1.47e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 21 FPFSAIVGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEAVEGCPVSSPnvemiPDWATVLSTNVI 100
Cdd:TIGR02442 1 FPFTAIVGQEDLKLALLLNAVDPRIGGVLIRGEKGTAKSTAARGLAALLPPIDVVAGCPFSCD-----PDDPEEWCEECR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 101 RK-------PTPVVDLPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGEN 173
Cdd:TIGR02442 76 RKyrpseqrPVPFVNLPLGATEDRVVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 174 VVERDGLSIRHPARFVLVGSGNPEEGDLRPQLLDRFGLSVEVLSPRDVETRVEVIRRRDTYDADPKAFLEEWRPKDMDIR 253
Cdd:TIGR02442 156 RVEREGLSVSHPARFVLIGTMNPEEGDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 254 NQILEARERLPKVEAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDPLD 333
Cdd:TIGR02442 236 NRIARARSLLPSVRISDSLIRFISELCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVREAAELVLPHRRRRKPFE 315
|
....
1G8P_A 334 EAGS 337
Cdd:TIGR02442 316 QPQG 319
|
|
| bchD |
PRK13406 |
magnesium chelatase subunit D; Provisional |
30-331 |
6.08e-26 |
|
magnesium chelatase subunit D; Provisional
Pssm-ID: 237378 [Multi-domain] Cd Length: 584 Bit Score: 108.57 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 30 EDMKLALLLTAVDP-GIGGVLVFGDRGTGKSTAVRALAALLPEieavegcpvsspnvemipdwatvlstnvirkPTPVVD 108
Cdd:PRK13406 9 ADAALAAALLAVDPaGLGGVVLRARAGPVRDRWLAALRALLPA-------------------------------GTPLRR 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 109 LPLGVSEDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGENVVERDGLSIRHPARF 188
Cdd:PRK13406 58 LPPGIADDRLLGGLDLAATLRAGRPVAQRGLLAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRLPARF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 189 VLVG--SGNPEEGDLRPQLLDRFGLSVEVlsprdvetrvEVIRRRDTYDADPKAfleewrpkdmdirNQILEARERLPKV 266
Cdd:PRK13406 138 GLVAldEGAEEDERAPAALADRLAFHLDL----------DGLALRDAREIPIDA-------------DDIAAARARLPAV 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
1G8P_A 267 EAPNTALYDCAALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDP 331
Cdd:PRK13406 195 GPPPEAIAALCAAAAALGIASLRAPLLALRAARAAAALAGRTAVEEEDLALAARLVLAPRATRLP 259
|
|
| AAA_lid_2 |
pfam17863 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
277-345 |
1.61e-16 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465538 [Multi-domain] Cd Length: 73 Bit Score: 73.40 E-value: 1.61e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1G8P_A 277 AALCIALGSDGLRGELTLLRSARALAALEGATAVGRDHLKRVATMALSHRLRRDPLDEAGSTARVARTV 345
Cdd:pfam17863 5 AHLAIALGVSPRRADLALLRAARALAALEGRDYVTPEDVKEAAPLVLAHRLRREPEAEGETAEEILEEI 73
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
23-326 |
4.95e-12 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 66.93 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 23 FSAIVGQEDMKLALLLTAVdpGIGGVLVFGDRGTGKSTAVRALAALLPEI---EAVEGCPVSSpnvemipdWATVLSTNV 99
Cdd:PRK09862 190 LSDVIGQEQGKRGLEITAA--GGHNLLLIGPPGTGKTMLASRINGLLPDLsneEALESAAILS--------LVNAESVQK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 100 IRKPTPVVDLPLGVSEDRVVGALDIEraiskgekafEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGENVVERDG 179
Cdd:PRK09862 260 QWRQRPFRSPHHSASLTAMVGGGAIP----------GPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 180 LSIRHPARFVLVGSGNPEE--------------------GDLRPQLLDRFGLSVE-------VLSPRDVETRVEVIRRRD 232
Cdd:PRK09862 330 AKITYPARFQLVAAMNPSPtghyqgnhnrctpeqtlrylNRLSGPFLDRFDLSLEiplpppgILSKTVVPGESSATVKQR 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 233 TYDADPKAFLeewRPKDMDIRNQILEARERLpKVEAPNTALYDCAALCIALgsdGLRGELTLLRSARALAALEGATAVGR 312
Cdd:PRK09862 410 VMAARERQFK---RQNKLNAWLDSPEIRQFC-KLESEDARWLEETLIHLGL---SIRAWQRLLKVARTIADIDQSDIITR 482
|
330
....*....|....
1G8P_A 313 DHLKRvatmALSHR 326
Cdd:PRK09862 483 QHLQE----AVSYR 492
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
24-335 |
1.48e-08 |
|
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: 55.17 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 24 SAIVGQEDMKLALLLTAVdpgIGG-VLVFGDRGTGKSTAVRALAALLpeieaveGCPVSSpnVEMIPDW--ATVLSTNVI 100
Cdd:COG0714 12 KVYVGQEELIELVLIALL---AGGhLLLEGVPGVGKTTLAKALARAL-------GLPFIR--IQFTPDLlpSDILGTYIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 101 RKptpvvdlplgvsedrvvgaldieraiSKGEKAFEPG-LLAranrGYLYIDECN---------LLEdhivdlLLDvaqs 170
Cdd:COG0714 80 DQ--------------------------QTGEFEFRPGpLFA----NVLLADEINrappktqsaLLE------AME---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 171 gENVVERDGLSIRHPARFVLVGSGNPEEG----DLRPQLLDRFGLSVEVLSPrDVETRVEVIRRRDTYDAD---PKAFLE 243
Cdd:COG0714 120 -ERQVTIPGGTYKLPEPFLVIATQNPIEQegtyPLPEAQLDRFLLKLYIGYP-DAEEEREILRRHTGRHLAevePVLSPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 244 EwrpkdmdirnqILEARERLPKVEAPNTALYDCAALC--------IALGSdGLRGELTLLRSARALAALEGATAVGRDHL 315
Cdd:COG0714 198 E-----------LLALQELVRQVHVSEAVLDYIVDLVratrehpdLRKGP-SPRASIALLRAARALALLDGRDYVTPDDV 265
|
330 340
....*....|....*....|
1G8P_A 316 KRVATMALSHRLRRDPLDEA 335
Cdd:COG0714 266 KAVAGPVLKHRLILSPEADA 285
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
23-196 |
9.24e-08 |
|
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: 51.77 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 23 FSAIVGQEDMKLALLLTAvdpgIGG--VLVFGDRGTGKSTAVRALAALLPEI---EAVEGCPVSSPNVEMipdwatvLST 97
Cdd:pfam01078 2 LADVKGQEQAKRALEIAA----AGGhnLLMIGPPGSGKTMLAKRLPGILPPLteaEALEVTAIHSVAGLG-------GDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 98 NVIRKPtPVVDLPLGVSEDRVVGAldieraiskGEKAFePGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGENVVER 177
Cdd:pfam01078 71 GLIRRR-PFRAPHHSASAAALVGG---------GSIPR-PGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISR 139
|
170
....*....|....*....
1G8P_A 178 DGLSIRHPARFVLVGSGNP 196
Cdd:pfam01078 140 ARAKVTFPARFQLVAAMNP 158
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
27-215 |
5.30e-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: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 27 VGQEDMKLALLLTAVDPGIGGVLVFGDRGTGKSTAVRALAALLPEIEavegcpvsspnvemipdwATVLSTNVirkptpv 106
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPG------------------APFLYLNA------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 107 vdlplgvseDRVVGALDIERAISKGEKAFEPGLLARANRGYLYIDECNLLEDHIVDLLLDVAQSGENvverdgLSIRHPA 186
Cdd:cd00009 56 ---------SDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLND------LRIDREN 120
|
170 180
....*....|....*....|....*....
1G8P_A 187 RFVLVGSGNPEEGDLRPQLLDRFGLSVEV 215
Cdd:cd00009 121 VRVIGATNRPLLGDLDRALYDRLDIRIVI 149
|
|
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
2-328 |
3.56e-03 |
|
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: 39.25 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 2 TTAVARLQPSASGAKTRPVFPFSAIVGQEDMKLALLLTAVdpgiGG--VLVFGDRGTGKSTAVRALAALLPEI---EAVE 76
Cdd:COG0606 170 EQPLPPAEPDAPPAEPPYEPDLADVKGQEQAKRALEIAAA----GGhnLLMIGPPGSGKTMLARRLPGILPPLteeEALE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 77 gcpVSSpnvemipdwatVLStnvirkptpvvdlplgvsedrVVGALDIERAISKgEKAFE-------------------P 137
Cdd:COG0606 246 ---VTA-----------IHS---------------------VAGLLPPDGGLIR-RRPFRaphhtasaaalvgggsiprP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 138 GLLARANRGYLYIDEC---------NL---LEDHIVdllldvaqsgenVVERDGLSIRHPARFVLVGSGNP--------E 197
Cdd:COG0606 290 GEISLAHNGVLFLDELpefsrrvleALrqpLEDGEV------------TISRANGSVTYPARFQLVAAMNPcpcgylgdP 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 198 EGDLR--PQ------------LLDRFGLSVEVlsprdveTRVEVIRRRDTYDADPKAfleewrpkdmDIRNQILEARE-- 261
Cdd:COG0606 358 DRECRcsPRqirrylsrlsgpLLDRIDLHVEV-------PPVPYEELSSAPPGESSA----------EVRERVAAARErq 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 262 --RLPKV------EAPNTALYDCAalciALGSDGL--------RGELT------LLRSARALAALEGATAVGRDHLkrva 319
Cdd:COG0606 421 leRFGGTgirlnaQLPGRELRKYC----RLDAEARalleraleRLGLSaraydrILRVARTIADLAGSERIEREHL---- 492
|
....*....
1G8P_A 320 TMALSHRLR 328
Cdd:COG0606 493 AEALQYRRL 501
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-219 |
3.77e-03 |
|
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: 37.35 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 46 GGVLVFGDRGTGKSTAVRALAALLPeieavegcpvsspnvemiPDWATVLSTNVIRKPTPVVDLPLGVSEDRVVGALDIE 125
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELG------------------PPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1G8P_A 126 RAIskgEKAFEpgLLARANRGYLYIDECNLLEDHIVDLLLDVAQsgenvVERDGLSIRHPARFVLVGSGNPEEGDLRPQL 205
Cdd:smart00382 65 LRL---RLALA--LARKLKPDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
170
....*....|....
1G8P_A 206 LDRFGLSVEVLSPR 219
Cdd:smart00382 135 RRRFDRRIVLLLIL 148
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
23-69 |
9.42e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 37.48 E-value: 9.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
1G8P_A 23 FSAIVGQEDMKlALLLTAVDPG-IGGVLVF-GDRGTGKSTAVRALAALL 69
Cdd:COG2812 9 FDDVVGQEHVV-RTLKNALASGrLAHAYLFtGPRGVGKTTLARILAKAL 56
|
|
| |
