|
Name |
Accession |
Description |
Interval |
E-value |
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
4-282 |
1.65e-121 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 353.28 E-value: 1.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 4 TVHYPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLP--------------------------- 56
Cdd:COG1239 3 RTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPpievvkgcpyncdpddpdelcpdcrer 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 57 --AGE----------FVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAAS 124
Cdd:COG1239 83 laAGEelptetrpvpVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 125 GVNLVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQD 204
Cdd:COG1239 163 GRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQA 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489204940 205 TLRRRCAEARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRR 282
Cdd:COG1239 243 ELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLR 320
|
|
| Cob-chelat-sub |
TIGR02442 |
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ... |
7-283 |
1.78e-106 |
|
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: 324.33 E-value: 1.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 7 YPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGE--------------------------- 59
Cdd:TIGR02442 1 FPFTAIVGQEDLKLALLLNAVDPRIGGVLIRGEKGTAKSTAARGLAALLPPIDvvagcpfscdpddpeewceecrrkyrp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 60 -------FVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVNLVERD 132
Cdd:TIGR02442 81 seqrpvpFVNLPLGATEDRVVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGVNRVERE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 133 GISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQDTLRRRCAE 212
Cdd:TIGR02442 161 GLSVSHPARFVLIGTMNPEEGDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEELRNRIAR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489204940 213 ARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRRQ 283
Cdd:TIGR02442 241 ARSLLPSVRISDSLIRFISELCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVREAAELVLPHRRRR 311
|
|
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
7-282 |
5.79e-93 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 280.72 E-value: 5.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 7 YPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGEFVT------------------------ 62
Cdd:CHL00081 14 FPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKddpfnshpsdpelmsdevreaiqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 63 ---------------LPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVN 127
Cdd:CHL00081 94 getietekikipmvdLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 128 LVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQDTLR 207
Cdd:CHL00081 174 TVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELR 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489204940 208 RRCAEARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRR 282
Cdd:CHL00081 254 SKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRLR 328
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
33-163 |
1.59e-13 |
|
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: 66.55 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 33 GVLIEGPRGMAKSTLARGVAELLPAGEFVTLPLGA--SEERIVGSLDLDaalgEGRARFSPGVLAKA--DGGVLYVDEVN 108
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRdtTEEDLFGRRNID----PGGASWVDGPLVRAarEGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489204940 109 LLPDHLVDLLLDVAASGVNLV-ERDGISHRHPARFVLIGTMNP---EEGELRPQLLDRF 163
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLpDGGELVKAAPDGFRLIATMNPldrGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
13-170 |
7.09e-12 |
|
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: 62.55 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 13 VAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGEFVTLPLGASEerIVGSLDLDAALGEGRARFSPG 92
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASD--LLEGLVVAELFGHFLVRLLFE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489204940 93 VLAKADGGVLYVDEVNLLPDHLVDLLLDVaasgVNLVERDGISHRHpaRFVLIGTMNPEEGELRPQLLDRFGLNVRLD 170
Cdd:cd00009 79 LAEKAKPGVLFIDEIDSLSRGAQNALLRV----LETLNDLRIDREN--VRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-163 |
5.20e-06 |
|
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: 45.83 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 32 GGVLIEGPRGMAKSTLARGVAELLP---------AGEFVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVL 102
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGppgggviyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489204940 103 YVDEVNLLPDHLVDLLLDvaasgVNLVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRF 163
Cdd:smart00382 83 ILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
4-282 |
1.65e-121 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 353.28 E-value: 1.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 4 TVHYPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLP--------------------------- 56
Cdd:COG1239 3 RTVFPFTAIVGQEEMKLALLLNAVDPGIGGVLIRGEKGTAKSTAVRALAALLPpievvkgcpyncdpddpdelcpdcrer 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 57 --AGE----------FVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAAS 124
Cdd:COG1239 83 laAGEelptetrpvpVVELPLGATEDRVVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 125 GVNLVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQD 204
Cdd:COG1239 163 GRNTVEREGVSVSHPARFVLVGTMNPEEGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQA 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489204940 205 TLRRRCAEARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRR 282
Cdd:COG1239 243 ELRERIAAARELLPEVTIPDELLRYIAELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIRRAAELALPHRLR 320
|
|
| Cob-chelat-sub |
TIGR02442 |
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ... |
7-283 |
1.78e-106 |
|
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: 324.33 E-value: 1.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 7 YPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGE--------------------------- 59
Cdd:TIGR02442 1 FPFTAIVGQEDLKLALLLNAVDPRIGGVLIRGEKGTAKSTAARGLAALLPPIDvvagcpfscdpddpeewceecrrkyrp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 60 -------FVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVNLVERD 132
Cdd:TIGR02442 81 seqrpvpFVNLPLGATEDRVVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGVNRVERE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 133 GISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQDTLRRRCAE 212
Cdd:TIGR02442 161 GLSVSHPARFVLIGTMNPEEGDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEELRNRIAR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489204940 213 ARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRRQ 283
Cdd:TIGR02442 241 ARSLLPSVRISDSLIRFISELCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVREAAELVLPHRRRR 311
|
|
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
7-282 |
5.79e-93 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 280.72 E-value: 5.79e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 7 YPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGEFVT------------------------ 62
Cdd:CHL00081 14 FPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKddpfnshpsdpelmsdevreaiqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 63 ---------------LPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVN 127
Cdd:CHL00081 94 getietekikipmvdLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 128 LVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQDTLR 207
Cdd:CHL00081 174 TVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELR 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489204940 208 RRCAEARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRR 282
Cdd:CHL00081 254 SKIVAAQNLLPKVEIDYDLRVKISQICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIFKVITLCLRHRLR 328
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
7-283 |
1.15e-87 |
|
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: 266.75 E-value: 1.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 7 YPLSAVVAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGE--------------------------- 59
Cdd:TIGR02030 1 FPFTAIVGQDEMKLALLLNVIDPKIGGVMVMGDRGTGKSTAVRALAALLPEIKavagcpfnsspsdpemmceevrirvds 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 60 ------------FVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVN 127
Cdd:TIGR02030 81 qeplsiikkpvpVVDLPLGATEDRVCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 128 LVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRFGLNVRLDTQPPPAERAEIIRRRLAFDADPQAFVERWEGQQDTLR 207
Cdd:TIGR02030 161 VVEREGISIRHPARFVLVGSGNPEEGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQ 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489204940 208 RRCAEARRRLARIPLDDAALDSIARRCFEAAVDGLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHRRRQ 283
Cdd:TIGR02030 241 AKIVNAQNLLPQVTIPYDVLVKVAELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIRRVAVLALRHRLRK 316
|
|
| bchD |
PRK13406 |
magnesium chelatase subunit D; Provisional |
16-280 |
9.61e-15 |
|
magnesium chelatase subunit D; Provisional
Pssm-ID: 237378 [Multi-domain] Cd Length: 584 Bit Score: 75.06 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 16 DELKLALCLAAVDPA-IGGVLIEGPRGMAKSTLARGVAELLPAGEFVT-LPLGASEERIVGSLDLDAALGEGRARFSPGV 93
Cdd:PRK13406 9 ADAALAAALLAVDPAgLGGVVLRARAGPVRDRWLAALRALLPAGTPLRrLPPGIADDRLLGGLDLAATLRAGRPVAQRGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 94 LAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVNLVERDGISHRHPARFVLIG-TMNPEEGELRPQ-LLDRFGLNVRL-- 169
Cdd:PRK13406 89 LAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRLPARFGLVAlDEGAEEDERAPAaLADRLAFHLDLdg 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 170 ----DTQPPPAERAEIIRRRLAFDAdpqafverwegqqdtlrrrcaearrrlarIPLDDAALDSIARRCFEAAVDGLRAD 245
Cdd:PRK13406 169 lalrDAREIPIDADDIAAARARLPA-----------------------------VGPPPEAIAALCAAAAALGIASLRAP 219
|
250 260 270
....*....|....*....|....*....|....*
gi 489204940 246 LVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHR 280
Cdd:PRK13406 220 LLALRAARAAAALAGRTAVEEEDLALAARLVLAPR 254
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
33-163 |
1.59e-13 |
|
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: 66.55 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 33 GVLIEGPRGMAKSTLARGVAELLPAGEFVTLPLGA--SEERIVGSLDLDaalgEGRARFSPGVLAKA--DGGVLYVDEVN 108
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRdtTEEDLFGRRNID----PGGASWVDGPLVRAarEGEIAVLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489204940 109 LLPDHLVDLLLDVAASGVNLV-ERDGISHRHPARFVLIGTMNP---EEGELRPQLLDRF 163
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLpDGGELVKAAPDGFRLIATMNPldrGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
13-170 |
7.09e-12 |
|
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: 62.55 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 13 VAADELKLALCLAAVDPAIGGVLIEGPRGMAKSTLARGVAELLPAGEFVTLPLGASEerIVGSLDLDAALGEGRARFSPG 92
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASD--LLEGLVVAELFGHFLVRLLFE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489204940 93 VLAKADGGVLYVDEVNLLPDHLVDLLLDVaasgVNLVERDGISHRHpaRFVLIGTMNPEEGELRPQLLDRFGLNVRLD 170
Cdd:cd00009 79 LAEKAKPGVLFIDEIDSLSRGAQNALLRV----LETLNDLRIDREN--VRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
10-280 |
1.11e-09 |
|
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: 58.64 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 10 SAVVAADELKLALcLAAVdpAIGG-VLIEGPRGMAKSTLARGVAELLpagefvtlplGASEERIVGSLDLDAA--LGE-- 84
Cdd:COG0714 12 KVYVGQEELIELV-LIAL--LAGGhLLLEGVPGVGKTTLAKALARAL----------GLPFIRIQFTPDLLPSdiLGTyi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 85 -----GRARFSPG-VLAkadgGVLYVDEVNLLPDHLVDLLLDVAAsgvnlvER----DGISHRHPARFVLIGTMNPEEGE 154
Cdd:COG0714 79 ydqqtGEFEFRPGpLFA----NVLLADEINRAPPKTQSALLEAME------ERqvtiPGGTYKLPEPFLVIATQNPIEQE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 155 ----LRPQLLDRFGLNVRLDTQPPPAERaEIIRRRLAFDAD---PQAFVERWEGQQDTLRRrcaearrrlarIPLDDAAL 227
Cdd:COG0714 149 gtypLPEAQLDRFLLKLYIGYPDAEEER-EILRRHTGRHLAevePVLSPEELLALQELVRQ-----------VHVSEAVL 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 228 DSIARRCFE----AAVD---GLRADLVWLRAARAHAAWRGGERIEAEDIDAVEHFALLHR 280
Cdd:COG0714 217 DYIVDLVRAtrehPDLRkgpSPRASIALLRAARALALLDGRDYVTPDDVKAVAGPVLKHR 276
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
34-187 |
9.56e-09 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 56.45 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELLP--AGEFVTLPLGA-SEERIVGSL--DLDAALGEGRARFSPGVLAKADGGVLYVDEVN 108
Cdd:COG3284 347 VLILGETGTGKELFARAIHAASPraDGPFVAVNCAAiPEELIESELfgYEPGAFTGARRKGRPGKIEQADGGTLFLDEIG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 109 LLPDHLVDLLLDVAASGVnlVERDGISHRHPARFVLIGTMNP------EEGELRPQLLDRF-GLNVRLdtqPPPAERAEI 181
Cdd:COG3284 427 DMPLALQARLLRVLQERE--VTPLGGTKPIPVDVRLIAATHRdlrelvAAGRFREDLYYRLnGLTLTL---PPLREREDL 501
|
....*....
gi 489204940 182 ---IRRRLA 187
Cdd:COG3284 502 palIEHLLR 510
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
34-165 |
2.63e-08 |
|
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: 54.66 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELLPAGEFVTLpLGASEERIVGSLDLDAALGEGRARfsPGVLAKADGGVLYVDEVNLLPDH 113
Cdd:cd17706 44 ILLVGDPGTAKSQILKYVLKIAPRGVYTSG-KGSSGAGLTAAVVRDSETGEWYLE--AGALVLADGGVCCIDEFDKMKEL 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489204940 114 LVDLLLDVAASGVNLVERDGISHRHPARFVLIGTMNPEEG------------ELRPQLLDRFGL 165
Cdd:cd17706 121 DRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGrynpklspieniNLPSPLLSRFDL 184
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
9-186 |
2.93e-06 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 48.82 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 9 LSAVVAADELKLALCLAAVdpaiGG--VLIEGPRGMAKSTLARGVAELLP---------AGEFVTLPLGASEERIVG--- 74
Cdd:PRK09862 190 LSDVIGQEQGKRGLEITAA----GGhnLLLIGPPGTGKTMLASRINGLLPdlsneealeSAAILSLVNAESVQKQWRqrp 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 75 ------SLDLDAALGEGrARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVNLVERDGISHRHPARFVLIGTM 148
Cdd:PRK09862 266 frsphhSASLTAMVGGG-AIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAM 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489204940 149 NPEE--------------------GELRPQLLDRFGLNVRLDTQPP--------PAERAEIIRRRL 186
Cdd:PRK09862 345 NPSPtghyqgnhnrctpeqtlrylNRLSGPFLDRFDLSLEIPLPPPgilsktvvPGESSATVKQRV 410
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-163 |
5.20e-06 |
|
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: 45.83 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 32 GGVLIEGPRGMAKSTLARGVAELLP---------AGEFVTLPLGASEERIVGSLDLDAALGEGRARFSPGVLAKADGGVL 102
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGppgggviyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489204940 103 YVDEVNLLPDHLVDLLLDvaasgVNLVERDGISHRHPARFVLIGTMNPEEGELRPQLLDRF 163
Cdd:smart00382 83 ILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| MCM8 |
cd17759 |
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a ... |
34-165 |
8.05e-05 |
|
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: 43.68 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELLPAGEFVTLPLGASEERIVGsldLDAALGEGRARFSPGVLAKADGGVLYVDEVNLLPDH 113
Cdd:cd17759 46 VLIVGDPGLGKSQMLQAACNIAPRGVYVCGNTTTTSGLTVT---LTKDGRSGDFALEAGALVLGDQGICGIDEFDKMGSQ 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489204940 114 LVDLLLDVAASGVNLVeRDGISHRHPARFVLIGTMNPEEGE------------LRPQLLDRFGL 165
Cdd:cd17759 123 HQALLEAMEQQSVSLA-KAGVVCSLPARTSVIAAANPVGGHynkgktvsenlkMGPALLSRFDL 185
|
|
| MCM |
pfam00493 |
MCM P-loop domain; |
34-165 |
1.46e-04 |
|
MCM P-loop domain;
Pssm-ID: 459830 [Multi-domain] Cd Length: 224 Bit Score: 42.52 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELLPAGEFVTLPlGASEERIVGSLDLDAALGEgrarFS--PGVLAKADGGVLYVDEVNLLP 111
Cdd:pfam00493 60 VLLVGDPGTAKSQLLKYVEKIAPRAVYTSGK-GSSAAGLTAAVVRDPVTGE----FVleAGALVLADGGVCCIDEFDKMN 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489204940 112 DHLVDLLLDVAASGVNLVERDGISHRHPARFVLIGTMNPEEG------------ELRPQLLDRFGL 165
Cdd:pfam00493 135 DEDRVALHEAMEQQTISIAKAGIVATLNARCSILAAANPIFGrydpkksiaeniNLPPPLLSRFDL 200
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
34-163 |
2.48e-04 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 40.27 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELL-------PAGEFVTLPLGASEERIvgsldldaalgegRARFSpgvLAKADG-GVLYVD 105
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELgapfieiSGSELVSKYVGESEKRL-------------RELFE---AAKKLApCVIFID 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 106 EVNLLPDHLVDLLLDVAASGVN--LVERDGISHRHPaRFVLIGTMNpEEGELRPQLLDRF 163
Cdd:pfam00004 65 EIDALAGSRGSGGDSESRRVVNqlLTELDGFTSSNS-KVIVIAATN-RPDKLDPALLGRF 122
|
|
| MCM_arch |
cd17761 |
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ... |
34-183 |
8.36e-04 |
|
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork
Pssm-ID: 350667 [Multi-domain] Cd Length: 308 Bit Score: 40.51 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELLPAGEFVTLPlGASEERIVGSLDLDAalGEGRARFSPGVLAKADGGVLYVDEVNLLPDH 113
Cdd:cd17761 45 ILLVGDPGTAKSQLLKYVSKVAPRAVYTTGK-GSTAAGLTAAVVRDE--GTGEWYLEAGALVLADKGIAVVDEIDKMRKE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 114 LVDLLLDVAASGVNLVERDGISHRHPARFVLIGTMNPEEG------------ELRPQLLDRFGLNVRLDTQPPPAERAEI 181
Cdd:cd17761 122 DRSALHEAMEQQTISIAKAGIVATLNARAAVLAAANPKFGrfdsyrpvaeqiDLPPTLLSRFDLIFVLKDTPNEEKDRRL 201
|
..
gi 489204940 182 IR 183
Cdd:cd17761 202 AN 203
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
9-150 |
1.17e-03 |
|
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: 39.44 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 9 LSAVVAADELKLALCLAAvdpaIGG--VLIEGPRGMAKSTLARGVAELLPagefvtlPLGASE----ERI--VGSLDLD- 79
Cdd:pfam01078 2 LADVKGQEQAKRALEIAA----AGGhnLLMIGPPGSGKTMLAKRLPGILP-------PLTEAEalevTAIhsVAGLGGDg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 80 -----------------AALGEGRARFSPGVLAKADGGVLYVDEVNLLPDHLVDLLLDVAASGVNLVERDGISHRHPARF 142
Cdd:pfam01078 71 glirrrpfraphhsasaAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARF 150
|
....*...
gi 489204940 143 VLIGTMNP 150
Cdd:pfam01078 151 QLVAAMNP 158
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
34-182 |
1.85e-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: 39.95 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 34 VLIEGPRGMAKSTLARGVAELLP--AGEFVTLPLGASEERIVGS----LDLDAALGEGRARfsPGVLAKADGGVLYVDEV 107
Cdd:COG2204 157 VLITGESGTGKELVARAIHRLSPraDGPFVAVNCAAIPEELLESelfgHEKGAFTGAVARR--IGKFELADGGTLFLDEI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204940 108 NLLPDHLVDLLLDVAASGVnlVERDGISHRHPARFVLIGTMNP------EEGELRPQLLDRfgLNVRLDTQPPPAERAEI 181
Cdd:COG2204 235 GEMPLALQAKLLRVLQERE--FERVGGNKPIPVDVRVIAATNRdleelvEEGRFREDLYYR--LNVFPIELPPLRERRED 310
|
.
gi 489204940 182 I 182
Cdd:COG2204 311 I 311
|
|
| |
