|
Name |
Accession |
Description |
Interval |
E-value |
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
1-277 |
0e+00 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 577.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKQNVILKKVMMVDLPLGATEDRV 80
Cdd:CHL00081 39 GGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:CHL00081 119 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:CHL00081 199 GELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKISQ 278
|
250 260 270
....*....|....*....|....*....|....*..
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDI 277
Cdd:CHL00081 279 ICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDI 315
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
1-278 |
3.72e-172 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 478.86 E-value: 3.72e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKQNVILKKVMMVDLPLGATEDRV 80
Cdd:COG1239 31 GGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDRV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:COG1239 111 VGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPEE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:COG1239 191 GELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIAE 270
|
250 260 270
....*....|....*....|....*....|....*...
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:COG1239 271 LCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIR 308
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
1-278 |
1.28e-154 |
|
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: 434.31 E-value: 1.28e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKQNVILKKVMMVDLPLGATEDRV 80
Cdd:TIGR02030 26 GGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDRV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:TIGR02030 106 CGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:TIGR02030 186 GELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVAE 265
|
250 260 270
....*....|....*....|....*....|....*...
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:TIGR02030 266 LCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIR 303
|
|
| AAA_lid_2 |
pfam17863 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
238-278 |
2.21e-10 |
|
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: 55.68 E-value: 2.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1557899027 238 ISQVCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:pfam17863 4 RAHLAIALGVSPRRADLALLRAARALAALEGRDYVTPEDVK 44
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
3-278 |
6.11e-05 |
|
MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).
Pssm-ID: 350658 [Multi-domain] Cd Length: 311 Bit Score: 43.49 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 3 VIIMGDRGTGKSTTIRAITDILPeievvqddpfnshpndfelmsddirdkieQGIKqnVILKKVMMVDLPLGATEDRVCG 82
Cdd:cd17706 44 ILLVGDPGTAKSQILKYVLKIAP-----------------------------RGVY--TSGKGSSGAGLTAAVVRDSETG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 83 TIdiekaltegvkAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG- 161
Cdd:cd17706 93 EW-----------YLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 162 -----------ELRPQLLDRFGMHSEIRTVKNPE----------------LRVQIVEQRSDFDKNPQESLSKYqaqqeef 214
Cdd:cd17706 162 ynpklspieniNLPSPLLSRFDLIFVIRDDPDEErdeelaehiidlhrgsDPEEQVKPEEDGIPIDIELLRKY------- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1557899027 215 rnkIVQAQTLLPQVTIDynLRVKISQVCSELDVDGLRGDIVTN---------RASRAYAAYEGRNIVTVEDIK 278
Cdd:cd17706 235 ---ILYARQIHPKISEE--AREKLVRWYVELRKESERRSTIPItarqlesviRLAEAHAKMRLSEVVTEEDVE 302
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1-180 |
2.23e-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: 37.74 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPeievvqddpfnshpndfelmsddirdkieqgiKQNVILKKVMMVDLPLGATEDRV 80
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELG--------------------------------PPGGGVIYIDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEpGLLAKANR---GILYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSGN 157
Cdd:smart00382 51 LIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|...
gi 1557899027 158 PEEGELRPQLLDRFGMHSEIRTV 180
Cdd:smart00382 125 DEKDLGPALLRRRFDRRIVLLLI 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
1-277 |
0e+00 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 577.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKQNVILKKVMMVDLPLGATEDRV 80
Cdd:CHL00081 39 GGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:CHL00081 119 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:CHL00081 199 GELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKISQ 278
|
250 260 270
....*....|....*....|....*....|....*..
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDI 277
Cdd:CHL00081 279 ICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDI 315
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
1-278 |
3.72e-172 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 478.86 E-value: 3.72e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKQNVILKKVMMVDLPLGATEDRV 80
Cdd:COG1239 31 GGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDRV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:COG1239 111 VGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPEE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:COG1239 191 GELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIAE 270
|
250 260 270
....*....|....*....|....*....|....*...
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:COG1239 271 LCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIR 308
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
1-278 |
1.28e-154 |
|
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: 434.31 E-value: 1.28e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKQNVILKKVMMVDLPLGATEDRV 80
Cdd:TIGR02030 26 GGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDRV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:TIGR02030 106 CGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:TIGR02030 186 GELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVAE 265
|
250 260 270
....*....|....*....|....*....|....*...
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:TIGR02030 266 LCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIR 303
|
|
| Cob-chelat-sub |
TIGR02442 |
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ... |
1-278 |
4.17e-128 |
|
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: 377.49 E-value: 4.17e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVVQDDPFNSHPNDFELMSDDIRDKIEQGIKqnvilKKVMMVDLPLGATEDRV 80
Cdd:TIGR02442 26 GGVLIRGEKGTAKSTAARGLAALLPPIDVVAGCPFSCDPDDPEEWCEECRRKYRPSEQ-----RPVPFVNLPLGATEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE 160
Cdd:TIGR02442 101 VGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGVNRVEREGLSVSHPARFVLIGTMNPEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 161 GELRPQLLDRFGMHSEIRTVKNPELRVQIVEQRSDFDKNPQESLSKYQAQQEEFRNKIVQAQTLLPQVTIDYNLRVKISQ 240
Cdd:TIGR02442 181 GDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEELRNRIARARSLLPSVRISDSLIRFISE 260
|
250 260 270
....*....|....*....|....*....|....*...
gi 1557899027 241 VCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:TIGR02442 261 LCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVR 298
|
|
| bchD |
PRK13406 |
magnesium chelatase subunit D; Provisional |
71-277 |
3.88e-15 |
|
magnesium chelatase subunit D; Provisional
Pssm-ID: 237378 [Multi-domain] Cd Length: 584 Bit Score: 75.06 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 71 LPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARF 150
Cdd:PRK13406 58 LPPGIADDRLLGGLDLAATLRAGRPVAQRGLLAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRLPARF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 151 VLV----GSgnpEEGELRPQ-LLDRFGMHSEIRTVKnpelrvqiveqRSDFDKNPQESlskyqaqqeefrNKIVQAQTLL 225
Cdd:PRK13406 138 GLValdeGA---EEDERAPAaLADRLAFHLDLDGLA-----------LRDAREIPIDA------------DDIAAARARL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1557899027 226 PQVTIDYNLRVKISQVCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDI 277
Cdd:PRK13406 192 PAVGPPPEAIAALCAAAAALGIASLRAPLLALRAARAAAALAGRTAVEEEDL 243
|
|
| AAA_lid_2 |
pfam17863 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
238-278 |
2.21e-10 |
|
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: 55.68 E-value: 2.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1557899027 238 ISQVCSELDVDGLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:pfam17863 4 RAHLAIALGVSPRRADLALLRAARALAALEGRDYVTPEDVK 44
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
98-177 |
2.06e-05 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 45.36 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 98 EPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEE----------------- 160
Cdd:PRK09862 286 GPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPtghyqgnhnrctpeqtl 365
|
90 100
....*....|....*....|
gi 1557899027 161 ---GELRPQLLDRFGMHSEI 177
Cdd:PRK09862 366 rylNRLSGPFLDRFDLSLEI 385
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
99-185 |
4.75e-05 |
|
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: 43.29 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 99 PGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNP----------EEGELRPQ-- 166
Cdd:pfam01078 99 PGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPcpcgylgdpnKRCRCSPRqi 178
|
90 100
....*....|....*....|....*....
gi 1557899027 167 ----------LLDRFGMHSEIRTVKNPEL 185
Cdd:pfam01078 179 rrylsrlsgpLLDRIDLQVEVPRLPGEEL 207
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
3-278 |
6.11e-05 |
|
MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).
Pssm-ID: 350658 [Multi-domain] Cd Length: 311 Bit Score: 43.49 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 3 VIIMGDRGTGKSTTIRAITDILPeievvqddpfnshpndfelmsddirdkieQGIKqnVILKKVMMVDLPLGATEDRVCG 82
Cdd:cd17706 44 ILLVGDPGTAKSQILKYVLKIAP-----------------------------RGVY--TSGKGSSGAGLTAAVVRDSETG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 83 TIdiekaltegvkAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG- 161
Cdd:cd17706 93 EW-----------YLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 162 -----------ELRPQLLDRFGMHSEIRTVKNPE----------------LRVQIVEQRSDFDKNPQESLSKYqaqqeef 214
Cdd:cd17706 162 ynpklspieniNLPSPLLSRFDLIFVIRDDPDEErdeelaehiidlhrgsDPEEQVKPEEDGIPIDIELLRKY------- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1557899027 215 rnkIVQAQTLLPQVTIDynLRVKISQVCSELDVDGLRGDIVTN---------RASRAYAAYEGRNIVTVEDIK 278
Cdd:cd17706 235 ---ILYARQIHPKISEE--AREKLVRWYVELRKESERRSTIPItarqlesviRLAEAHAKMRLSEVVTEEDVE 302
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
97-278 |
8.12e-05 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 43.23 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 97 FEPG-LLAkanrGILYVDEVN---------LL---DDHLVDIlldsaasgwntverEGISIRHPARFVLVGSGNPEEGE- 162
Cdd:COG0714 88 FRPGpLFA----NVLLADEINrappktqsaLLeamEERQVTI--------------PGGTYKLPEPFLVIATQNPIEQEg 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 163 ---LRPQLLDRFGMHSEIRTVkNPELRVQIVEQRSDFDKNPQESLSKYQAqqeefrnkIVQAQTLLPQVTIDYNLRVKIS 239
Cdd:COG0714 150 typLPEAQLDRFLLKLYIGYP-DAEEEREILRRHTGRHLAEVEPVLSPEE--------LLALQELVRQVHVSEAVLDYIV 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1557899027 240 QVCSEL----DVD---GLRGDIVTNRASRAYAAYEGRNIVTVEDIK 278
Cdd:COG0714 221 DLVRATrehpDLRkgpSPRASIALLRAARALALLDGRDYVTPDDVK 266
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1-178 |
3.57e-04 |
|
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: 40.21 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPEIEVvqddpfnshpndfelmsddirdkieqgikqnvilkKVMMVDLPLGATEDRV 80
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGA-----------------------------------PFLYLNASDLLEGLVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKaltegvKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLdsaasgwNTVEREGISIRHPARFVLVGSGN-PE 159
Cdd:cd00009 65 AELFGHFL------VRLLFELAEKAKPGVLFIDEIDSLSRGAQNALL-------RVLETLNDLRIDRENVRVIGATNrPL 131
|
170
....*....|....*....
gi 1557899027 160 EGELRPQLLDRFGMHSEIR 178
Cdd:cd00009 132 LGDLDRALYDRLDIRIVIP 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1-180 |
2.23e-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: 37.74 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 1 GGVIIMGDRGTGKSTTIRAITDILPeievvqddpfnshpndfelmsddirdkieqgiKQNVILKKVMMVDLPLGATEDRV 80
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELG--------------------------------PPGGGVIYIDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899027 81 CGTIDIEKALTEGVKAFEpGLLAKANR---GILYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSGN 157
Cdd:smart00382 51 LIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|...
gi 1557899027 158 PEEGELRPQLLDRFGMHSEIRTV 180
Cdd:smart00382 125 DEKDLGPALLRRRFDRRIVLLLI 147
|
|
| |
