|
Name |
Accession |
Description |
Interval |
E-value |
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
8-487 |
0e+00 |
|
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: 693.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 8 PASWALAQRIGYLYSEGEIIYLA---DTPFERLLDIQRQVGQCQTMTSLSQADFEARLEAvFHQNTGESQQIAQDIDQSv 84
Cdd:COG2804 82 PEELARRHRVLPLRLEGGTLTVAmadPLDLEALDELRRLTGRPVEPVVATESDIERALDR-LYGSESSIEELLEELAED- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 85 dllsLSEEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRI 164
Cdd:COG2804 160 ----LTSEEEDLEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAPALVSRI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 165 KVMARLDIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGI 244
Cdd:COG2804 236 KIMANLDIAERRLPQDGRIKLRLGGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLIRRPHGI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTE 324
Cdd:COG2804 316 ILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVGEIRDLE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 325 TAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFTPVSPQQAQM--FKYH 402
Cdd:COG2804 396 TAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELERlgLPPE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 403 QLAVTTIGTPVGCPHCHQSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEV 481
Cdd:COG2804 476 ELAPLTFYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEgMRTLREDGLEKVLQGITTLEEV 555
|
....*.
gi 1743360309 482 MRVASA 487
Cdd:COG2804 556 LRVTGE 561
|
|
| type_II_gspE |
TIGR02533 |
type II secretion system protein E; This family describes GspE, the E protein of the type II ... |
8-484 |
0e+00 |
|
type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 131585 [Multi-domain] Cd Length: 486 Bit Score: 631.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 8 PASWALAQRIGYLYSEGE---IIYLADTPFERLLDIQRQVGQCQTMTSLSQADFEARLEAVFHQNTGESQQIAQDIDQSV 84
Cdd:TIGR02533 5 PIGFAKQSRVLPLSEHDGtlvVAVSDPLDLAALDEVRRLFGAPVQLIIATASEIDDAINSVYARTGSAAAQIVEEIEGED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 85 DLLSLSEEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRI 164
Cdd:TIGR02533 85 DLSALELDEPKIEDLLDLEDDAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRFRVDGVLRDVLSPPKKLHAALVSRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 165 KVMARLDIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGI 244
Cdd:TIGR02533 165 KIMAKLNIAEKRLPQDGRISLRVGGRDIDIRVSTVPTSHGERVVMRLLDKTAVRLDLETLGMSPELLSRFERLIRRPHGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTE 324
Cdd:TIGR02533 245 ILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPVEYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMVGEIRDLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 325 TAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFTPVSPQQAQMFKYHQL 404
Cdd:TIGR02533 325 TAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIALFGISPE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 405 AVTTIGTPVGCPHCHQSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEVMR 483
Cdd:TIGR02533 405 GPINLYRPVGCPHCNHTGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAgMRTLRDDGLRKVLAGITTIEEVLR 484
|
.
gi 1743360309 484 V 484
Cdd:TIGR02533 485 V 485
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
91-484 |
7.27e-158 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 456.31 E-value: 7.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 91 EEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARL 170
Cdd:PRK10436 67 QRTQQTLPVADQEKDTPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAALTARLKVLGNL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 171 DIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGIILVTGP 250
Cdd:PRK10436 147 DIAERRLPQDGQFTVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQFRQALQQPQGLILVTGP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 251 TGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAV 330
Cdd:PRK10436 227 TGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 331 QASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFT--PVSPQQA--QMFKYHQLAv 406
Cdd:PRK10436 307 KAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLVRKLCPHCRQQAsePIHLPPNiwPGPLPHWQA- 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743360309 407 ttigtpVGCPHCHqSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEVMRV 484
Cdd:PRK10436 386 ------VGCEHCY-HGYYGRTALFEVLPITPVLQQAIASNASPEELETHARQQgMTTLFENGLLAVEQGLTTLEELYRV 457
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
113-381 |
5.15e-147 |
|
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: 421.31 E-value: 5.15e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 113 NAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARLDIAEKRIPQDGRISLRIGRRNI 192
Cdd:pfam00437 1 NLIPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRIGGKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 193 DVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALNTPGRN 272
Cdd:pfam00437 81 RVRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 273 ILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAV 352
Cdd:pfam00437 161 IVTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGAL 240
|
250 260
....*....|....*....|....*....
gi 1743360309 353 TRLRDMGVESFLLSSSLAGIIAQRLVRRL 381
Cdd:pfam00437 241 TRLQDMGVPPFELASSLLLVIAQRLVRKL 269
|
|
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
113-378 |
3.86e-100 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 301.67 E-value: 3.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 113 NAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARLDIAEKRIPQDGRISLRIGRRNI 192
Cdd:NF041000 1 EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYELNEQQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 193 DVRVSTLPSIYG-ERAVLRLL-DKNSLQLSLNNlgmtAADKQDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALnTPG 270
Cdd:NF041000 81 SLRLSTVGDFLGrESLVIRLLyQLEQIKPQLFF----PEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSLARKL-ALN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 271 RNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASG 350
Cdd:NF041000 156 KQVITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAG 235
|
250 260
....*....|....*....|....*...
gi 1743360309 351 AVTRLRDMGVESFLLSSSLAGIIAQRLV 378
Cdd:NF041000 236 VIYRLLELGISKEELEQTLIGISYQRLI 263
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
232-380 |
1.26e-91 |
|
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: 275.90 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 232 QDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQD 311
Cdd:cd01129 1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743360309 312 PDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRR 380
Cdd:cd01129 81 PDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLVGR 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
241-320 |
3.27e-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: 46.98 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 241 PHGIILVTGPTGSGKSTTLYAILSALNTPGRNILTV--EDPVEYELEGIGQTQVNTRVDMSF----ARGLRAILRQ-DPD 313
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIdgEDILEEVLDQLLLIIVGGKKASGSgelrLRLALALARKlKPD 80
|
....*..
gi 1743360309 314 VVMVGEI 320
Cdd:smart00382 81 VLILDEI 87
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
8-487 |
0e+00 |
|
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: 693.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 8 PASWALAQRIGYLYSEGEIIYLA---DTPFERLLDIQRQVGQCQTMTSLSQADFEARLEAvFHQNTGESQQIAQDIDQSv 84
Cdd:COG2804 82 PEELARRHRVLPLRLEGGTLTVAmadPLDLEALDELRRLTGRPVEPVVATESDIERALDR-LYGSESSIEELLEELAED- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 85 dllsLSEEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRI 164
Cdd:COG2804 160 ----LTSEEEDLEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAPALVSRI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 165 KVMARLDIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGI 244
Cdd:COG2804 236 KIMANLDIAERRLPQDGRIKLRLGGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLIRRPHGI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTE 324
Cdd:COG2804 316 ILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVGEIRDLE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 325 TAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFTPVSPQQAQM--FKYH 402
Cdd:COG2804 396 TAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELERlgLPPE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 403 QLAVTTIGTPVGCPHCHQSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEV 481
Cdd:COG2804 476 ELAPLTFYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEgMRTLREDGLEKVLQGITTLEEV 555
|
....*.
gi 1743360309 482 MRVASA 487
Cdd:COG2804 556 LRVTGE 561
|
|
| type_II_gspE |
TIGR02533 |
type II secretion system protein E; This family describes GspE, the E protein of the type II ... |
8-484 |
0e+00 |
|
type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 131585 [Multi-domain] Cd Length: 486 Bit Score: 631.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 8 PASWALAQRIGYLYSEGE---IIYLADTPFERLLDIQRQVGQCQTMTSLSQADFEARLEAVFHQNTGESQQIAQDIDQSV 84
Cdd:TIGR02533 5 PIGFAKQSRVLPLSEHDGtlvVAVSDPLDLAALDEVRRLFGAPVQLIIATASEIDDAINSVYARTGSAAAQIVEEIEGED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 85 DLLSLSEEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRI 164
Cdd:TIGR02533 85 DLSALELDEPKIEDLLDLEDDAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRFRVDGVLRDVLSPPKKLHAALVSRV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 165 KVMARLDIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGI 244
Cdd:TIGR02533 165 KIMAKLNIAEKRLPQDGRISLRVGGRDIDIRVSTVPTSHGERVVMRLLDKTAVRLDLETLGMSPELLSRFERLIRRPHGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTE 324
Cdd:TIGR02533 245 ILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPVEYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMVGEIRDLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 325 TAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFTPVSPQQAQMFKYHQL 404
Cdd:TIGR02533 325 TAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIALFGISPE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 405 AVTTIGTPVGCPHCHQSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEVMR 483
Cdd:TIGR02533 405 GPINLYRPVGCPHCNHTGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAgMRTLRDDGLRKVLAGITTIEEVLR 484
|
.
gi 1743360309 484 V 484
Cdd:TIGR02533 485 V 485
|
|
| type_IV_pilB |
TIGR02538 |
type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus ... |
20-487 |
3.62e-172 |
|
type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus biogenesis designated PilB in Pseudomonas aeruginosa but PilF in Neisseria gonorrhoeae; the more common usage, reflected here, is PilB. This protein is an ATPase involved in protein export for pilin assembly and is closely related to GspE (TIGR02533) of type II secretion, also called the main terminal branch of the general secretion pathway. Note that type IV pilus systems are often divided into type IV-A and IV-B, with the latter group including bundle-forming pilus, mannose-sensitive hemagglutinin, etc. Members of this family are found in type IV-A systems. [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274186 [Multi-domain] Cd Length: 564 Bit Score: 496.46 E-value: 3.62e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 20 LYSEGEIIYLA---DTPFERLLDIQRQVGqCQTMTSLSQAD-FEARLEAVFHQNTGESQQIAQD---IDQSVDLLSLSEE 92
Cdd:TIGR02538 87 LFKRGNTLFVAvsdPTNISALDDIRFATG-LNVEVVIVEEDkLSALIEKYYGGSDSLAKELGDEdigDLEELDVDAIDDE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 93 MPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARLDI 172
Cdd:TIGR02538 166 GPDDIEQDAVDDDAPIVKFVNKILLDAIRKGASDIHFEPYEKSYRVRFRIDGILHEVAQPPLALANRIAARIKVMSRLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 173 AEKRIPQDGRISLRIGR-RNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGIILVTGPT 251
Cdd:TIGR02538 246 AEKRIPQDGRIKLKLSKsKAIDFRVSTLPTLFGEKVVLRILDSSAAQLDIDKLGFEPDQKALFLEAIHKPQGMVLVTGPT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 252 GSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQ 331
Cdd:TIGR02538 326 GSGKTVSLYTALNILNTEEVNISTAEDPVEINLPGINQVNVNPKIGLTFAAALRSFLRQDPDIIMVGEIRDLETAEIAIK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 332 ASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFTPVSPQQ--AQMFKYHQLAVTTI 409
Cdd:TIGR02538 406 AAQTGHLVLSTLHTNDAPETLARLVNMGIAPFNIASSVNLIMAQRLARRLCSHCKAPEEVPAEAllELGFTQEDLADLKL 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743360309 410 GTPVGCPHCHQSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEVMRVASA 487
Cdd:TIGR02538 486 YGPVGCDECSNTGYKGRVGIYEVMPMSEEIAELILKGGNALQIAELAQKEgMRTLRRSGLLKVKQGVTSLEEVLRVTVD 564
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
91-484 |
7.27e-158 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 456.31 E-value: 7.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 91 EEMPANEDLLNEDSAAPVIRLINAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARL 170
Cdd:PRK10436 67 QRTQQTLPVADQEKDTPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAALTARLKVLGNL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 171 DIAEKRIPQDGRISLRIGRRNIDVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGIILVTGP 250
Cdd:PRK10436 147 DIAERRLPQDGQFTVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQFRQALQQPQGLILVTGP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 251 TGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAV 330
Cdd:PRK10436 227 TGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 331 QASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRRLCPQCRQFT--PVSPQQA--QMFKYHQLAv 406
Cdd:PRK10436 307 KAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLVRKLCPHCRQQAsePIHLPPNiwPGPLPHWQA- 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743360309 407 ttigtpVGCPHCHqSGYQGRMAIHEMMVVTPELRAAIHENVDEQALERLVRQQ-HKALIKNGLQKVISGDTSWDEVMRV 484
Cdd:PRK10436 386 ------VGCEHCY-HGYYGRTALFEVLPITPVLQQAIASNASPEELETHARQQgMTTLFENGLLAVEQGLTTLEELYRV 457
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
113-381 |
5.15e-147 |
|
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: 421.31 E-value: 5.15e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 113 NAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARLDIAEKRIPQDGRISLRIGRRNI 192
Cdd:pfam00437 1 NLIPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRIGGKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 193 DVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLGMTAADKQDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALNTPGRN 272
Cdd:pfam00437 81 RVRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 273 ILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAV 352
Cdd:pfam00437 161 IVTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGAL 240
|
250 260
....*....|....*....|....*....
gi 1743360309 353 TRLRDMGVESFLLSSSLAGIIAQRLVRRL 381
Cdd:pfam00437 241 TRLQDMGVPPFELASSLLLVIAQRLVRKL 269
|
|
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
113-378 |
3.86e-100 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 301.67 E-value: 3.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 113 NAILSEAIKETASDIHIETYEKTMSIRFRIDGVLRTILQPNKKLAALLISRIKVMARLDIAEKRIPQDGRISLRIGRRNI 192
Cdd:NF041000 1 EELIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYELNEQQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 193 DVRVSTLPSIYG-ERAVLRLL-DKNSLQLSLNNlgmtAADKQDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALnTPG 270
Cdd:NF041000 81 SLRLSTVGDFLGrESLVIRLLyQLEQIKPQLFF----PEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSLARKL-ALN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 271 RNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASG 350
Cdd:NF041000 156 KQVITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAG 235
|
250 260
....*....|....*....|....*...
gi 1743360309 351 AVTRLRDMGVESFLLSSSLAGIIAQRLV 378
Cdd:NF041000 236 VIYRLLELGISKEELEQTLIGISYQRLI 263
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
232-380 |
1.26e-91 |
|
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: 275.90 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 232 QDLENLIQLPHGIILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARGLRAILRQD 311
Cdd:cd01129 1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743360309 312 PDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMGVESFLLSSSLAGIIAQRLVRR 380
Cdd:cd01129 81 PDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLVGR 149
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
112-458 |
2.83e-71 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 229.98 E-value: 2.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 112 INAILSEAIKETASDIHIETYEKtmsIRFRIDGVLRTIlqpnkKLAALLISRIKVMARLDIAEKRIPQ-------DGRIS 184
Cdd:COG2805 5 LDELLKLAVEQGASDLHLTVGSP---PMLRIDGELVPL-----DDPPLTPEDLEALLKEILTEEQRERleeegelDFSYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 185 LR-IGRrnidVRVStlpsIYGER----AVLRLLdkNSLQLSLNNLGMtaadKQDLENLIQLPHGIILVTGPTGSGKSTTL 259
Cdd:COG2805 77 LPgLGR----FRVN----IFRQRggvaAVLRLI--PSEIPTLEELGL----PPVLKELAELPRGLVLVTGPTGSGKSTTL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 260 YAILSALN-TPGRNILTVEDPVEYELEG----IGQTQVNTRVDmSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASL 334
Cdd:COG2805 143 AAMIDYINeTRAKHIITIEDPIEFVHKHkkslINQREVGRDTP-SFANALRAALREDPDVILVGEMRDLETIEAALTAAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 335 TGHLVLSTLHTNSASGAVTRLRDMgvesF----------LLSSSLAGIIAQRLVRRLcpqcrqftpvspqqaqmfkyhql 404
Cdd:COG2805 222 TGHLVFATLHTNSAAQTIDRIIDV----FppeeqaqirsQLAESLRGVISQRLLPRA----------------------- 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743360309 405 avttigtpvgcphchqSGyQGRMAIHEMMVVTPELRAAIHENVD------------------EQALERLVRQ 458
Cdd:COG2805 275 ----------------DG-GGRVAAREILVNTPAVRNLIREGKThqipsliqtgkklgmqtmDQSLAELVKE 329
|
|
| pilT_fam |
TIGR01420 |
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ... |
112-446 |
1.94e-55 |
|
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: 188.68 E-value: 1.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 112 INAILSEAIKETASDIHIETYEKTmsiRFRIDGVLRTILQPnkklaALLISRIKVMAR--LDIAEKRIPQ-----DGRIS 184
Cdd:TIGR01420 2 LEEILREAVKLGASDIHLTAGAPP---AMRIDGDLVRIEFE-----PLTPEDTQKLAReiLSEKQREEFEengelDFSFS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 185 LR-IGRrnidVRVSTLPSIYGERAVLRLLDKNSLQLSLNNLgmtaadKQDLENLIQLPHGIILVTGPTGSGKSTTLYAIL 263
Cdd:TIGR01420 74 LPgVGR----FRVNAFYQRGGVALVLRLIPSKIPTFEELGL------PPVLRELAERPRGLILVTGPTGSGKSTTLASMI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 264 SALN-TPGRNILTVEDPVEYELEG----IGQTQVNtRVDMSFARGLRAILRQDPDVVMVGEIRDTETAQIAVQASLTGHL 338
Cdd:TIGR01420 144 DYINkNKAYHIITIEDPIEYVHTNkrslINQREVG-EDTLSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 339 VLSTLHTNSASGAVTRLRDMGVES------FLLSSSLAGIIAQRLVRRlcpqcrqftpvspqqaqmfkyhqlavttigtp 412
Cdd:TIGR01420 223 VFGTLHTNSAAQTIERIIDVFPAEeqeqirTQLAESLVAIISQRLLPK-------------------------------- 270
|
330 340 350
....*....|....*....|....*....|....
gi 1743360309 413 vgcphchqSGYQGRMAIHEMMVVTPELRAAIHEN 446
Cdd:TIGR01420 271 --------ADGGGRVLAVEILINTPAVRNLIREG 296
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
234-446 |
4.19e-55 |
|
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: 183.89 E-value: 4.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 234 LENLIQLPHGIILVTGPTGSGKSTTLYAILSALN-TPGRNILTVEDPVEYELEG----IGQTQVNTRVDmSFARGLRAIL 308
Cdd:cd01131 13 LKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINeTRSKHIITIEDPIEFVHKHkkslINQREVGRDTE-SFAAALRAAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 309 RQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDMgvesF----------LLSSSLAGIIAQRLV 378
Cdd:cd01131 92 REDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDV----FppeqqeqvriQLASSLRGVISQRLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743360309 379 RRLcpqcrqftpvspqqaqmfkyhqlavttigtpvgcphchqsGYQGRMAIHEMMVVTPELRAAIHEN 446
Cdd:cd01131 168 PKK----------------------------------------DGGGRVAAFEILINTPAIRNLIREG 195
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
234-388 |
8.05e-49 |
|
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: 165.64 E-value: 8.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 234 LENLIQLPhGIILVTGPTGSGKSTTLYAILSALNTPgRNILTVEDPVEYEL---EGIGQTQVNTRVdmSFARGLRAILRQ 310
Cdd:cd19477 3 IKDGIAIG-KNVIVCGGTGSGKTTYIKSILEFIPKE-ERIISIEDTEEIVFkhhKNYTQLFFGGNI--TSADCLKSCLRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 311 DPDVVMVGEIRDtETAQIAVQASLTGH-LVLSTLHTNSASGAVTRLRDMG------------VESFLLSSSLAGIIAQRL 377
Cdd:cd19477 79 RPDRIILGELRS-SEAYDFYNVLCSGHkGTLTTLHAGSSEEAFIRLAN*SssnsaarnikfeSLIEGFKDLIDGIVHINH 157
|
170
....*....|.
gi 1743360309 378 VRrlcpQCRQF 388
Cdd:cd19477 158 HK----QCDEF 164
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
243-379 |
9.97e-39 |
|
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: 139.05 E-value: 9.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 243 GIILVTGPTGSGKSTTLYAILSAL---NTPGRNILTVEDPVEYELEGIG-------QTQVNTRVdMSFARGLRAILRQDP 312
Cdd:cd19516 12 GLVYVAGATGSGKSTLLAAIYRYIlenDPPDRKIITYEDPIEFVYDGIKskhsiivQSQIPRHF-KSFAKAVREALRRKP 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743360309 313 DVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDM-------GVESFLLSSSLAgIIAQRLVR 379
Cdd:cd19516 91 SLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLfppeerdAAAYDLLSTLRF-IIVQRLVR 163
|
|
| PilU |
COG5008 |
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures]; |
234-380 |
9.90e-37 |
|
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
Pssm-ID: 444032 Cd Length: 370 Bit Score: 139.08 E-value: 9.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 234 LENLIQLPHGIILVTGPTGSGKSTTLYAILS--ALNTPGrNILTVEDPVEYelegIGQTQ---VNTR---VD-MSFARGL 304
Cdd:COG5008 115 LKDLIMEKRGLVLFVGATGSGKSTTLAAMIDhrNENSSG-HILTIEDPIEF----VHKHKksiVTQRevgVDtESYEVAL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 305 RAILRQDPDVVMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRL--------RdmgvESFL--LSSSLAGIIA 374
Cdd:COG5008 190 KNALRQAPDVILIGEIRDRETMEHAIAFAETGHLCLATLHANNANQALDRIinffpeerR----PQLLmdLSLNLRAIVS 265
|
....*.
gi 1743360309 375 QRLVRR 380
Cdd:COG5008 266 QRLVPT 271
|
|
| plasmid_TraJ |
TIGR02525 |
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ... |
243-379 |
1.33e-28 |
|
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: 116.44 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 243 GIILVTGPTGSGKSTTLYAILSAL--NTPGRNILTVEDPVEYELEGIG------QTQVNTRVDmSFARGLRAILRQDPDV 314
Cdd:TIGR02525 150 GLGLICGETGSGKSTLAASIYQHCgeTYPDRKIVTYEDPIEYILGSPDdllppaQSQIGRDVD-SFANGIRLALRRAPKI 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743360309 315 VMVGEIRDTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRDM------GVESFLLSSSLAGIIAQRLVR 379
Cdd:TIGR02525 229 IGVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSPGEAISRCLQMyppemrEAAAFDLLSILQYIIVQRLLR 299
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
242-380 |
1.87e-22 |
|
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: 99.77 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 242 HGIILVTGPTGSGKSTTLYAILSALNtPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARG-------LRAILRQDPDV 314
Cdd:COG0630 290 GKSVLVAGGTASGKTTLLNALLSFIP-PDAKIVTIEDTRELNLPHENWISLVTRESFGGEEGdvtmfdlLKAALRQRPDY 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743360309 315 VMVGEIRdTETAQIAVQASLTGHLVLSTLHTNSASGAVTRLRD--MGVESFLLsSSLAGIIAQRLVRR 380
Cdd:COG0630 369 IVVGEVR-GEEAYTLFQAMATGHGVLSTFHADSVESAINRLTSppINVPRTLL-QALDLVVFQKRVRV 434
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
245-362 |
6.35e-20 |
|
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: 87.21 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSALNtPGRNILTVEDPVE--------YELEGIGQTQVNTRVDMsfARGLRAILRQDPDVVM 316
Cdd:cd01130 15 ILISGGTGSGKTTLLNALLSFIP-PDERIVTIEDTRElqlphpnvVHLLTRPGGGEKGEVTM--ADLLKAALRMRPDRII 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1743360309 317 VGEIRDTEtAQIAVQASLTGHL-VLSTLHTNSASGAVTRLRDMGVES 362
Cdd:cd01130 92 VGEVRGGE-AYDMLQAMNTGHPgSITTIHANSAEDAIDRLATLVLEA 137
|
|
| PRK13894 |
PRK13894 |
conjugal transfer ATPase TrbB; Provisional |
226-356 |
5.46e-15 |
|
conjugal transfer ATPase TrbB; Provisional
Pssm-ID: 184377 Cd Length: 319 Bit Score: 75.93 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 226 MTAADKQDLENLIQlPHGIILVTGPTGSGKSTTLYAILSAL--NTPGRNILTVEDPVEYELEGIGQTQVNTRVDMSFARG 303
Cdd:PRK13894 133 MTAAQREAIIAAVR-AHRNILVIGGTGSGKTTLVNAIINEMviQDPTERVFIIEDTGEIQCAAENYVQYHTSIDVNMTAL 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1743360309 304 LRAILRQDPDVVMVGEIRDTETAQIaVQASLTGHL-VLSTLHTNSASGAVTRLR 356
Cdd:PRK13894 212 LKTTLRMRPDRILVGEVRGPEALDL-LMAWNTGHEgGAATLHANNAKAGLDRLK 264
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
245-359 |
9.44e-15 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 75.59 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKsTTLYAILSALNTPGRNILTVEDpvEYEL-----------------EGIGQtqvntrVDMsfARGLRAI 307
Cdd:COG4962 185 ILVSGGTGSGK-TTLLNALSGFIPPDERIVTIED--AAELqlqhphvvrletrppnvEGAGE------VTL--RDLVRNA 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1743360309 308 LRQDPDVVMVGEIRDTEtAQIAVQASLTGHL-VLSTLHTNSASGAVTRLRDMG 359
Cdd:COG4962 254 LRMRPDRIIVGEVRGAE-ALDMLQAMNTGHDgSMSTLHANSARDALARLETLA 305
|
|
| PRK13833 |
PRK13833 |
conjugal transfer protein TrbB; Provisional |
245-361 |
8.83e-10 |
|
conjugal transfer protein TrbB; Provisional
Pssm-ID: 172360 [Multi-domain] Cd Length: 323 Bit Score: 60.20 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSAL--NTPGRNILTVEDPVEYELEGIGQTQVNT--RVDMsfARGLRAILRQDPDVVMVGEI 320
Cdd:PRK13833 147 IVISGGTGSGKTTLANAVIAEIvaSAPEDRLVILEDTAEIQCAAENAVALHTsdTVDM--ARLLKSTMRLRPDRIIVGEV 224
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1743360309 321 RDTeTAQIAVQASLTGHL-VLSTLHTNSASGAVTRLRDMGVE 361
Cdd:PRK13833 225 RDG-AALTLLKAWNTGHPgGVTTIHSNTAMSALRRLEQLTAE 265
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
241-320 |
3.27e-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: 46.98 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 241 PHGIILVTGPTGSGKSTTLYAILSALNTPGRNILTV--EDPVEYELEGIGQTQVNTRVDMSF----ARGLRAILRQ-DPD 313
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIdgEDILEEVLDQLLLIIVGGKKASGSgelrLRLALALARKlKPD 80
|
....*..
gi 1743360309 314 VVMVGEI 320
Cdd:smart00382 81 VLILDEI 87
|
|
| PRK13851 |
PRK13851 |
type IV secretion system protein VirB11; Provisional |
230-344 |
3.62e-06 |
|
type IV secretion system protein VirB11; Provisional
Pssm-ID: 172375 Cd Length: 344 Bit Score: 49.13 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 230 DKQDLENLIQ---LPHGIILVTGPTGSGKSTTLYAILSALnTPGRNILTVEDPVE------------YELEGIGQTQVNT 294
Cdd:PRK13851 147 DNGDLEAFLHacvVGRLTMLLCGPTGSGKTTMSKTLISAI-PPQERLITIEDTLElviphenhvrllYSKNGAGLGAVTA 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1743360309 295 RvdmsfaRGLRAILRQDPDVVMVGEIRDtETAQIAVQASLTGHL-VLSTLH 344
Cdd:PRK13851 226 E------HLLQASLRMRPDRILLGEMRD-DAAWAYLSEVVSGHPgSISTIH 269
|
|
| PRK13900 |
PRK13900 |
type IV secretion system ATPase VirB11; Provisional |
213-358 |
1.63e-05 |
|
type IV secretion system ATPase VirB11; Provisional
Pssm-ID: 184381 Cd Length: 332 Bit Score: 47.06 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 213 DKNSLQLSLNNLGMTAADKQDLENLIQLPHGIIlVTGPTGSGKSTTLYAILSALNTPGRnILTVEDPVEYELE------- 285
Cdd:PRK13900 132 LVDEDDVILNELLAEKKIKEFLEHAVISKKNII-ISGGTSTGKTTFTNAALREIPAIER-LITVEDAREIVLSnhpnrvh 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 286 ------GIGQTQVNTRvDMsfargLRAILRQDPDVVMVGEIRDTEtAQIAVQASLTGHL-VLSTLHTNSASGAVTRLRDM 358
Cdd:PRK13900 210 llaskgGQGRAKVTTQ-DL-----IEACLRLRPDRIIVGELRGAE-AFSFLRAINTGHPgSISTLHADSPAMAIEQLKLM 282
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
238-292 |
3.01e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 44.79 E-value: 3.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743360309 238 IQLPHGIILVTGPTGSGKSTTLYAILSAL------NTPGRNILTVEDPVEYELEGIGQTQV 292
Cdd:pfam13476 14 IDFSKGLTLITGPNGSGKTTILDAIKLALygktsrLKRKSGGGFVKGDIRIGLEGKGKAYV 74
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
241-273 |
1.73e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|...
gi 1743360309 241 PHGIILVTGPTGSGKSTTLYAIlSALNTPGRNI 273
Cdd:pfam13555 21 PRGNTLLTGPSGSGKSTLLDAI-QTLLVPAKRA 52
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
235-266 |
2.11e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 2.11e-04
10 20 30
....*....|....*....|....*....|..
gi 1743360309 235 ENLIQLPHGIILVTGPTGSGKSTTLYAILSAL 266
Cdd:COG0419 16 TETIDFDDGLNLIVGPNGAGKSTILEAIRYAL 47
|
|
| NTPase_1 |
pfam03266 |
NTPase; This domain is found across all species from bacteria to human, and the function was ... |
245-356 |
2.45e-04 |
|
NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
Pssm-ID: 460869 Cd Length: 168 Bit Score: 41.84 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 245 ILVTGPTGSGKSTTLYAILSALN----------TP---------GRNILTVEDPVEYELEG--------IGQTQVNTRvd 297
Cdd:pfam03266 2 IFITGPPGVGKTTLVLKVAELLKssgvkvggfyTPevreggrriGFKIVDLASGEEGWLARvgavsgprVGKYVVNVE-- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743360309 298 mSFAR-GLRAILR--QDPDVVMVGEI----RDTETAQIAVQASLTGH-LVLSTLHTNSASGAVTRLR 356
Cdd:pfam03266 80 -SFEEiAVPALRRalEEADLIIIDEIgpmeLKSKKFREAVREVLDSGkPVLAVIHRRSDSPLLEEIR 145
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
217-278 |
1.69e-03 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 40.00 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743360309 217 LQLSLNNLGMTAADKQDLENL-IQLPHG-IILVTGPTGSGKSTTLYAiLSALNTPGRNILTVED 278
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLsLSLPTGkITALIGPNGCGKSTLLKC-FARLLTPQSGTVFLGD 63
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
219-264 |
1.95e-03 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 39.41 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1743360309 219 LSLNNLGMTAADKQDLENL-IQLPHG-IILVTGPTGSGKSTTLYAILS 264
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVsLTLEAGeCVAITGPSGSGKSTLLRALAD 48
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
238-287 |
2.43e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 2.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1743360309 238 IQLPHGIILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYELEGI 287
Cdd:pfam13401 1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDL 50
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
220-274 |
2.70e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.38 E-value: 2.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1743360309 220 SLNNLGMTAADKQDLENL-IQLPHG-IILVTGPTGSGKSTTLYAILSALNTPGRNIL 274
Cdd:cd00267 1 EIENLSFRYGGRTALDNVsLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL 57
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
217-303 |
3.26e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 217 LQLSLNNLG----MTAADKQDLENliqlpHGIILVTGPTGSGKSTTLYAILSAL--NTPGrniltveDPVEYELEGIGQT 290
Cdd:cd03279 4 LKLELKNFGpfreEQVIDFTGLDN-----NGLFLICGPTGAGKSTILDAITYALygKTPR-------YGRQENLRSVFAP 71
|
90
....*....|....
gi 1743360309 291 QVNT-RVDMSFARG 303
Cdd:cd03279 72 GEDTaEVSFTFQLG 85
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
240-274 |
3.54e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 37.92 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|....*
gi 1743360309 240 LPHGIILVTGPTGSGKSTTLYAILSALNTPGRNIL 274
Cdd:cd17933 10 LRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVV 44
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
231-320 |
5.67e-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: 37.51 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 231 KQDLENLIQLPHG-IILVTGPTGSGKSTTLYAILSALNTPGRNILTVEDPVEYElegigQTQVNTRVDMSFARGLRAILR 309
Cdd:cd00009 7 IEALREALELPPPkNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLE-----GLVVAELFGHFLVRLLFELAE 81
|
90
....*....|..
gi 1743360309 310 Q-DPDVVMVGEI 320
Cdd:cd00009 82 KaKPGVLFIDEI 93
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
224-299 |
7.43e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743360309 224 LGMTAADKQDLENL-IQLPHG-IILVTGPTGSGKST----TLYAILSAlntpgRNILTVEDPVEY-ELEGIGQTQVNTRV 296
Cdd:cd03271 1 LTLKGARENNLKNIdVDIPLGvLTCVTGVSGSGKSSlindTLYPALAR-----RLHLKKEQPGNHdRIEGLEHIDKVIVI 75
|
...
gi 1743360309 297 DMS 299
Cdd:cd03271 76 DQS 78
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
235-266 |
9.91e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.95 E-value: 9.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1743360309 235 ENLIQLPHGII-LVTGPTGSGKSTTLYAILSAL 266
Cdd:cd03227 13 PNDVTFGEGSLtIITGPNGSGKSTILDAIGLAL 45
|
|
| |
