|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
3-492 |
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: 839.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 3 FAKIYTRGLLGLHAPLIEVEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSRLD 82
Cdd:COG0606 2 LARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 83 LPIALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQ-HQLILPSPNAQEASQLPDFQVFAANHLQ 161
Cdd:COG0606 82 LPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGiRRLIVPAANAAEAALVPGIEVYGASSLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 162 EVCAHLAQAETLPPFKTSPLDQHSFYKFDLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILPPLNTQ 241
Cdd:COG0606 162 EVVAFLRGEQPLPPAEPDAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 242 ENLEVASIYSIA----NANHPFGQRPFRAPHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLE 317
Cdd:COG0606 242 EALEVTAIHSVAgllpPDGGLIRRRPFRAPHHTASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 318 SKEIVISRASRQITFPANFQLVAAMNPCPCGYAFNQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVPPLQAQELQDNK 397
Cdd:COG0606 322 DGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSAP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 398 PVENSETVRQRVISAYNIQIERQNA----LNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIADL 473
Cdd:COG0606 402 PGESSAEVRERVAAARERQLERFGGtgirLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIADL 481
|
490
....*....|....*....
gi 2552241993 474 NQSPDIQTGHLSEALSYRG 492
Cdd:COG0606 482 AGSERIEREHLAEALQYRR 500
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
6-491 |
0e+00 |
|
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: 582.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 6 IYTRGLLGLHAPLIEVEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSRLDLPI 85
Cdd:TIGR00368 1 VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 86 ALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQHQ-LILPSPNAQEASQLPDFQVFAANHLQEVC 164
Cdd:TIGR00368 81 AIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKfIIVPKENAEEASLIDGLNIYGADHLKEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 165 AHLAQAETLPP---FKTSPLDQHSF-YKFDLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILPPLNT 240
Cdd:TIGR00368 161 KFLEGSEKLPPrtnTKPKSIINKSYiIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 241 QENLEVASIYSIANANHPFG---QRPFRAPHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLE 317
Cdd:TIGR00368 241 EEAIETARIWSLVGKLIDRKqikQRPFRSPHHSASKPALVGGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 318 SKEIVISRASRQITFPANFQLVAAMNPCPCGYAFNQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVPPLQAQELQDNK 397
Cdd:TIGR00368 321 DGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 398 PVENSETVRQRVISAYNIQIERQN-----ALNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIAD 472
Cdd:TIGR00368 401 SGESSAEVKQRVIKAREIQNIRYEkfaniNKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVARTIAD 480
|
490
....*....|....*....
gi 2552241993 473 LNQSPDIQTGHLSEALSYR 491
Cdd:TIGR00368 481 LKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
1-491 |
0e+00 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 538.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 1 MSFAKIYTRGLLGLHAPLIEVEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSR 80
Cdd:PRK09862 1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 81 LDLPIALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQHQLILPSPNAQEASQLPDFQVFAANHL 160
Cdd:PRK09862 81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLINGEGCLIADHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 161 QEVCAHL----AQAETLPPFKTSPLDQHsfykfDLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILP 236
Cdd:PRK09862 161 QAVCAFLegkhALERPKPTDAVSRALQH-----DLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 237 PLNTQENLEVASIYSIANA---NHPFGQRPFRAPHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLR 313
Cdd:PRK09862 236 DLSNEEALESAAILSLVNAesvQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 314 QPLESKEIVISRASRQITFPANFQLVAAMNPCPCGYAfnQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVP-PLQAQE 392
Cdd:PRK09862 316 EPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHY--QGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPlPPPGIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 393 LQDNKPVENSETVRQRVISAYNIQIERQNALNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIAD 472
Cdd:PRK09862 394 SKTVVPGESSATVKQRVMAARERQFKRQNKLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIAD 473
|
490
....*....|....*....
gi 2552241993 473 LNQSPDIQTGHLSEALSYR 491
Cdd:PRK09862 474 IDQSDIITRQHLQEAVSYR 492
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
190-393 |
2.26e-133 |
|
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: 384.19 E-value: 2.26e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 190 DLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILPPLNTQENLEVASIYSIAN---ANHPFGQRPFRA 266
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGlggDGGLIRRRPFRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 267 PHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRQITFPANFQLVAAMNPCP 346
Cdd:pfam01078 81 PHHSASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPCP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2552241993 347 CGYAFNQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVPPLQAQEL 393
Cdd:pfam01078 161 CGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
211-344 |
4.34e-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: 46.60 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 211 GHSLLFRGPPGTGKTLLASRLASILPPLNtqenlevASIYSIANANHPFGQRPFRAPHHTASAIALVGGGSHPKpGEITL 290
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG-------GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR-LALAL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2552241993 291 AH---LGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRqitfpANFQLVAAMNP 344
Cdd:smart00382 74 ARklkPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSE-----KNLTVILTTND 125
|
|
| MCM6 |
cd17757 |
DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in ... |
286-487 |
1.41e-05 |
|
DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which 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.
Pssm-ID: 350663 [Multi-domain] Cd Length: 307 Bit Score: 46.98 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 286 GEITLAHLGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRQITFPANFQLVAAMNPCPCGYAFNQdsrcqcspeSIK 365
Cdd:cd17757 99 GALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPVGGRYDRSK---------SLK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 366 ryQN-RISGPLLDRIDLH---IDVPplqaqelqdNKPVENSetVRQRVIsayNIQIERQNALNMSLSPKQLEQY------ 435
Cdd:cd17757 170 --QNiNISAPIMSRFDLFfvlLDEC---------NEVTDYA--IASHIV---DLHSKREEAIEPPFTAEQLKRYiayart 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552241993 436 -AP-LDPPAQKMI-----ELAQQKLNLSARGYHRI--------LRVARTIADLNQSPDIQTGHLSEA 487
Cdd:cd17757 234 fKPkLTKEAKDELveqykELRQDDASGSTRSSYRItvrqleslIRLSEAIARLHCSDEVTPEHVEEA 300
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YifB |
COG0606 |
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ... |
3-492 |
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: 839.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 3 FAKIYTRGLLGLHAPLIEVEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSRLD 82
Cdd:COG0606 2 LARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 83 LPIALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQ-HQLILPSPNAQEASQLPDFQVFAANHLQ 161
Cdd:COG0606 82 LPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGiRRLIVPAANAAEAALVPGIEVYGASSLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 162 EVCAHLAQAETLPPFKTSPLDQHSFYKFDLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILPPLNTQ 241
Cdd:COG0606 162 EVVAFLRGEQPLPPAEPDAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 242 ENLEVASIYSIA----NANHPFGQRPFRAPHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLE 317
Cdd:COG0606 242 EALEVTAIHSVAgllpPDGGLIRRRPFRAPHHTASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 318 SKEIVISRASRQITFPANFQLVAAMNPCPCGYAFNQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVPPLQAQELQDNK 397
Cdd:COG0606 322 DGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGDPDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSAP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 398 PVENSETVRQRVISAYNIQIERQNA----LNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIADL 473
Cdd:COG0606 402 PGESSAEVRERVAAARERQLERFGGtgirLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIADL 481
|
490
....*....|....*....
gi 2552241993 474 NQSPDIQTGHLSEALSYRG 492
Cdd:COG0606 482 AGSERIEREHLAEALQYRR 500
|
|
| TIGR00368 |
TIGR00368 |
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ... |
6-491 |
0e+00 |
|
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: 582.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 6 IYTRGLLGLHAPLIEVEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSRLDLPI 85
Cdd:TIGR00368 1 VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 86 ALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQHQ-LILPSPNAQEASQLPDFQVFAANHLQEVC 164
Cdd:TIGR00368 81 AIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKfIIVPKENAEEASLIDGLNIYGADHLKEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 165 AHLAQAETLPP---FKTSPLDQHSF-YKFDLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILPPLNT 240
Cdd:TIGR00368 161 KFLEGSEKLPPrtnTKPKSIINKSYiIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 241 QENLEVASIYSIANANHPFG---QRPFRAPHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLE 317
Cdd:TIGR00368 241 EEAIETARIWSLVGKLIDRKqikQRPFRSPHHSASKPALVGGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 318 SKEIVISRASRQITFPANFQLVAAMNPCPCGYAFNQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVPPLQAQELQDNK 397
Cdd:TIGR00368 321 DGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGKNTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 398 PVENSETVRQRVISAYNIQIERQN-----ALNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIAD 472
Cdd:TIGR00368 401 SGESSAEVKQRVIKAREIQNIRYEkfaniNKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVARTIAD 480
|
490
....*....|....*....
gi 2552241993 473 LNQSPDIQTGHLSEALSYR 491
Cdd:TIGR00368 481 LKEEKNISREHLAEAIEYR 499
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
1-491 |
0e+00 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 538.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 1 MSFAKIYTRGLLGLHAPLIEVEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSR 80
Cdd:PRK09862 1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 81 LDLPIALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQHQLILPSPNAQEASQLPDFQVFAANHL 160
Cdd:PRK09862 81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLINGEGCLIADHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 161 QEVCAHL----AQAETLPPFKTSPLDQHsfykfDLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILP 236
Cdd:PRK09862 161 QAVCAFLegkhALERPKPTDAVSRALQH-----DLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 237 PLNTQENLEVASIYSIANA---NHPFGQRPFRAPHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLR 313
Cdd:PRK09862 236 DLSNEEALESAAILSLVNAesvQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 314 QPLESKEIVISRASRQITFPANFQLVAAMNPCPCGYAfnQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVP-PLQAQE 392
Cdd:PRK09862 316 EPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHY--QGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPlPPPGIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 393 LQDNKPVENSETVRQRVISAYNIQIERQNALNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIAD 472
Cdd:PRK09862 394 SKTVVPGESSATVKQRVMAARERQFKRQNKLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIAD 473
|
490
....*....|....*....
gi 2552241993 473 LNQSPDIQTGHLSEALSYR 491
Cdd:PRK09862 474 IDQSDIITRQHLQEAVSYR 492
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
190-393 |
2.26e-133 |
|
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: 384.19 E-value: 2.26e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 190 DLADVKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLASILPPLNTQENLEVASIYSIAN---ANHPFGQRPFRA 266
Cdd:pfam01078 1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGlggDGGLIRRRPFRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 267 PHHTASAIALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRQITFPANFQLVAAMNPCP 346
Cdd:pfam01078 81 PHHSASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPCP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2552241993 347 CGYAFNQDSRCQCSPESIKRYQNRISGPLLDRIDLHIDVPPLQAQEL 393
Cdd:pfam01078 161 CGYLGDPNKRCRCSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
21-142 |
1.14e-57 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 186.89 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 21 VEVHVSSGMPSLTIVGLPEAAVRESKDRVRSAILNSGFQFPTKRLTINLAPADLPKDGSRLDLPIALGILVASGQLPEnc 100
Cdd:pfam13541 1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFEFPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQIPV-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2552241993 101 TDDLEFIGELALDGQLRPVTGILSIAIACQQAQHQ-LILPSPN 142
Cdd:pfam13541 79 LEETIFLGELSLDGSLRPVRGALPIALAARKHGFRgLIVPKEN 121
|
|
| Mg_chelatase_C |
pfam13335 |
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative ... |
400-491 |
4.22e-40 |
|
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: 139.45 E-value: 4.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 400 ENSETVRQRVISAYNIQIERQNALNMSLSPKQLEQYAPLDPPAQKMIELAQQKLNLSARGYHRILRVARTIADLNQSPDI 479
Cdd:pfam13335 2 ESSAEVRERVAAARERQAERFGGENAQLPGRELRRFCRLDAAARALLERALERLGLSARAYDRILRVARTIADLAGSERI 81
|
90
....*....|..
gi 2552241993 480 QTGHLSEALSYR 491
Cdd:pfam13335 82 GREHLAEALQYR 93
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
213-348 |
3.65e-09 |
|
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: 54.99 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 213 SLLFRGPPGTGKTLLASRLASILpplnTQENLEVASIYSIANANHPFGQRPFRaphhtasaialvGGGSHPKPGEITLA- 291
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL----SNRPVFYVQLTRDTTEEDLFGRRNID------------PGGASWVDGPLVRAa 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2552241993 292 -HLGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRQITFPA-NFQLVAAMNPCPCG 348
Cdd:pfam07728 65 rEGEIAVLDEINRANPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRG 123
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
64-235 |
5.19e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 51.84 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 64 RLTINLAPADLPKDGSRLDLPIALGILVASGQLPENCTDDLEFIGELALDGQLRPVTGILSIAIACQQAQHQLILPSPNA 143
Cdd:COG0464 31 LALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 144 QEASQLPDFQVFAANHLQEVCAHLAQAETLPPFKTSPLDQHSFYKFD----LADVKGQLR-----PRRALEIAAAGGHS- 213
Cdd:COG0464 111 LLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDdlggLEEVKEELRelvalPLKRPELREEYGLPp 190
|
170 180
....*....|....*....|....*
gi 2552241993 214 ---LLFRGPPGTGKTLLASRLASIL 235
Cdd:COG0464 191 prgLLLYGPPGTGKTLLARALAGEL 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
211-344 |
4.34e-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: 46.60 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 211 GHSLLFRGPPGTGKTLLASRLASILPPLNtqenlevASIYSIANANHPFGQRPFRAPHHTASAIALVGGGSHPKpGEITL 290
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG-------GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR-LALAL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2552241993 291 AH---LGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRqitfpANFQLVAAMNP 344
Cdd:smart00382 74 ARklkPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSE-----KNLTVILTTND 125
|
|
| MCM6 |
cd17757 |
DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in ... |
286-487 |
1.41e-05 |
|
DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which 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.
Pssm-ID: 350663 [Multi-domain] Cd Length: 307 Bit Score: 46.98 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 286 GEITLAHLGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRQITFPANFQLVAAMNPCPCGYAFNQdsrcqcspeSIK 365
Cdd:cd17757 99 GALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPVGGRYDRSK---------SLK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 366 ryQN-RISGPLLDRIDLH---IDVPplqaqelqdNKPVENSetVRQRVIsayNIQIERQNALNMSLSPKQLEQY------ 435
Cdd:cd17757 170 --QNiNISAPIMSRFDLFfvlLDEC---------NEVTDYA--IASHIV---DLHSKREEAIEPPFTAEQLKRYiayart 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552241993 436 -AP-LDPPAQKMI-----ELAQQKLNLSARGYHRI--------LRVARTIADLNQSPDIQTGHLSEA 487
Cdd:cd17757 234 fKPkLTKEAKDELveqykELRQDDASGSTRSSYRItvrqleslIRLSEAIARLHCSDEVTPEHVEEA 300
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
211-387 |
3.25e-05 |
|
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: 44.06 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 211 GHSLLFRGPPGTGKTLLASRLASILPPLNtqenlevASIYSIaNANHpfgqrpFRAPHHTASAIALVGGGSHPKPGEitL 290
Cdd:cd00009 19 PKNLLLYGPPGTGKTTLARAIANELFRPG-------APFLYL-NASD------LLEGLVVAELFGHFLVRLLFELAE--K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 291 AHLGVLFLDELPEFDRKVLEVLRQpleskeiVISRASRQITFPANFQLVAAMNPcpcgyafnqdsrcqcspesikRYQNR 370
Cdd:cd00009 83 AKPGVLFIDEIDSLSRGAQNALLR-------VLETLNDLRIDRENVRVIGATNR---------------------PLLGD 134
|
170
....*....|....*..
gi 2552241993 371 ISGPLLDRIDLHIDVPP 387
Cdd:cd00009 135 LDRALYDRLDIRIVIPL 151
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
194-233 |
7.27e-05 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 43.04 E-value: 7.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2552241993 194 VKGQLRPRRALEIAAAGGHSLLFRGPPGTGKTLLASRLAS 233
Cdd:cd19481 9 VEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAG 48
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
201-341 |
1.36e-04 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 44.51 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 201 RRALEIA---AAGGHSLLFRGPPGTGKTLLASRLAsilpplntqenlevasiysianANHPFGQRPFRA------PHHTA 271
Cdd:COG3284 331 RRALRRArrlADRDIPVLILGETGTGKELFARAIH----------------------AASPRADGPFVAvncaaiPEELI 388
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552241993 272 SA-------IALVGGGSHPKPGEITLAHLGVLFLDELPEFDRKVLEVLRQPLESKEIVISRASRQItfPANFQLVAA 341
Cdd:COG3284 389 ESelfgyepGAFTGARRKGRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTPLGGTKPI--PVDVRLIAA 463
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
194-235 |
1.55e-04 |
|
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: 43.62 E-value: 1.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2552241993 194 VKGQLRPRRALEIA-AAGGHsLLFRGPPGTGKTLLASRLASIL 235
Cdd:COG0714 14 YVGQEELIELVLIAlLAGGH-LLLEGVPGVGKTTLAKALARAL 55
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
212-233 |
3.32e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 42.18 E-value: 3.32e-04
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
191-233 |
3.43e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 42.76 E-value: 3.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2552241993 191 LADVKGQ---LRPRRALEIAAAGG--HSLLFRGPPGTGKTLLASRLAS 233
Cdd:PRK13342 11 LDEVVGQehlLGPGKPLRRMIEAGrlSSMILWGPPGTGKTTLARIIAG 58
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
191-232 |
4.96e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 42.35 E-value: 4.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2552241993 191 LADVKGQ---LRPRRALEIAAAGG--HSLLFRGPPGTGKTLLASRLA 232
Cdd:COG2256 24 LDEVVGQehlLGPGKPLRRAIEAGrlSSMILWGPPGTGKTTLARLIA 70
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
191-235 |
6.46e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 41.92 E-value: 6.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2552241993 191 LADVKGQLR-----PRRALEIAAAGG----HSLLFRGPPGTGKTLLASRLASIL 235
Cdd:COG1222 83 LDEQIEEIReavelPLKNPELFRKYGieppKGVLLYGPPGTGKTLLAKAVAGEL 136
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
192-232 |
1.40e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 40.95 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2552241993 192 ADVKGQLRPRRALEIAAAGG---HSLLFRGPPGTGKTLLASRLA 232
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGrlaHAYLFTGPRGVGKTTLARILA 53
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
188-300 |
2.03e-03 |
|
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 188437 [Multi-domain] Cd Length: 557 Bit Score: 40.60 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 188 KFDLADVKGQL-----RPRRALEIAAAGGHsLLFRGPPGTGKTLLASRLASILPPLNTQENLEVASIysiananhpfgqr 262
Cdd:TIGR03922 285 KRQVAALKSSTamalaRAERGLPVAQTSNH-MLFAGPPGTGKTTIARVVAKIYCGLGVLRKPLVREV------------- 350
|
90 100 110
....*....|....*....|....*....|....*....
gi 2552241993 263 pfraphHTASAIALVGGGSHPKPGEITLAHL-GVLFLDE 300
Cdd:TIGR03922 351 ------SRADLIGQYIGESEAKTNEIIDSALgGVLFLDE 383
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
191-341 |
4.42e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 39.21 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 191 LADVKGQLRPRRALEIA--------AAGGHSLLFrGPPGTGKTLLASRLASILpplntQENLEVASiysiananhpfgqr 262
Cdd:TIGR00635 3 LAEFIGQEKVKEQLQLFieaakmrqEALDHLLLY-GPPGLGKTTLAHIIANEM-----GVNLKITS-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 263 pfraphhtasaialvgGGSHPKPGEIT--LAHL---GVLFLDELPEFDRKVLEVLRQPLESKE--IVISR--ASRQITFP 333
Cdd:TIGR00635 63 ----------------GPALEKPGDLAaiLTNLeegDVLFIDEIHRLSPAVEELLYPAMEDFRldIVIGKgpSARSVRLD 126
|
....*....
gi 2552241993 334 AN-FQLVAA 341
Cdd:TIGR00635 127 LPpFTLVGA 135
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
214-235 |
5.12e-03 |
|
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: 37.19 E-value: 5.12e-03
|
| MCM |
cd17706 |
MCM helicase family; MCM helicases are a family of helicases that play an important role in ... |
284-489 |
5.68e-03 |
|
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: 38.86 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 284 KPGEITLAHLGVLFLDEL---PEFDR-KVLEVlrqpLESKEIVISRASRQITFPANFQLVAAMNPcpcGYAFNQDSRcqc 359
Cdd:cd17706 97 EAGALVLADGGVCCIDEFdkmKELDRtALHEA----MEQQTISIAKAGIVTTLNARCSILAAANP---KGGRYNPKL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552241993 360 SP-ESIKryqnrISGPLLDRIDLhIDVpplqaqeLQDNKPVENSETVRQRVISAY-NIQIERQNALNMSLSPKQLE---- 433
Cdd:cd17706 167 SPiENIN-----LPSPLLSRFDL-IFV-------IRDDPDEERDEELAEHIIDLHrGSDPEEQVKPEEDGIPIDIEllrk 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2552241993 434 --QYAPLDPPaqKMIELAQQKLN-----------------LSARGYHRILRVARTIADLNQSPDIQTGHLSEALS 489
Cdd:cd17706 234 yiLYARQIHP--KISEEAREKLVrwyvelrkeserrstipITARQLESVIRLAEAHAKMRLSEVVTEEDVEEAIR 306
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
204-245 |
7.66e-03 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 37.37 E-value: 7.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2552241993 204 LEIAAAGGHSLLFRGPPGTGKTLLASRLASILPP----------------LNTQENLE 245
Cdd:pfam12775 24 LDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKekylplfinfsaqttsNQTQDIIE 81
|
|
| |
