|
Name |
Accession |
Description |
Interval |
E-value |
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
6-268 |
2.84e-136 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 387.19 E-value: 2.84e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 6 QEIINKAIEMKASDVHFIPVKNEVSIKFRINDNLEQYEQIGNSIYQKLLVYMKFQAGLDVSTQQVAQSGRYSYHFNKI-Y 84
Cdd:NF041000 1 EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYELNEQqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 85 FLRISTLPLSLGQESCVIRIVPQFFQQQKSTYKFNDFKHL---MNKKQGLLLFSGPTGSGKSTLMYQMVSyaNKALNLNV 161
Cdd:NF041000 81 SLRLSTVGDFLGRESLVIRLLYQLEQIKPQLFFPEQFQLLkqlLQRRSGLILFSGPTGSGKTTTMYSLAR--KLALNKQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 162 ISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAIL 241
Cdd:NF041000 159 ITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVIY 238
|
250 260
....*....|....*....|....*..
gi 577649004 242 RLLEMGISVQELIQATNLIINQRLVTT 268
Cdd:NF041000 239 RLLELGISKEELEQTLIGISYQRLIPT 265
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
4-266 |
2.26e-84 |
|
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442055 [Multi-domain] Cd Length: 561 Bit Score: 264.75 E-value: 2.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 4 LFQEIINKAIEMKASDVHFIPVKNEVSIKFRINDNLEQYEQIGNSIYQKLLVYMKFQAGLDVSTQQVAQSGRYSYHF-NK 82
Cdd:COG2804 182 LVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAPALVSRIKIMANLDIAERRLPQDGRIKLRLgGR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 83 IYFLRISTLPLSLGqESCVIRIvpqfFQQQKSTYKFND----------FKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSY 152
Cdd:COG2804 262 EIDLRVSTLPTVYG-EKVVLRI----LDKSAALLDLEQlgfspdqlerLRRLIRRPHGIILVTGPTGSGKTTTLYAALNE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 153 ANKAlNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLH 232
Cdd:COG2804 337 LNTP-ERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVGEIRDLETAEIAVQAALTGHLVLSTLH 415
|
250 260 270
....*....|....*....|....*....|....
gi 577649004 233 ATDCKGAILRLLEMGISVQELIQATNLIINQRLV 266
Cdd:COG2804 416 TNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLV 449
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
119-280 |
7.86e-78 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 234.69 E-value: 7.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 119 NDFKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKaLNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRC 198
Cdd:cd01129 1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNG-PERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 199 DPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAILRLLEMGISVQELIQATNLIINQRLVttikqQRQLVCE 278
Cdd:cd01129 80 DPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLV-----GRTAIAE 154
|
..
gi 577649004 279 IL 280
Cdd:cd01129 155 VL 156
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
8-266 |
1.65e-73 |
|
Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.
Pssm-ID: 425681 [Multi-domain] Cd Length: 269 Bit Score: 227.55 E-value: 1.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 8 IINKAIEMKASDVHFIPVKNEVSIKFRINDNLEQYEQIGNSIYQKLLVYMKFQAGLDVSTQQVAQSGRYSYHFN-KIYFL 86
Cdd:pfam00437 3 IPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRIGgKGVRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 87 RISTLPLSLGqESCVIRIVPQF-----FQQQKSTYKF-NDFKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKAlNLN 160
Cdd:pfam00437 83 RVSTLPTAGG-EKLVIRLLDPSnvalsLDELGMTGAQdEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTR-DEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 161 VISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAI 240
Cdd:pfam00437 161 IVTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGAL 240
|
250 260
....*....|....*....|....*.
gi 577649004 241 LRLLEMGISVQELIQATNLIINQRLV 266
Cdd:pfam00437 241 TRLQDMGVPPFELASSLLLVIAQRLV 266
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
7-266 |
6.19e-54 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 182.82 E-value: 6.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 7 EIINK----AIEMKASDVHFIPVKNEVSIKFRINDNLEQY----EQIGNSIYQKLlvymKFQAGLDVSTQQVAQSGRYSY 78
Cdd:PRK10436 86 QLINQtlqsALQKRASDIHFEPAQNHYRIRLRIDGVLHPLpdpsPELGAALTARL----KVLGNLDIAERRLPQDGQFTV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 79 HFNKI-YFLRISTLPLSLGqESCVIRIVPQffQQQK--------STYKFNDFKHLMNKKQGLLLFSGPTGSGKSTLMYQM 149
Cdd:PRK10436 162 ELAGNaYSFRIATLPCRGG-EKVVLRLLQQ--VQQAldletlgmTPAQLAQFRQALQQPQGLILVTGPTGSGKTVTLYSA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 150 VSYANKAlNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLT 229
Cdd:PRK10436 239 LQTLNTA-QINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLS 317
|
250 260 270
....*....|....*....|....*....|....*..
gi 577649004 230 TLHATDCKGAILRLLEMGISVQELIQATNLIINQRLV 266
Cdd:PRK10436 318 TLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLV 354
|
|
| pilT_fam |
TIGR01420 |
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ... |
5-280 |
4.87e-37 |
|
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation. [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]
Pssm-ID: 273613 Cd Length: 343 Bit Score: 135.53 E-value: 4.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 5 FQEIINKAIEMKASDVH----FIPVknevsikFRINDNLE--QYEQIGNSIYQKLLVYM---------KFQAGLDVSTQq 69
Cdd:TIGR01420 2 LEEILREAVKLGASDIHltagAPPA-------MRIDGDLVriEFEPLTPEDTQKLAREIlsekqreefEENGELDFSFS- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 70 VAQSGRysyhfnkiyfLRISTLpLSLGQESCVIRIVPQFFQQQKSTYKFNDFKHLMNKKQGLLLFSGPTGSGKSTLMYQM 149
Cdd:TIGR01420 74 LPGVGR----------FRVNAF-YQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLASM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 150 VSYANKALNLNVISIEDPVEMQIPGIVQINVNDKAGI---NYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHL 226
Cdd:TIGR01420 143 IDYINKNKAYHIITIEDPIEYVHTNKRSLINQREVGEdtlSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577649004 227 VLTTLHATDCKGAILRLLEM-GISVQELIQ---ATNL--IINQRLVTTIKQQ-RQLVCEIL 280
Cdd:TIGR01420 223 VFGTLHTNSAAQTIERIIDVfPAEEQEQIRtqlAESLvaIISQRLLPKADGGgRVLAVEIL 283
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
128-208 |
2.06e-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: 38.12 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 128 KQGLLLFSGPTGSGKSTLMYQMVSYANKAlNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAI-------LRCDP 200
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlalalaRKLKP 79
|
....*...
gi 577649004 201 DVILIGEI 208
Cdd:smart00382 80 DVLILDEI 87
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
6-268 |
2.84e-136 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 387.19 E-value: 2.84e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 6 QEIINKAIEMKASDVHFIPVKNEVSIKFRINDNLEQYEQIGNSIYQKLLVYMKFQAGLDVSTQQVAQSGRYSYHFNKI-Y 84
Cdd:NF041000 1 EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYELNEQqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 85 FLRISTLPLSLGQESCVIRIVPQFFQQQKSTYKFNDFKHL---MNKKQGLLLFSGPTGSGKSTLMYQMVSyaNKALNLNV 161
Cdd:NF041000 81 SLRLSTVGDFLGRESLVIRLLYQLEQIKPQLFFPEQFQLLkqlLQRRSGLILFSGPTGSGKTTTMYSLAR--KLALNKQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 162 ISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAIL 241
Cdd:NF041000 159 ITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVIY 238
|
250 260
....*....|....*....|....*..
gi 577649004 242 RLLEMGISVQELIQATNLIINQRLVTT 268
Cdd:NF041000 239 RLLELGISKEELEQTLIGISYQRLIPT 265
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
4-266 |
2.26e-84 |
|
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442055 [Multi-domain] Cd Length: 561 Bit Score: 264.75 E-value: 2.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 4 LFQEIINKAIEMKASDVHFIPVKNEVSIKFRINDNLEQYEQIGNSIYQKLLVYMKFQAGLDVSTQQVAQSGRYSYHF-NK 82
Cdd:COG2804 182 LVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAPALVSRIKIMANLDIAERRLPQDGRIKLRLgGR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 83 IYFLRISTLPLSLGqESCVIRIvpqfFQQQKSTYKFND----------FKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSY 152
Cdd:COG2804 262 EIDLRVSTLPTVYG-EKVVLRI----LDKSAALLDLEQlgfspdqlerLRRLIRRPHGIILVTGPTGSGKTTTLYAALNE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 153 ANKAlNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLH 232
Cdd:COG2804 337 LNTP-ERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVGEIRDLETAEIAVQAALTGHLVLSTLH 415
|
250 260 270
....*....|....*....|....*....|....
gi 577649004 233 ATDCKGAILRLLEMGISVQELIQATNLIINQRLV 266
Cdd:COG2804 416 TNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLV 449
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
119-280 |
7.86e-78 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 234.69 E-value: 7.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 119 NDFKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKaLNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRC 198
Cdd:cd01129 1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNG-PERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 199 DPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAILRLLEMGISVQELIQATNLIINQRLVttikqQRQLVCE 278
Cdd:cd01129 80 DPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLV-----GRTAIAE 154
|
..
gi 577649004 279 IL 280
Cdd:cd01129 155 VL 156
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
8-266 |
1.65e-73 |
|
Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.
Pssm-ID: 425681 [Multi-domain] Cd Length: 269 Bit Score: 227.55 E-value: 1.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 8 IINKAIEMKASDVHFIPVKNEVSIKFRINDNLEQYEQIGNSIYQKLLVYMKFQAGLDVSTQQVAQSGRYSYHFN-KIYFL 86
Cdd:pfam00437 3 IPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRIGgKGVRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 87 RISTLPLSLGqESCVIRIVPQF-----FQQQKSTYKF-NDFKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKAlNLN 160
Cdd:pfam00437 83 RVSTLPTAGG-EKLVIRLLDPSnvalsLDELGMTGAQdEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTR-DEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 161 VISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAI 240
Cdd:pfam00437 161 IVTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGAL 240
|
250 260
....*....|....*....|....*.
gi 577649004 241 LRLLEMGISVQELIQATNLIINQRLV 266
Cdd:pfam00437 241 TRLQDMGVPPFELASSLLLVIAQRLV 266
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
7-266 |
6.19e-54 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 182.82 E-value: 6.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 7 EIINK----AIEMKASDVHFIPVKNEVSIKFRINDNLEQY----EQIGNSIYQKLlvymKFQAGLDVSTQQVAQSGRYSY 78
Cdd:PRK10436 86 QLINQtlqsALQKRASDIHFEPAQNHYRIRLRIDGVLHPLpdpsPELGAALTARL----KVLGNLDIAERRLPQDGQFTV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 79 HFNKI-YFLRISTLPLSLGqESCVIRIVPQffQQQK--------STYKFNDFKHLMNKKQGLLLFSGPTGSGKSTLMYQM 149
Cdd:PRK10436 162 ELAGNaYSFRIATLPCRGG-EKVVLRLLQQ--VQQAldletlgmTPAQLAQFRQALQQPQGLILVTGPTGSGKTVTLYSA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 150 VSYANKAlNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLT 229
Cdd:PRK10436 239 LQTLNTA-QINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLS 317
|
250 260 270
....*....|....*....|....*....|....*..
gi 577649004 230 TLHATDCKGAILRLLEMGISVQELIQATNLIINQRLV 266
Cdd:PRK10436 318 TLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLV 354
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
1-280 |
1.94e-43 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 152.17 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 1 MKILFQEIINKAIEMKASDVHFIPvkNEVsIKFRINDNL----------EQYEQIGNSIY---QKLlvymKFQAGLDVST 67
Cdd:COG2805 1 MAMDLDELLKLAVEQGASDLHLTV--GSP-PMLRIDGELvplddppltpEDLEALLKEILteeQRE----RLEEEGELDF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 68 qqvaqsgrySYHFNKIYFLRISTLpLSLGQESCVIRIVPQffqQQKSTYKFN---DFKHLMNKKQGLLLFSGPTGSGKST 144
Cdd:COG2805 74 ---------SYSLPGLGRFRVNIF-RQRGGVAAVLRLIPS---EIPTLEELGlppVLKELAELPRGLVLVTGPTGSGKST 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 145 LMYQMVSYANKALNLNVISIEDPVEMQIPG----IVQINVndkaGINyVNSF----KAILRCDPDVILIGEIRDKDVAKC 216
Cdd:COG2805 141 TLAAMIDYINETRAKHIITIEDPIEFVHKHkkslINQREV----GRD-TPSFanalRAALREDPDVILVGEMRDLETIEA 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577649004 217 VIQASLSGHLVLTTLHATDCKGAILRLLEM-------GISVQeLIQATNLIINQRLVTTI-KQQRQLVCEIL 280
Cdd:COG2805 216 ALTAAETGHLVFATLHTNSAAQTIDRIIDVfppeeqaQIRSQ-LAESLRGVISQRLLPRAdGGGRVAAREIL 286
|
|
| pilT_fam |
TIGR01420 |
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ... |
5-280 |
4.87e-37 |
|
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation. [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]
Pssm-ID: 273613 Cd Length: 343 Bit Score: 135.53 E-value: 4.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 5 FQEIINKAIEMKASDVH----FIPVknevsikFRINDNLE--QYEQIGNSIYQKLLVYM---------KFQAGLDVSTQq 69
Cdd:TIGR01420 2 LEEILREAVKLGASDIHltagAPPA-------MRIDGDLVriEFEPLTPEDTQKLAREIlsekqreefEENGELDFSFS- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 70 VAQSGRysyhfnkiyfLRISTLpLSLGQESCVIRIVPQFFQQQKSTYKFNDFKHLMNKKQGLLLFSGPTGSGKSTLMYQM 149
Cdd:TIGR01420 74 LPGVGR----------FRVNAF-YQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLASM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 150 VSYANKALNLNVISIEDPVEMQIPGIVQINVNDKAGI---NYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHL 226
Cdd:TIGR01420 143 IDYINKNKAYHIITIEDPIEYVHTNKRSLINQREVGEdtlSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577649004 227 VLTTLHATDCKGAILRLLEM-GISVQELIQ---ATNL--IINQRLVTTIKQQ-RQLVCEIL 280
Cdd:TIGR01420 223 VFGTLHTNSAAQTIERIIDVfPAEEQEQIRtqlAESLvaIISQRLLPKADGGgRVLAVEIL 283
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
121-280 |
6.91e-37 |
|
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 131.89 E-value: 6.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 121 FKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKALNLNVISIEDPVEMqipgivqINVNDKAGINY------VNSF-- 192
Cdd:cd01131 13 LKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINETRSKHIITIEDPIEF-------VHKHKKSLINQrevgrdTESFaa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 193 --KAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAILRLLEM-GISVQELIQ---ATNL--IINQR 264
Cdd:cd01131 86 alRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDVfPPEQQEQVRiqlASSLrgVISQR 165
|
170
....*....|....*..
gi 577649004 265 LVTTIKQQ-RQLVCEIL 280
Cdd:cd01131 166 LLPKKDGGgRVAAFEIL 182
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
128-280 |
6.47e-28 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 106.69 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 128 KQGLLLFSGPTGSGKSTLMYQMVSYA--NKALNLNVISIEDPVEM---QIPGIVQINVNDKAGINYVNSFKAI---LRCD 199
Cdd:cd19516 10 REGLVYVAGATGSGKSTLLAAIYRYIleNDPPDRKIITYEDPIEFvydGIKSKHSIIVQSQIPRHFKSFAKAVreaLRRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 200 PDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAILRLLEMGISVQ------ELIQATNLIINQRLVTTIKQQR 273
Cdd:cd19516 90 PSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLFPPEErdaaayDLLSTLRFIIVQRLVRTTDGKR 169
|
....*..
gi 577649004 274 QLVCEIL 280
Cdd:cd19516 170 VAVREYL 176
|
|
| PilU |
COG5008 |
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures]; |
122-280 |
1.02e-26 |
|
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
Pssm-ID: 444032 Cd Length: 370 Bit Score: 107.88 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 122 KHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKALNLNVISIEDPVEMQIP---GIV-QINVndkaGI---NYVNSFKA 194
Cdd:COG5008 116 KDLIMEKRGLVLFVGATGSGKSTTLAAMIDHRNENSSGHILTIEDPIEFVHKhkkSIVtQREV----GVdteSYEVALKN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 195 ILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAILRLLE-----------MGISVqeliqatNL--II 261
Cdd:COG5008 192 ALRQAPDVILIGEIRDRETMEHAIAFAETGHLCLATLHANNANQALDRIINffpeerrpqllMDLSL-------NLraIV 264
|
170
....*....|....*....
gi 577649004 262 NQRLVTTIKQQRQLVCEIL 280
Cdd:COG5008 265 SQRLVPTKDGGRVAAVEVL 283
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
119-271 |
9.55e-25 |
|
type II/type IV hexameric secretion ATPases; 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: 410885 [Multi-domain] Cd Length: 168 Bit Score: 98.23 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 119 NDFKHLMnKKQGLLLFSGPTGSGKSTLMYQMVSYANKalNLNVISIEDPVEMQIP---GIVQINVNDKagINYVNSFKAI 195
Cdd:cd19477 1 SAIKDGI-AIGKNVIVCGGTGSGKTTYIKSILEFIPK--EERIISIEDTEEIVFKhhkNYTQLFFGGN--ITSADCLKSC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 196 LRCDPDVILIGEIRDKDvAKCVIQASLSGH-LVLTTLHATDCKGAILRLLEMGISVQ-----------ELIQAT-NLIIN 262
Cdd:cd19477 76 LRQRPDRIILGELRSSE-AYDFYNVLCSGHkGTLTTLHAGSSEEAFIRLAN*SSSNSaarnikfesliEGFKDLiDGIVH 154
|
....*....
gi 577649004 263 QRLVTTIKQ 271
Cdd:cd19477 155 INHHKQCDE 163
|
|
| plasmid_TraJ |
TIGR02525 |
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ... |
99-286 |
9.30e-21 |
|
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524). [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 131577 [Multi-domain] Cd Length: 372 Bit Score: 91.40 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 99 SCVIRIVPQFFQQQKSTYKFNDFKHLMNKKQGLLLFSGPTGSGKSTLMYQMVSYANKAL-NLNVISIEDPVEMQIPGIVQ 177
Cdd:TIGR02525 119 SLTLRVIPSDIPDLKQMGIEPDLFNSLLPAAGLGLICGETGSGKSTLAASIYQHCGETYpDRKIVTYEDPIEYILGSPDD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 178 INVNDKAGI-----NYVNSFKAILRCDPDVILIGEIRDKDVAKCVIQASLSGHLVLTTLHATDCKGAILRLLEMGIS--- 249
Cdd:TIGR02525 199 LLPPAQSQIgrdvdSFANGIRLALRRAPKIIGVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSPGEAISRCLQMYPPemr 278
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 577649004 250 ---VQELIQATNLIINQRLVTTIKQQRQLVCE-ILSQQQLR 286
Cdd:TIGR02525 279 eaaAFDLLSILQYIIVQRLLRTTDGKRQAVREyIVFDDSLR 319
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
132-268 |
4.86e-19 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 87.44 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 132 LLFSGPTGSGKSTLM---YQMVSYANKalnlnVISIEDPVEMQIPGivqinvndKAGINYV--NSF-------------K 193
Cdd:COG0630 293 VLVAGGTASGKTTLLnalLSFIPPDAK-----IVTIEDTRELNLPH--------ENWISLVtrESFggeegdvtmfdllK 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577649004 194 AILRCDPDVILIGEIRDKDvAKCVIQASLSGHLVLTTLHATDCKGAILRLLEMGISV-QELIQATNLIINQRLVTT 268
Cdd:COG0630 360 AALRQRPDYIVVGEVRGEE-AYTLFQAMATGHGVLSTFHADSVESAINRLTSPPINVpRTLLQALDLVVFQKRVRV 434
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
133-269 |
2.95e-18 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 80.66 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 133 LFSGPTGSGKSTLMYQMVSYANKalNLNVISIEDPVEMQIPG--IVQI----NVNDKAGINYVNSFKAILRCDPDVILIG 206
Cdd:cd01130 16 LISGGTGSGKTTLLNALLSFIPP--DERIVTIEDTRELQLPHpnVVHLltrpGGGEKGEVTMADLLKAALRMRPDRIIVG 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577649004 207 EIRDKDvAKCVIQASLSGHL-VLTTLHATDCKGAILRLLEMGIsvQELIQATNLIINQRLVTTI 269
Cdd:cd01130 94 EVRGGE-AYDMLQAMNTGHPgSITTIHANSAEDAIDRLATLVL--EAGVNLDEEALRRLIASAI 154
|
|
| PRK13851 |
PRK13851 |
type IV secretion system protein VirB11; Provisional |
132-235 |
1.13e-09 |
|
type IV secretion system protein VirB11; Provisional
Pssm-ID: 172375 Cd Length: 344 Bit Score: 58.76 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 132 LLFSGPTGSGKSTLMYQMVSYANKALNLnvISIEDPVEMQIPGIVQINV---NDKAGINYVNS---FKAILRCDPDVILI 205
Cdd:PRK13851 165 MLLCGPTGSGKTTMSKTLISAIPPQERL--ITIEDTLELVIPHENHVRLlysKNGAGLGAVTAehlLQASLRMRPDRILL 242
|
90 100 110
....*....|....*....|....*....|.
gi 577649004 206 GEIRDkDVAKCVIQASLSGHL-VLTTLHATD 235
Cdd:PRK13851 243 GEMRD-DAAWAYLSEVVSGHPgSISTIHGAN 272
|
|
| PRK13833 |
PRK13833 |
conjugal transfer protein TrbB; Provisional |
132-261 |
6.32e-07 |
|
conjugal transfer protein TrbB; Provisional
Pssm-ID: 172360 [Multi-domain] Cd Length: 323 Bit Score: 50.18 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 132 LLFSGPTGSGKSTLMYQMVS-YANKALNLNVISIEDPVEMQIPG--IVQINVNDKAGINYVnsFKAILRCDPDVILIGEI 208
Cdd:PRK13833 147 IVISGGTGSGKTTLANAVIAeIVASAPEDRLVILEDTAEIQCAAenAVALHTSDTVDMARL--LKSTMRLRPDRIIVGEV 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 209 RDkDVAKCVIQASLSGHL-VLTTLHATDCKGAILRLLEMGISV-----QELI-QATNLII 261
Cdd:PRK13833 225 RD-GAALTLLKAWNTGHPgGVTTIHSNTAMSALRRLEQLTAEAsqqpmQEVIgEAVDLIV 283
|
|
| PRK13894 |
PRK13894 |
conjugal transfer ATPase TrbB; Provisional |
132-243 |
1.02e-06 |
|
conjugal transfer ATPase TrbB; Provisional
Pssm-ID: 184377 Cd Length: 319 Bit Score: 49.74 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 132 LLFSGPTGSGKSTL----MYQMVSYANkalNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAILRCDPDVILIGE 207
Cdd:PRK13894 151 ILVIGGTGSGKTTLvnaiINEMVIQDP---TERVFIIEDTGEIQCAAENYVQYHTSIDVNMTALLKTTLRMRPDRILVGE 227
|
90 100 110
....*....|....*....|....*....|....*..
gi 577649004 208 IRDKDvAKCVIQASLSGHL-VLTTLHATDCKGAILRL 243
Cdd:PRK13894 228 VRGPE-ALDLLMAWNTGHEgGAATLHANNAKAGLDRL 263
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
129-163 |
1.40e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.42 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|....*..
gi 577649004 129 QGLLLFSGPTGSGKSTLM--YQMVSYANKALNLNVIS 163
Cdd:pfam13555 22 RGNTLLTGPSGSGKSTLLdaIQTLLVPAKRARFNKAA 58
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
128-208 |
2.06e-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: 38.12 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577649004 128 KQGLLLFSGPTGSGKSTLMYQMVSYANKAlNLNVISIEDPVEMQIPGIVQINVNDKAGINYVNSFKAI-------LRCDP 200
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP-GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLrlalalaRKLKP 79
|
....*...
gi 577649004 201 DVILIGEI 208
Cdd:smart00382 80 DVLILDEI 87
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
132-208 |
9.00e-03 |
|
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: 36.36 E-value: 9.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577649004 132 LLFSGPTGSGKSTLMyQMVSYANKALNLNVISIEDPVEMQIPgivqINVNDKAGINYVNSFKAILRCDPDVILIGEI 208
Cdd:cd00009 22 LLLYGPPGTGKTTLA-RAIANELFRPGAPFLYLNASDLLEGL----VVAELFGHFLVRLLFELAEKAKPGVLFIDEI 93
|
|
| |
