|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
1-500 |
0e+00 |
|
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440371 [Multi-domain] Cd Length: 502 Bit Score: 768.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 1 MVARVNTVAFQGIEGVPVEVQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHF 80
Cdd:COG0606 1 MLARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 81 DLPIALGLMAALGAIPAEALSQYVVLGELNLDGTIGTVSGALPAAIGANALG-KGLICPAESGPEAAWAGaGIDILAPRS 159
Cdd:COG0606 81 DLPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGiRRLIVPAANAAEAALVP-GIEVYGASS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 160 LIALANHFRGTQLLSRPTPAIRAN-PVNLPDLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLE 238
Cdd:COG0606 160 LLEVVAFLRGEQPLPPAEPDAPPAePPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 239 VAELLEVSMVHSIAGQLS-GGKLSDRRPFRTPHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQP 317
Cdd:COG0606 240 EEEALEVTAIHSVAGLLPpDGGLIRRRPFRAPHHTASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 318 LETGECIIARANHRVSYPAEIQLVAAMNPCRCGMAGEPGFTCARGPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDLIR 397
Cdd:COG0606 320 LEDGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 398 PVVSEPSAVVAARVARARLAQQERYAAAGfpaIRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVAR 477
Cdd:COG0606 400 APPGESSAEVRERVAAARERQLERFGGTG---IRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVAR 476
|
490 500
....*....|....*....|...
gi 499273418 478 TLADLDGKQTVGRIHVAEAVSYR 500
Cdd:COG0606 477 TIADLAGSERIEREHLAEALQYR 499
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
5-500 |
8.31e-161 |
|
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]
Pssm-ID: 129465 [Multi-domain] Cd Length: 499 Bit Score: 465.86 E-value: 8.31e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 5 VNTVAFQGIEGVPVEVQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHFDLPI 84
Cdd:TIGR00368 1 VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 85 ALGLMAALGAIPAEALSQYVVLGELNLDGTIGTVSGALPAAIGANALG-KGLICPAESGPEAAWAgAGIDILAPRSLIAL 163
Cdd:TIGR00368 81 AIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGrKFIIVPKENAEEASLI-DGLNIYGADHLKEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 164 ANHFRGTQLLSRPT-----PAIRANPVNLPDLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLE 238
Cdd:TIGR00368 160 VKFLEGSEKLPPRTntkpkSIINKSYIIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 239 VAELLEVSMVHSIAGQLSGGKLSDRRPFRTPHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPL 318
Cdd:TIGR00368 240 NEEAIETARIWSLVGKLIDRKQIKQRPFRSPHHSASKPALVGGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 319 ETGECIIARANHRVSYPAEIQLVAAMNPCRCGMAGEPGFTCARGPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDLIRP 398
Cdd:TIGR00368 320 EDGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLST 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 399 VVSEPSAVVAARVARARLAQQERYAAagFPAIRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVART 478
Cdd:TIGR00368 400 GSGESSAEVKQRVIKAREIQNIRYEK--FANINKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVART 477
|
490 500
....*....|....*....|..
gi 499273418 479 LADLDGKQTVGRIHVAEAVSYR 500
Cdd:TIGR00368 478 IADLKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
5-508 |
3.60e-131 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 390.49 E-value: 3.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 5 VNTVAFQGIEGVPVEVQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHFDLPI 84
Cdd:PRK09862 6 VHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGRYDLPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 85 ALGLMAALGAIPAEALSQYVVLGELNLDGTIGTVSGALPAAIGANALGKGLICPAESGPEAAWAgAGIDILAPRSLIALA 164
Cdd:PRK09862 86 AIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLI-NGEGCLIADHLQAVC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 165 NHFRGTQLLSRPTPAIRANPVNLPDLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLEVAELLE 244
Cdd:PRK09862 165 AFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNEEALE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 245 VSMVHSIAGQLSGGKLSDRRPFRTPHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECI 324
Cdd:PRK09862 245 SAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 325 IARANHRVSYPAEIQLVAAMNPCRCGMAGEPGFTCArgPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDLIRPVVsePS 404
Cdd:PRK09862 325 LSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCT--PEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVV--PG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 405 AVVAARVARARLAQQERYAAAGfpaiRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVARTLADLDG 484
Cdd:PRK09862 401 ESSATVKQRVMAARERQFKRQN----KLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIADIDQ 476
|
490 500
....*....|....*....|....
gi 499273418 485 KQTVGRIHVAEAVSYRiAGERLTV 508
Cdd:PRK09862 477 SDIITRQHLQEAVSYR-AIDRLLI 499
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
189-395 |
3.98e-128 |
|
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: 371.48 E-value: 3.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 189 DLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLEVAELLEVSMVHSIAGQLSGGKLSDRRPFRT 268
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLGGDGGLIRRRPFRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 269 PHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECIIARANHRVSYPAEIQLVAAMNPCR 348
Cdd:pfam01078 81 PHHSASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPCP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499273418 349 CGMAGEPGFTCARGPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDL 395
Cdd:pfam01078 161 CGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
194-388 |
5.80e-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: 49.07 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 194 KGQESARRAMEVAAAGGH--NLLMVGPPGSGKSMLAarlpsilpplevaellevsmvHSIAGQLSGgklsDRRPFRTPHH 271
Cdd:cd00009 1 VGQEEAIEALREALELPPpkNLLLYGPPGTGKTTLA---------------------RAIANELFR----PGAPFLYLNA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 272 SATMAALIGGGL------RARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECIIARanhrvsyPAEIQLVAAMN 345
Cdd:cd00009 56 SDLLEGLVVAELfghflvRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID-------RENVRVIGATN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499273418 346 PcrcgmagepgftcargprcvtDYQSRISGPLLDRIDIRIDVP 388
Cdd:cd00009 129 R---------------------PLLGDLDRALYDRLDIRIVIP 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-346 |
6.71e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 210 GHNLLMVGPPGSGKSMLAARLPSILPPLEvAELLEVSMVHSIAGQLSGGKLSDRRPFRTPHHSATMAALigggLRARpge 289
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG-GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL----ALAL--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499273418 290 ASLAHHGVLFLDEFPEFSPQVLDALRQPLetgecIIARANHRVSYPAEIQLVAAMNP 346
Cdd:smart00382 74 ARKLKPDVLILDEITSLLDAEQEALLLLL-----EELRLLLLLKSEKNLTVILTTND 125
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
1-500 |
0e+00 |
|
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440371 [Multi-domain] Cd Length: 502 Bit Score: 768.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 1 MVARVNTVAFQGIEGVPVEVQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHF 80
Cdd:COG0606 1 MLARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 81 DLPIALGLMAALGAIPAEALSQYVVLGELNLDGTIGTVSGALPAAIGANALG-KGLICPAESGPEAAWAGaGIDILAPRS 159
Cdd:COG0606 81 DLPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGiRRLIVPAANAAEAALVP-GIEVYGASS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 160 LIALANHFRGTQLLSRPTPAIRAN-PVNLPDLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLE 238
Cdd:COG0606 160 LLEVVAFLRGEQPLPPAEPDAPPAePPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 239 VAELLEVSMVHSIAGQLS-GGKLSDRRPFRTPHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQP 317
Cdd:COG0606 240 EEEALEVTAIHSVAGLLPpDGGLIRRRPFRAPHHTASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 318 LETGECIIARANHRVSYPAEIQLVAAMNPCRCGMAGEPGFTCARGPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDLIR 397
Cdd:COG0606 320 LEDGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 398 PVVSEPSAVVAARVARARLAQQERYAAAGfpaIRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVAR 477
Cdd:COG0606 400 APPGESSAEVRERVAAARERQLERFGGTG---IRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVAR 476
|
490 500
....*....|....*....|...
gi 499273418 478 TLADLDGKQTVGRIHVAEAVSYR 500
Cdd:COG0606 477 TIADLAGSERIEREHLAEALQYR 499
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
5-500 |
8.31e-161 |
|
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]
Pssm-ID: 129465 [Multi-domain] Cd Length: 499 Bit Score: 465.86 E-value: 8.31e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 5 VNTVAFQGIEGVPVEVQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHFDLPI 84
Cdd:TIGR00368 1 VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 85 ALGLMAALGAIPAEALSQYVVLGELNLDGTIGTVSGALPAAIGANALG-KGLICPAESGPEAAWAgAGIDILAPRSLIAL 163
Cdd:TIGR00368 81 AIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGrKFIIVPKENAEEASLI-DGLNIYGADHLKEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 164 ANHFRGTQLLSRPT-----PAIRANPVNLPDLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLE 238
Cdd:TIGR00368 160 VKFLEGSEKLPPRTntkpkSIINKSYIIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 239 VAELLEVSMVHSIAGQLSGGKLSDRRPFRTPHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPL 318
Cdd:TIGR00368 240 NEEAIETARIWSLVGKLIDRKQIKQRPFRSPHHSASKPALVGGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 319 ETGECIIARANHRVSYPAEIQLVAAMNPCRCGMAGEPGFTCARGPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDLIRP 398
Cdd:TIGR00368 320 EDGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLST 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 399 VVSEPSAVVAARVARARLAQQERYAAagFPAIRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVART 478
Cdd:TIGR00368 400 GSGESSAEVKQRVIKAREIQNIRYEK--FANINKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVART 477
|
490 500
....*....|....*....|..
gi 499273418 479 LADLDGKQTVGRIHVAEAVSYR 500
Cdd:TIGR00368 478 IADLKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
5-508 |
3.60e-131 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 390.49 E-value: 3.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 5 VNTVAFQGIEGVPVEVQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHFDLPI 84
Cdd:PRK09862 6 VHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGRYDLPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 85 ALGLMAALGAIPAEALSQYVVLGELNLDGTIGTVSGALPAAIGANALGKGLICPAESGPEAAWAgAGIDILAPRSLIALA 164
Cdd:PRK09862 86 AIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLI-NGEGCLIADHLQAVC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 165 NHFRGTQLLSRPTPAIRANPVNLPDLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLEVAELLE 244
Cdd:PRK09862 165 AFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNEEALE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 245 VSMVHSIAGQLSGGKLSDRRPFRTPHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECI 324
Cdd:PRK09862 245 SAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIESGQIH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 325 IARANHRVSYPAEIQLVAAMNPCRCGMAGEPGFTCArgPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDLIRPVVsePS 404
Cdd:PRK09862 325 LSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCT--PEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVV--PG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 405 AVVAARVARARLAQQERYAAAGfpaiRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVARTLADLDG 484
Cdd:PRK09862 401 ESSATVKQRVMAARERQFKRQN----KLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIADIDQ 476
|
490 500
....*....|....*....|....
gi 499273418 485 KQTVGRIHVAEAVSYRiAGERLTV 508
Cdd:PRK09862 477 SDIITRQHLQEAVSYR-AIDRLLI 499
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
189-395 |
3.98e-128 |
|
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: 371.48 E-value: 3.98e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 189 DLADIKGQESARRAMEVAAAGGHNLLMVGPPGSGKSMLAARLPSILPPLEVAELLEVSMVHSIAGQLSGGKLSDRRPFRT 268
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLGGDGGLIRRRPFRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 269 PHHSATMAALIGGGLRARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECIIARANHRVSYPAEIQLVAAMNPCR 348
Cdd:pfam01078 81 PHHSASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPCP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499273418 349 CGMAGEPGFTCARGPRCVTDYQSRISGPLLDRIDIRIDVPAVSATDL 395
Cdd:pfam01078 161 CGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
20-140 |
4.62e-47 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 159.54 E-value: 4.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 20 VQVMVAPGKIGIQIVGLPDKAVAESRERVQAALHASGLALPAKKVTVNLAPADLPKEGSHFDLPIALGLMAALGAIPAEa 99
Cdd:pfam13541 1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFEFPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQIPVL- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499273418 100 lSQYVVLGELNLDGTIGTVSGALPAAIGANALG-KGLICPAE 140
Cdd:pfam13541 80 -EETIFLGELSLDGSLRPVRGALPIALAARKHGfRGLIVPKE 120
|
|
| Mg_chelatase_C |
pfam13335 |
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative ... |
417-500 |
1.25e-28 |
|
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative bacterial magnesium chelatase subunit ChlI proteins. Most members have the associated pfam01078.
Pssm-ID: 433125 Cd Length: 93 Bit Score: 108.63 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 417 AQQERYAaagfpaiRTNARCTTTLIEKYAEPDASGLQLLRDAAERLKFSARGYHRILKVARTLADLDGKQTVGRIHVAEA 496
Cdd:pfam13335 17 RQAERFG-------GENAQLPGRELRRFCRLDAAARALLERALERLGLSARAYDRILRVARTIADLAGSERIGREHLAEA 89
|
....
gi 499273418 497 VSYR 500
Cdd:pfam13335 90 LQYR 93
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
212-346 |
1.61e-08 |
|
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: 53.07 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 212 NLLMVGPPGSGKSMLAARLpsilpplevAELlevsmvhsiagqlsggkLSDRRPFRTPHHSATMAALIGGGLRARPGEAS 291
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERL---------AAA-----------------LSNRPVFYVQLTRDTTEEDLFGRRNIDPGGAS 54
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499273418 292 L--------AHHG-VLFLDEFPEFSPQVLDALRQPLETGECIIARANHRVSYPAE-IQLVAAMNP 346
Cdd:pfam07728 55 WvdgplvraAREGeIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAAPDgFRLIATMNP 119
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
194-388 |
5.80e-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: 49.07 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 194 KGQESARRAMEVAAAGGH--NLLMVGPPGSGKSMLAarlpsilpplevaellevsmvHSIAGQLSGgklsDRRPFRTPHH 271
Cdd:cd00009 1 VGQEEAIEALREALELPPpkNLLLYGPPGTGKTTLA---------------------RAIANELFR----PGAPFLYLNA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 272 SATMAALIGGGL------RARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECIIARanhrvsyPAEIQLVAAMN 345
Cdd:cd00009 56 SDLLEGLVVAELfghflvRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRID-------RENVRVIGATN 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499273418 346 PcrcgmagepgftcargprcvtDYQSRISGPLLDRIDIRIDVP 388
Cdd:cd00009 129 R---------------------PLLGDLDRALYDRLDIRIVIP 150
|
|
| ChlI |
COG1239 |
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism]; |
193-497 |
3.39e-06 |
|
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
Pssm-ID: 440852 [Multi-domain] Cd Length: 344 Bit Score: 48.98 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 193 IKGQESARRAMEVAAA----GGhnLLMVGPPGSGKSMLAARLPSILPPLEV----------AELLEVSMVHSIAGQLSGG 258
Cdd:COG1239 11 IVGQEEMKLALLLNAVdpgiGG--VLIRGEKGTAKSTAVRALAALLPPIEVvkgcpyncdpDDPDELCPDCRERLAAGEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 259 KLSDRRPFRT---PHhSATMAALIGG---------GLRA-RPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGECII 325
Cdd:COG1239 89 LPTETRPVPVvelPL-GATEDRVVGSldlekalkeGEKAfEPGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRNTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 326 ARANHRVSYPAEIQLVAAMNPcrcgmagEPGftcargprcvtdyqsRISGPLLDRIDIRIDVPAVSATDLIRPVVsepsa 405
Cdd:COG1239 168 EREGVSVSHPARFVLVGTMNP-------EEG---------------ELRPQLLDRFGLSVEVEGPRDPEERVEIV----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 406 vvaarvararlAQQERYAA--AGFpairtnarctttlIEKYAEPDASGLQLLRDAAERL------------------KFS 465
Cdd:COG1239 221 -----------RRRLAFEAdpEAF-------------AAEYAEEQAELRERIAAARELLpevtipdellryiaelciALG 276
|
330 340 350
....*....|....*....|....*....|....*.
gi 499273418 466 ARGyHR----ILKVARTLADLDGKQTVGRIHVAEAV 497
Cdd:COG1239 277 VDG-HRadivIARAARALAALEGRTEVTAEDIRRAA 311
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-346 |
6.71e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 210 GHNLLMVGPPGSGKSMLAARLPSILPPLEvAELLEVSMVHSIAGQLSGGKLSDRRPFRTPHHSATMAALigggLRARpge 289
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG-GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL----ALAL--- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 499273418 290 ASLAHHGVLFLDEFPEFSPQVLDALRQPLetgecIIARANHRVSYPAEIQLVAAMNP 346
Cdd:smart00382 74 ARKLKPDVLILDEITSLLDAEQEALLLLL-----EELRLLLLLKSEKNLTVILTTND 125
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
213-388 |
3.01e-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: 40.65 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 213 LLMVGPPGSGKSMLAarlpsilppLEVAELLEVSMVhsiagQLSGGKLsdrrpfrTPHHSATMAALIggglRARPGEASL 292
Cdd:pfam00004 1 LLLYGPPGTGKTTLA---------KAVAKELGAPFI-----EISGSEL-------VSKYVGESEKRL----RELFEAAKK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 293 AHHGVLFLDEfpefspqvLDAlrqpletgeciIARANHRVSYPAEIQLVAAMNPCrcgMAgepGFTCARGPRCV---TDY 369
Cdd:pfam00004 56 LAPCVIFIDE--------IDA-----------LAGSRGSGGDSESRRVVNQLLTE---LD---GFTSSNSKVIViaaTNR 110
|
170
....*....|....*....
gi 499273418 370 QSRISGPLLDRIDIRIDVP 388
Cdd:pfam00004 111 PDKLDPALLGRFDRIIEFP 129
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
190-230 |
2.34e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 39.87 E-value: 2.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499273418 190 LADIKGQESARRAM----------EVAAAGG----HNLLMVGPPGSGKSMLAARL 230
Cdd:COG1223 1 LDDVVGQEEAKKKLkliikelrrrENLRKFGlwppRKILFYGPPGTGKTMLAEAL 55
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
144-343 |
4.41e-03 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 39.88 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 144 EAAWAGAGIDILAPRSLIALANHFRGTQLLSRP-------TPAIRANPVNLPDLA--DIKGQESARRAMEVAAAGgHNLL 214
Cdd:COG3284 270 EALPDGARRAPASPRPLRLRDGRRLGALLRLRParraaraAPAGAPAPAALAALAggDPAMRRALRRARRLADRD-IPVL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273418 215 MVGPPGSGKSMLAARLpsilpplevaellevsmvHsiagQLSGGKlsdRRPFRTPHHSATMAALIGGGL----------- 283
Cdd:COG3284 349 ILGETGTGKELFARAI------------------H----AASPRA---DGPFVAVNCAAIPEELIESELfgyepgaftga 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499273418 284 --RARPGEASLAHHGVLFLDEFPEFSPQVLDALRQPLETGEciIARANHRVSYPAEIQLVAA 343
Cdd:COG3284 404 rrKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQERE--VTPLGGTKPIPVDVRLIAA 463
|
|
| TIP49 |
pfam06068 |
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ... |
195-227 |
6.22e-03 |
|
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.
Pssm-ID: 399217 [Multi-domain] Cd Length: 347 Bit Score: 38.83 E-value: 6.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 499273418 195 GQESARRAMEV-------AAAGGHNLLMVGPPGSGKSMLA 227
Cdd:pfam06068 28 GQEKAREAAGVivemikeGKIAGRAVLIAGPPGTGKTALA 67
|
|
| |
