|
Name |
Accession |
Description |
Interval |
E-value |
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
1-279 |
0e+00 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 565.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGETIETIQKKVSMVDLPLGATEDR 80
Cdd:CHL00081 38 IGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:CHL00081 118 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:CHL00081 198 EGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKIS 277
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:CHL00081 278 QICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIF 316
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
1-279 |
3.24e-162 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 453.82 E-value: 3.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGETIETIQKKVSMVDLPLGATEDR 80
Cdd:COG1239 30 IGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:COG1239 110 VVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:COG1239 190 EGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIA 269
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:COG1239 270 ELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIR 308
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
1-279 |
2.33e-142 |
|
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: 403.50 E-value: 2.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGETIETIQKKVSMVDLPLGATEDR 80
Cdd:TIGR02030 25 IGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:TIGR02030 105 VCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:TIGR02030 185 EGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVA 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:TIGR02030 265 ELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIR 303
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
4-185 |
2.14e-04 |
|
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: 41.94 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 4 VIIMGDRGTGKSTTIRAITDILPkmevvkddpfnshptdfdlmsediRNKVENGetietiqKKVSMVDLPLGATEDRVCG 83
Cdd:cd17706 44 ILLVGDPGTAKSQILKYVLKIAP------------------------RGVYTSG-------KGSSGAGLTAAVVRDSETG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 84 TIdiekaltegvkAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG- 162
Cdd:cd17706 93 EW-----------YLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGr 161
|
170 180 190
....*....|....*....|....*....|....
gi 1557899049 163 -----------ELRPQLLDRFGMHSEIRTVRDPE 185
Cdd:cd17706 162 ynpklspieniNLPSPLLSRFDLIFVIRDDPDEE 195
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
100-186 |
5.83e-04 |
|
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: 40.21 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 100 PGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNP----------EEGELRPQ-- 167
Cdd:pfam01078 99 PGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPcpcgylgdpnKRCRCSPRqi 178
|
90 100
....*....|....*....|....*....
gi 1557899049 168 ----------LLDRFGMHSEIRTVRDPEL 186
Cdd:pfam01078 179 rrylsrlsgpLLDRIDLQVEVPRLPGEEL 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2-182 |
1.18e-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: 38.51 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 2 GGVIIMGDRGTGKSTTIRAItdilpkmevvkddpfnshptdfdlmsedIRNKVENGETIETIqkkvSMVDLPLGATEDRV 81
Cdd:smart00382 3 EVILIVGPPGSGKTTLARAL----------------------------ARELGPPGGGVIYI----DGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 82 CGTIDIEKALTEGVKAFEpGLLAKANR---GILYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSGN 158
Cdd:smart00382 51 LIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|....
gi 1557899049 159 PEEGELRPQLLDRFGMHSEIRTVR 182
Cdd:smart00382 125 DEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| chlI |
CHL00081 |
Mg-protoporyphyrin IX chelatase |
1-279 |
0e+00 |
|
Mg-protoporyphyrin IX chelatase
Pssm-ID: 177020 [Multi-domain] Cd Length: 350 Bit Score: 565.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGETIETIQKKVSMVDLPLGATEDR 80
Cdd:CHL00081 38 IGGVMIMGDRGTGKSTTIRALVDLLPEIEVVKDDPFNSHPSDPELMSDEVREAIQNGETIETEKIKIPMVDLPLGATEDR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:CHL00081 118 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:CHL00081 198 EGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTSFDKNPQEFREKYEESQEELRSKIVAAQNLLPKVEIDYDLRVKIS 277
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:CHL00081 278 QICSELDVDGLRGDIVTNRAAKALAAFEGRTEVTPKDIF 316
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
1-279 |
3.24e-162 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 453.82 E-value: 3.24e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGETIETIQKKVSMVDLPLGATEDR 80
Cdd:COG1239 30 IGGVLIRGEKGTAKSTAVRALAALLPPIEVVKGCPYNCDPDDPDELCPDCRERLAAGEELPTETRPVPVVELPLGATEDR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:COG1239 110 VVGSLDLEKALKEGEKAFEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTVEREGVSVSHPARFVLVGTMNPE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:COG1239 190 EGELRPQLLDRFGLSVEVEGPRDPEERVEIVRRRLAFEADPEAFAAEYAEEQAELRERIAAARELLPEVTIPDELLRYIA 269
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:COG1239 270 ELCIALGVDGHRADIVIARAARALAALEGRTEVTAEDIR 308
|
|
| BchI-ChlI |
TIGR02030 |
magnesium chelatase ATPase subunit I; This model represents one of two ATPase subunits of the ... |
1-279 |
2.33e-142 |
|
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: 403.50 E-value: 2.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGETIETIQKKVSMVDLPLGATEDR 80
Cdd:TIGR02030 25 IGGVMVMGDRGTGKSTAVRALAALLPEIKAVAGCPFNSSPSDPEMMCEEVRIRVDSQEPLSIIKKPVPVVDLPLGATEDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:TIGR02030 105 VCGTLDIERALTEGVKAFEPGLLARANRGILYIDEVNLLEDHLVDVLLDVAASGWNVVEREGISIRHPARFVLVGSGNPE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:TIGR02030 185 EGELRPQLLDRFGLHAEIRTVRDVELRVEIVERRTEYDADPHAFCEKWQTEQEALQAKIVNAQNLLPQVTIPYDVLVKVA 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:TIGR02030 265 ELCAELDVDGLRGELTLNRAAKALAAFEGRTEVTVDDIR 303
|
|
| Cob-chelat-sub |
TIGR02442 |
cobaltochelatase subunit; Cobaltochelatase is responsible for the insertion of cobalt into the ... |
1-279 |
6.55e-119 |
|
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: 354.00 E-value: 6.55e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 1 IGGVIIMGDRGTGKSTTIRAITDILPKMEVVKDDPFNSHPTDFDLMSEDIRNKVENGEtietiQKKVSMVDLPLGATEDR 80
Cdd:TIGR02442 25 IGGVLIRGEKGTAKSTAARGLAALLPPIDVVAGCPFSCDPDDPEEWCEECRRKYRPSE-----QRPVPFVNLPLGATEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 81 VCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPE 160
Cdd:TIGR02442 100 VVGSLDIERALREGEKAFQPGLLAEAHRGILYIDEVNLLDDHLVDVLLDAAAMGVNRVEREGLSVSHPARFVLIGTMNPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 161 EGELRPQLLDRFGMHSEIRTVRDPELRVQIVEQRSAFDRNPQECLKEYHAGQEEFKERIVKAQEMLPNVSLDYDLRVKIS 240
Cdd:TIGR02442 180 EGDLRPQLLDRFGLCVDVAAPRDPEERVEIIRRRLAFDADPEAFAARWAAEQEELRNRIARARSLLPSVRISDSLIRFIS 259
|
250 260 270
....*....|....*....|....*....|....*....
gi 1557899049 241 QVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDIQ 279
Cdd:TIGR02442 260 ELCIEFGVDGHRADIVMARAARALAALDGRRRVTAEDVR 298
|
|
| bchD |
PRK13406 |
magnesium chelatase subunit D; Provisional |
72-278 |
1.20e-09 |
|
magnesium chelatase subunit D; Provisional
Pssm-ID: 237378 [Multi-domain] Cd Length: 584 Bit Score: 58.50 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 72 LPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARF 151
Cdd:PRK13406 58 LPPGIADDRLLGGLDLAATLRAGRPVAQRGLLAEADGGVLVLAMAERLEPGTAARLAAALDTGEVRLERDGLALRLPARF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 152 VLV----GSgnpEEGELRPQ-LLDRFGMHSEIRTVRdpelrvqiveqrsafDRNPQECLKEyhagqeefKERIVKAQEML 226
Cdd:PRK13406 138 GLValdeGA---EEDERAPAaLADRLAFHLDLDGLA---------------LRDAREIPID--------ADDIAAARARL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1557899049 227 PNVSLDYDLRVKISQVCGELDVDGLRGDIVTNRAAKAYAAYNNKTEVTVEDI 278
Cdd:PRK13406 192 PAVGPPPEAIAALCAAAAALGIASLRAPLLALRAARAAAALAGRTAVEEEDL 243
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
2-178 |
1.20e-05 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 46.13 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 2 GG--VIIMGDRGTGKSTTIRAITDILPkmevvkddPFNSHPTdfdLMSEDIRNKVENgetiETIQKKVSMvdLPLGATED 79
Cdd:PRK09862 209 GGhnLLLIGPPGTGKTMLASRINGLLP--------DLSNEEA---LESAAILSLVNA----ESVQKQWRQ--RPFRSPHH 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 80 RVCGTidiekALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNP 159
Cdd:PRK09862 272 SASLT-----AMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNP 346
|
170 180 190
....*....|....*....|....*....|....*....
gi 1557899049 160 EE--------------------GELRPQLLDRFGMHSEI 178
Cdd:PRK09862 347 SPtghyqgnhnrctpeqtlrylNRLSGPFLDRFDLSLEI 385
|
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
4-185 |
2.14e-04 |
|
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: 41.94 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 4 VIIMGDRGTGKSTTIRAITDILPkmevvkddpfnshptdfdlmsediRNKVENGetietiqKKVSMVDLPLGATEDRVCG 83
Cdd:cd17706 44 ILLVGDPGTAKSQILKYVLKIAP------------------------RGVYTSG-------KGSSGAGLTAAVVRDSETG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 84 TIdiekaltegvkAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNPEEG- 162
Cdd:cd17706 93 EW-----------YLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVTTLNARCSILAAANPKGGr 161
|
170 180 190
....*....|....*....|....*....|....
gi 1557899049 163 -----------ELRPQLLDRFGMHSEIRTVRDPE 185
Cdd:cd17706 162 ynpklspieniNLPSPLLSRFDLIFVIRDDPDEE 195
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
100-186 |
5.83e-04 |
|
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: 40.21 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 100 PGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISIRHPARFVLVGSGNP----------EEGELRPQ-- 167
Cdd:pfam01078 99 PGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPcpcgylgdpnKRCRCSPRqi 178
|
90 100
....*....|....*....|....*....
gi 1557899049 168 ----------LLDRFGMHSEIRTVRDPEL 186
Cdd:pfam01078 179 rrylsrlsgpLLDRIDLQVEVPRLPGEEL 207
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2-179 |
6.79e-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: 39.44 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 2 GGVIIMGDRGTGKSTTIRAITDILPKMEVvkddpfnshptdfdlmsedirnkvengetietiqkKVSMVDLPLGATEDRV 81
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGA-----------------------------------PFLYLNASDLLEGLVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 82 CGTIDIEKaltegvKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLdsaasgwNTVEREGISIRHPARFVLVGSGN-PE 160
Cdd:cd00009 65 AELFGHFL------VRLLFELAEKAKPGVLFIDEIDSLSRGAQNALL-------RVLETLNDLRIDRENVRVIGATNrPL 131
|
170
....*....|....*....
gi 1557899049 161 EGELRPQLLDRFGMHSEIR 179
Cdd:cd00009 132 LGDLDRALYDRLDIRIVIP 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2-182 |
1.18e-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: 38.51 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 2 GGVIIMGDRGTGKSTTIRAItdilpkmevvkddpfnshptdfdlmsedIRNKVENGETIETIqkkvSMVDLPLGATEDRV 81
Cdd:smart00382 3 EVILIVGPPGSGKTTLARAL----------------------------ARELGPPGGGVIYI----DGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 82 CGTIDIEKALTEGVKAFEpGLLAKANR---GILYVDEVNLLDDHLVDILLDSAAsgwntVEREGISIRHPARFVLVGSGN 158
Cdd:smart00382 51 LIIVGGKKASGSGELRLR-LALALARKlkpDVLILDEITSLLDAEQEALLLLLE-----ELRLLLLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|....
gi 1557899049 159 PEEGELRPQLLDRFGMHSEIRTVR 182
Cdd:smart00382 125 DEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
3-172 |
7.61e-03 |
|
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: 35.73 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 3 GVIIMGDRGTGKSTTIRAITDILPkmevvkddpfnshptdfdlmsedirnkvengetietiQKKVSMVDLPLGATEDRVC 82
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALS-------------------------------------NRPVFYVQLTRDTTEEDLF 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1557899049 83 GTIDIEkaltEGVKAFEPGLLAKANR--GILYVDEVNLLDDHLVDILL----DSAASGWNTVEREGISirhPARFVLVGS 156
Cdd:pfam07728 44 GRRNID----PGGASWVDGPLVRAARegEIAVLDEINRANPDVLNSLLslldERRLLLPDGGELVKAA---PDGFRLIAT 116
|
170
....*....|....*....
gi 1557899049 157 GNP---EEGELRPQLLDRF 172
Cdd:pfam07728 117 MNPldrGLNELSPALRSRF 135
|
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| |
