|
Name |
Accession |
Description |
Interval |
E-value |
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
13-583 |
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: 711.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 13 LEQLLQEGRITERDKLLVQTTNRQKDQLkwhplqwiahfnLKDQHHVQAHLSLNRLCQWFADRAQLPLFVIDPLKADvSA 92
Cdd:COG2804 10 GDLLVEAGLISEEQLLAALAEQKKTGKP------------LGELLVELGLVTEELLAEALAEQLGLPFVDLDELEID-PE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 93 LTQVMSQEFAIRNHILAVEVHADRIVIGTDQPFQTDWLNNLEKsLAPKKIERVFLNPEQLQRYLREYYQVSRAVNSAQKD 172
Cdd:COG2804 77 VLELLPEELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRR-LTGRPVEPVVATESDIERALDRLYGSESSIEELLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 173 AAHDrdnkgVEALLQLGDSQNPDANDQHIVKLVDWILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTA 252
Cdd:COG2804 156 LAED-----LTSEEEDLEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAPA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 253 VISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETELRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRIT 332
Cdd:COG2804 231 LVSRIKIMANLDIAERRLPQDGRIKLRL-GGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 333 QNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIG 412
Cdd:COG2804 310 RRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 413 EIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRKLCPNCKQQTHINEDEWQH 492
Cdd:COG2804 390 EIRDLETAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELER 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 493 LTFDYIMEMPEKVYRAVGCEECRHTGYKGRIGIYEFMPVSLELKHLISSHATLNELRSQTKKESVEPLRIAGARKVIEGL 572
Cdd:COG2804 470 LGLPPEELAPLTFYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEGMRTLREDGLEKVLQGI 549
|
570
....*....|.
gi 446943652 573 TTLEEVLRVVP 583
Cdd:COG2804 550 TTLEEVLRVTG 560
|
|
| type_II_gspE |
TIGR02533 |
type II secretion system protein E; This family describes GspE, the E protein of the type II ... |
101-581 |
4.89e-169 |
|
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: 489.20 E-value: 4.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 101 FAIRNHILAVEVHADRIVIGTDQPFQTDWLNNLeKSLAPKKIERVFLNPEQLQRYLREYYQVSRA-----VNSAQKDAAH 175
Cdd:TIGR02533 8 FAKQSRVLPLSEHDGTLVVAVSDPLDLAALDEV-RRLFGAPVQLIIATASEIDDAINSVYARTGSaaaqiVEEIEGEDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 176 DR---DNKGVEALLQLGDsqnpdanDQHIVKLVDWILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTA 252
Cdd:TIGR02533 87 SAlelDEPKIEDLLDLED-------DAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRFRVDGVLRDVLSPPKKLHAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 253 VISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETELRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRIT 332
Cdd:TIGR02533 160 LVSRVKIMAKLNIAEKRLPQDGRISLRV-GGRDIDIRVSTVPTSHGERVVMRLLDKTAVRLDLETLGMSPELLSRFERLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 333 QNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIG 412
Cdd:TIGR02533 239 RRPHGIILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPVEYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 413 EIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRKLCPNCKQQTHINEDEWQh 492
Cdd:TIGR02533 319 EIRDLETAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIA- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 493 lTFDYIMEMPEKVYRAVGCEECRHTGYKGRIGIYEFMPVSLELKHLISSHATLNELRSQTKKESVEPLRIAGARKVIEGL 572
Cdd:TIGR02533 398 -LFGISPEGPINLYRPVGCPHCNHTGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAGMRTLRDDGLRKVLAGI 476
|
....*....
gi 446943652 573 TTLEEVLRV 581
Cdd:TIGR02533 477 TTIEEVLRV 485
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
185-582 |
3.96e-138 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 409.32 E-value: 3.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 185 LLQLGDSQNPDANDQHIVKLVDWILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLN 264
Cdd:PRK10436 68 RTQQTLPVADQEKDTPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAALTARLKVLGNLD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 265 VAEKRKPQDGRLkTRTPKGQETELRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRITQNSHGIILVTGP 344
Cdd:PRK10436 148 IAERRLPQDGQF-TVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQFRQALQQPQGLILVTGP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 345 TGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAI 424
Cdd:PRK10436 227 TGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 425 QAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRKLCPNCKQQ----THINEDEWQhltfdyime 500
Cdd:PRK10436 307 KAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLVRKLCPHCRQQasepIHLPPNIWP--------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 501 MPEKVYRAVGCEECRHtGYKGRIGIYEFMPVSLELKHLISSHATLNELRSQTKKESVEPLRIAGARKVIEGLTTLEEVLR 580
Cdd:PRK10436 378 GPLPHWQAVGCEHCYH-GYYGRTALFEVLPITPVLQQAIASNASPEELETHARQQGMTTLFENGLLAVEQGLTTLEELYR 456
|
..
gi 446943652 581 VV 582
Cdd:PRK10436 457 VL 458
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
208-475 |
1.11e-110 |
|
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: 331.94 E-value: 1.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 208 ILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETE 287
Cdd:pfam00437 3 IPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRI-GGKGVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 288 LRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNV 367
Cdd:pfam00437 82 VRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDENI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 368 CTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLT 447
Cdd:pfam00437 162 VTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGALT 241
|
250 260
....*....|....*....|....*...
gi 446943652 448 RLHDLGVQPFLTAATILGVLAQRLVRKL 475
Cdd:pfam00437 242 RLQDMGVPPFELASSLLLVIAQRLVRKL 269
|
|
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
208-472 |
5.79e-95 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 291.27 E-value: 5.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 208 ILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETE 287
Cdd:NF041000 3 LIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYEL-NEQQIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 288 LRLSTLPTAFG-EKLVMRIFDPDvlvRSFQQLGFDQSLLQQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQvN 366
Cdd:NF041000 82 LRLSTVGDFLGrESLVIRLLYQL---EQIKPQLFFPEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSLARKLALNK-Q 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 367 VCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSL 446
Cdd:NF041000 158 VITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVI 237
|
250 260
....*....|....*....|....*.
gi 446943652 447 TRLHDLGVQPFLTAATILGVLAQRLV 472
Cdd:NF041000 238 YRLLELGISKEELEQTLIGISYQRLI 263
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
326-474 |
1.24e-83 |
|
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: 258.18 E-value: 1.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 326 QQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQD 405
Cdd:cd01129 1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943652 406 PDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRK 474
Cdd:cd01129 81 PDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLVGR 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
335-414 |
4.50e-04 |
|
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: 40.82 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 335 SHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGV------RALMRQ-DPD 407
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrlaLALARKlKPD 80
|
....*..
gi 446943652 408 IIMIGEI 414
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 ... |
13-583 |
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: 711.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 13 LEQLLQEGRITERDKLLVQTTNRQKDQLkwhplqwiahfnLKDQHHVQAHLSLNRLCQWFADRAQLPLFVIDPLKADvSA 92
Cdd:COG2804 10 GDLLVEAGLISEEQLLAALAEQKKTGKP------------LGELLVELGLVTEELLAEALAEQLGLPFVDLDELEID-PE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 93 LTQVMSQEFAIRNHILAVEVHADRIVIGTDQPFQTDWLNNLEKsLAPKKIERVFLNPEQLQRYLREYYQVSRAVNSAQKD 172
Cdd:COG2804 77 VLELLPEELARRHRVLPLRLEGGTLTVAMADPLDLEALDELRR-LTGRPVEPVVATESDIERALDRLYGSESSIEELLEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 173 AAHDrdnkgVEALLQLGDSQNPDANDQHIVKLVDWILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTA 252
Cdd:COG2804 156 LAED-----LTSEEEDLEDLLEEADDAPVVRLVNAILEDAIKEGASDIHIEPYEKRLRVRFRIDGVLREVLRLPKSLAPA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 253 VISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETELRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRIT 332
Cdd:COG2804 231 LVSRIKIMANLDIAERRLPQDGRIKLRL-GGREIDLRVSTLPTVYGEKVVLRILDKSAALLDLEQLGFSPDQLERLRRLI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 333 QNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIG 412
Cdd:COG2804 310 RRPHGIILVTGPTGSGKTTTLYAALNELNTPERNIITVEDPVEYQLPGINQVQVNPKIGLTFASALRSILRQDPDVIMVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 413 EIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRKLCPNCKQQTHINEDEWQH 492
Cdd:COG2804 390 EIRDLETAEIAVQAALTGHLVLSTLHTNDAPSAITRLLDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEPDPEELER 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 493 LTFDYIMEMPEKVYRAVGCEECRHTGYKGRIGIYEFMPVSLELKHLISSHATLNELRSQTKKESVEPLRIAGARKVIEGL 572
Cdd:COG2804 470 LGLPPEELAPLTFYRGVGCEHCNGTGYKGRTGIYELLVIDDELRELIAEGASAAELREAARKEGMRTLREDGLEKVLQGI 549
|
570
....*....|.
gi 446943652 573 TTLEEVLRVVP 583
Cdd:COG2804 550 TTLEEVLRVTG 560
|
|
| type_II_gspE |
TIGR02533 |
type II secretion system protein E; This family describes GspE, the E protein of the type II ... |
101-581 |
4.89e-169 |
|
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: 489.20 E-value: 4.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 101 FAIRNHILAVEVHADRIVIGTDQPFQTDWLNNLeKSLAPKKIERVFLNPEQLQRYLREYYQVSRA-----VNSAQKDAAH 175
Cdd:TIGR02533 8 FAKQSRVLPLSEHDGTLVVAVSDPLDLAALDEV-RRLFGAPVQLIIATASEIDDAINSVYARTGSaaaqiVEEIEGEDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 176 DR---DNKGVEALLQLGDsqnpdanDQHIVKLVDWILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTA 252
Cdd:TIGR02533 87 SAlelDEPKIEDLLDLED-------DAPVIRLVNSLLSRAVKERASDIHIEPFEKALVVRFRVDGVLRDVLSPPKKLHAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 253 VISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETELRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRIT 332
Cdd:TIGR02533 160 LVSRVKIMAKLNIAEKRLPQDGRISLRV-GGRDIDIRVSTVPTSHGERVVMRLLDKTAVRLDLETLGMSPELLSRFERLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 333 QNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIG 412
Cdd:TIGR02533 239 RRPHGIILVTGPTGSGKTTTLYAALSRLNTPERNILTVEDPVEYQIEGIGQIQVNPKIGLTFAAGLRAILRQDPDIIMVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 413 EIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRKLCPNCKQQTHINEDEWQh 492
Cdd:TIGR02533 319 EIRDLETAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLLGVLAQRLVRRLCPHCKEPYEATPEEIA- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 493 lTFDYIMEMPEKVYRAVGCEECRHTGYKGRIGIYEFMPVSLELKHLISSHATLNELRSQTKKESVEPLRIAGARKVIEGL 572
Cdd:TIGR02533 398 -LFGISPEGPINLYRPVGCPHCNHTGYLGRTGIYELLIVDDDLRSLIHSRADEGEIKEIARAAGMRTLRDDGLRKVLAGI 476
|
....*....
gi 446943652 573 TTLEEVLRV 581
Cdd:TIGR02533 477 TTIEEVLRV 485
|
|
| type_IV_pilB |
TIGR02538 |
type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus ... |
78-581 |
1.72e-165 |
|
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: 482.98 E-value: 1.72e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 78 LPLFVIDPLKADvSALTQVMSQEFAIRNHILAVEVHADRIVIGTDQPFQTDWLNNLeKSLAPKKIERVFLNPEQLQRYLR 157
Cdd:TIGR02538 56 VPLLDLNAFDPD-ALPVQLVSEELIQKHQALPLFKRGNTLFVAVSDPTNISALDDI-RFATGLNVEVVIVEEDKLSALIE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 158 EYYqvsraVNSAQKDAAHDRDNKGVEALLQLG---------DSQNPDANDQHIVKLVDWILQFAFEQSASDIHMEPRKDN 228
Cdd:TIGR02538 134 KYY-----GGSDSLAKELGDEDIGDLEELDVDaiddegpddIEQDAVDDDAPIVKFVNKILLDAIRKGASDIHFEPYEKS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 229 GKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLNVAEKRKPQDGRLKTRTPKGQETELRLSTLPTAFGEKLVMRIFDP 308
Cdd:TIGR02538 209 YRVRFRIDGILHEVAQPPLALANRIAARIKVMSRLDIAEKRIPQDGRIKLKLSKSKAIDFRVSTLPTLFGEKVVLRILDS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 309 DVLVRSFQQLGFDQSLLQQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNH 388
Cdd:TIGR02538 289 SAAQLDIDKLGFEPDQKALFLEAIHKPQGMVLVTGPTGSGKTVSLYTALNILNTEEVNISTAEDPVEINLPGINQVNVNP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 389 AIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLA 468
Cdd:TIGR02538 369 KIGLTFAAALRSFLRQDPDIIMVGEIRDLETAEIAIKAAQTGHLVLSTLHTNDAPETLARLVNMGIAPFNIASSVNLIMA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 469 QRLVRKLCPNCKQQTHINEDEWQHLTFDyimemPE-----KVYRAVGCEECRHTGYKGRIGIYEFMPVSLELKHLISSHA 543
Cdd:TIGR02538 449 QRLARRLCSHCKAPEEVPAEALLELGFT-----QEdladlKLYGPVGCDECSNTGYKGRVGIYEVMPMSEEIAELILKGG 523
|
490 500 510
....*....|....*....|....*....|....*...
gi 446943652 544 TLNELRSQTKKESVEPLRIAGARKVIEGLTTLEEVLRV 581
Cdd:TIGR02538 524 NALQIAELAQKEGMRTLRRSGLLKVKQGVTSLEEVLRV 561
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
185-582 |
3.96e-138 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 409.32 E-value: 3.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 185 LLQLGDSQNPDANDQHIVKLVDWILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLN 264
Cdd:PRK10436 68 RTQQTLPVADQEKDTPVAQLINQTLQSALQKRASDIHFEPAQNHYRIRLRIDGVLHPLPDPSPELGAALTARLKVLGNLD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 265 VAEKRKPQDGRLkTRTPKGQETELRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRITQNSHGIILVTGP 344
Cdd:PRK10436 148 IAERRLPQDGQF-TVELAGNAYSFRIATLPCRGGEKVVLRLLQQVQQALDLETLGMTPAQLAQFRQALQQPQGLILVTGP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 345 TGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAI 424
Cdd:PRK10436 227 TGSGKTVTLYSALQTLNTAQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 425 QAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRKLCPNCKQQ----THINEDEWQhltfdyime 500
Cdd:PRK10436 307 KAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASALKLVIAQRLVRKLCPHCRQQasepIHLPPNIWP--------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 501 MPEKVYRAVGCEECRHtGYKGRIGIYEFMPVSLELKHLISSHATLNELRSQTKKESVEPLRIAGARKVIEGLTTLEEVLR 580
Cdd:PRK10436 378 GPLPHWQAVGCEHCYH-GYYGRTALFEVLPITPVLQQAIASNASPEELETHARQQGMTTLFENGLLAVEQGLTTLEELYR 456
|
..
gi 446943652 581 VV 582
Cdd:PRK10436 457 VL 458
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
208-475 |
1.11e-110 |
|
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: 331.94 E-value: 1.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 208 ILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETE 287
Cdd:pfam00437 3 IPLEALDEGASDIHVEPPERIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPLRI-GGKGVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 288 LRLSTLPTAFGEKLVMRIFDPDVLVRSFQQLGFDQSLLQQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNV 367
Cdd:pfam00437 82 VRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTRDENI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 368 CTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLT 447
Cdd:pfam00437 162 VTVEDPVEIQLEGINQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGALT 241
|
250 260
....*....|....*....|....*...
gi 446943652 448 RLHDLGVQPFLTAATILGVLAQRLVRKL 475
Cdd:pfam00437 242 RLQDMGVPPFELASSLLLVIAQRLVRKL 269
|
|
| ATPase_ComGA |
NF041000 |
competence type IV pilus ATPase ComGA; |
208-472 |
5.79e-95 |
|
competence type IV pilus ATPase ComGA;
Pssm-ID: 468930 [Multi-domain] Cd Length: 265 Bit Score: 291.27 E-value: 5.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 208 ILQFAFEQSASDIHMEPRKDNGKVRFRIDGVLHTIYNMPSNTLTAVISRIKILGRLNVAEKRKPQDGRLKTRTpKGQETE 287
Cdd:NF041000 3 LIEEAIELRASDIHFLPREDGYQIKFRIGGGLIPYRELSLEEGQRLISYFKFLAGMDIGEKRRPQSGAFTYEL-NEQQIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 288 LRLSTLPTAFG-EKLVMRIFDPDvlvRSFQQLGFDQSLLQQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQvN 366
Cdd:NF041000 82 LRLSTVGDFLGrESLVIRLLYQL---EQIKPQLFFPEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSLARKLALNK-Q 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 367 VCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSL 446
Cdd:NF041000 158 VITIEDPVEIKEPNFLQLQVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVI 237
|
250 260
....*....|....*....|....*.
gi 446943652 447 TRLHDLGVQPFLTAATILGVLAQRLV 472
Cdd:NF041000 238 YRLLELGISKEELEQTLIGISYQRLI 263
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
326-474 |
1.24e-83 |
|
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: 258.18 E-value: 1.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 326 QQWQRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVRALMRQD 405
Cdd:cd01129 1 ARLRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITIEDPVEYQIPGINQSQVNEKIGLTFADALRAILRQD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446943652 406 PDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDLGVQPFLTAATILGVLAQRLVRK 474
Cdd:cd01129 81 PDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASALRGVIAQRLVGR 149
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
208-474 |
2.84e-57 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 195.70 E-value: 2.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 208 ILQFAFEQSASDIHMeprKDNGKVRFRIDGVLHTIyNMPSNTLTAVISRIKILgrLNVAEKRKPQDGRlktrtpkgqetE 287
Cdd:COG2805 8 LLKLAVEQGASDLHL---TVGSPPMLRIDGELVPL-DDPPLTPEDLEALLKEI--LTEEQRERLEEEG-----------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 288 LRLS-TLP-------TAFGEK----LVMRIFDPDVLvrSFQQLGFDQSLlqqwQRITQNSHGIILVTGPTGSGKTTTLYS 355
Cdd:COG2805 71 LDFSySLPglgrfrvNIFRQRggvaAVLRLIPSEIP--TLEELGLPPVL----KELAELPRGLVLVTGPTGSGKSTTLAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 356 SLKQL-ATEQVNVCTIEDPIEMLEPS----FNQMQV-NHAieLGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALT 429
Cdd:COG2805 145 MIDYInETRAKHIITIEDPIEFVHKHkkslINQREVgRDT--PSFANALRAALREDPDVILVGEMRDLETIEAALTAAET 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446943652 430 GHLVLSTLHTNDAPSSLTRLHDL---GVQPFLT---AATILGVLAQRLVRK 474
Cdd:COG2805 223 GHLVFATLHTNSAAQTIDRIIDVfppEEQAQIRsqlAESLRGVISQRLLPR 273
|
|
| pilT_fam |
TIGR01420 |
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ... |
208-474 |
6.48e-46 |
|
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: 165.19 E-value: 6.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 208 ILQFAFEQSASDIHMeprKDNGKVRFRIDGVLHTIYNMPsntLTAVISRIKILGRLNVAEKRKPQdgrlktrtpkgQETE 287
Cdd:TIGR01420 5 ILREAVKLGASDIHL---TAGAPPAMRIDGDLVRIEFEP---LTPEDTQKLAREILSEKQREEFE-----------ENGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 288 LRLS-TLP-------TAFGEK----LVMRIFDPDVlvRSFQQLGFDQSLLQqwqrITQNSHGIILVTGPTGSGKTTTLYS 355
Cdd:TIGR01420 68 LDFSfSLPgvgrfrvNAFYQRggvaLVLRLIPSKI--PTFEELGLPPVLRE----LAERPRGLILVTGPTGSGKSTTLAS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 356 SLKQLATEQ-VNVCTIEDPIEMLEPsfNQMQVNHAIELG-----FADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALT 429
Cdd:TIGR01420 142 MIDYINKNKaYHIITIEDPIEYVHT--NKRSLINQREVGedtlsFANALRAALREDPDVILIGEMRDLETVELALTAAET 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446943652 430 GHLVLSTLHTNDAPSSLTRLHDL-------GVQPFLtAATILGVLAQRLVRK 474
Cdd:TIGR01420 220 GHLVFGTLHTNSAAQTIERIIDVfpaeeqeQIRTQL-AESLVAIISQRLLPK 270
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
312-474 |
1.47e-43 |
|
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: 155.00 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 312 VRSFQQLGFDQSLlqqwQRITQNSHGIILVTGPTGSGKTTTLYSSLKQL-ATEQVNVCTIEDPIEMLEPS----FNQMQV 386
Cdd:cd01131 1 IPTFEELGLPPVL----KDLALKPRGLVLVTGPTGSGKSTTLAAMIDYInETRSKHIITIEDPIEFVHKHkkslINQREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 387 nHAIELGFADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLhdLGVQPF--------L 458
Cdd:cd01131 77 -GRDTESFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRI--IDVFPPeqqeqvriQ 153
|
170
....*....|....*.
gi 446943652 459 TAATILGVLAQRLVRK 474
Cdd:cd01131 154 LASSLRGVISQRLLPK 169
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
337-475 |
5.71e-36 |
|
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: 132.52 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 337 GIILVTGPTGSGKTTTLYSSLKQLATEQvNVCTIEDPIEML---EPSFNQMQVNHAIElgFADGVRALMRQDPDIIMIGE 413
Cdd:cd19477 11 KNVIVCGGTGSGKTTYIKSILEFIPKEE-RIISIEDTEEIVfkhHKNYTQLFFGGNIT--SADCLKSCLRQRPDRIILGE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446943652 414 IRDQdTANMAIQAALTGH-LVLSTLHTNDAPSSLTRLHDLG------------VQPFLTAATILGVLAQRLVRKL 475
Cdd:cd19477 88 LRSS-EAYDFYNVLCSGHkGTLTTLHAGSSEEAFIRLAN*SssnsaarnikfeSLIEGFKDLIDGIVHINHHKQC 161
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
337-474 |
5.15e-33 |
|
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: 124.41 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 337 GIILVTGPTGSGKTTTLYSSLKQLATE---QVNVCTIEDPIEMLepsFNQMQVNHAI----ELG-----FADGVRALMRQ 404
Cdd:cd19516 12 GLVYVAGATGSGKSTLLAAIYRYILENdppDRKIITYEDPIEFV---YDGIKSKHSIivqsQIPrhfksFAKAVREALRR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446943652 405 DPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLHDL--GVQPFLTAATILGVL----AQRLVRK 474
Cdd:cd19516 89 KPSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLfpPEERDAAAYDLLSTLrfiiVQRLVRT 164
|
|
| PilU |
COG5008 |
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures]; |
336-474 |
5.12e-28 |
|
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
Pssm-ID: 444032 Cd Length: 370 Bit Score: 115.58 E-value: 5.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 336 HGIILVTGPTGSGKTTTLYSSLKQLATeqvNVC----TIEDPIEMLEPSFNQMqVNHAiELG-----FADGVRALMRQDP 406
Cdd:COG5008 123 RGLVLFVGATGSGKSTTLAAMIDHRNE---NSSghilTIEDPIEFVHKHKKSI-VTQR-EVGvdtesYEVALKNALRQAP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 407 DIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTR-------------LHDLgvqpfltAATILGVLAQRLVR 473
Cdd:COG5008 198 DVILIGEIRDRETMEHAIAFAETGHLCLATLHANNANQALDRiinffpeerrpqlLMDL-------SLNLRAIVSQRLVP 270
|
.
gi 446943652 474 K 474
Cdd:COG5008 271 T 271
|
|
| plasmid_TraJ |
TIGR02525 |
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ... |
301-477 |
2.33e-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: 96.03 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 301 LVMRIFDPDVlvRSFQQLGFDQSLLQQWQRITqnshGIILVTGPTGSGKTTtLYSSLKQLATEQV---NVCTIEDPIEML 377
Cdd:TIGR02525 120 LTLRVIPSDI--PDLKQMGIEPDLFNSLLPAA----GLGLICGETGSGKST-LAASIYQHCGETYpdrKIVTYEDPIEYI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 378 EPSFNQMQVNHAIELG-----FADGVRALMRQDPDIIMIGEIRDQDTANMAIQAALTGHLVLSTLHTNDAPSSLTRLhdL 452
Cdd:TIGR02525 193 LGSPDDLLPPAQSQIGrdvdsFANGIRLALRRAPKIIGVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSPGEAISRC--L 270
|
170 180
....*....|....*....|....*....
gi 446943652 453 GVQPF----LTAATILGVLAQRLVRKLCP 477
Cdd:TIGR02525 271 QMYPPemreAAAFDLLSILQYIIVQRLLR 299
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
339-449 |
6.69e-19 |
|
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: 84.51 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 339 ILVTGPTGSGKTTTLySSLKQLATEQVNVCTIEDPIEMLepsFNQMQVNHAI---------ELGFADGVRALMRQDPDII 409
Cdd:cd01130 15 ILISGGTGSGKTTLL-NALLSFIPPDERIVTIEDTRELQ---LPHPNVVHLLtrpgggekgEVTMADLLKAALRMRPDRI 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446943652 410 MIGEIRDQDTANMaIQAALTGHL-VLSTLHTNDAPSSLTRL 449
Cdd:cd01130 91 IVGEVRGGEAYDM-LQAMNTGHPgSITTIHANSAEDAIDRL 130
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
336-473 |
1.08e-15 |
|
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: 79.74 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 336 HGIILVTGPTGSGKTTTLySSLKQLATEQVNVCTIEDPIEMLEPSFN-------QMQVNHAIELGFADGVRALMRQDPDI 408
Cdd:COG0630 290 GKSVLVAGGTASGKTTLL-NALLSFIPPDAKIVTIEDTRELNLPHENwislvtrESFGGEEGDVTMFDLLKAALRQRPDY 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446943652 409 IMIGEIRDQDtANMAIQAALTGHLVLSTLHTNDAPSSLTRL--HDLGV-QPFLTAATIlgVLAQRLVR 473
Cdd:COG0630 369 IVVGEVRGEE-AYTLFQAMATGHGVLSTFHADSVESAINRLtsPPINVpRTLLQALDL--VVFQKRVR 433
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
339-453 |
3.69e-13 |
|
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: 71.35 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 339 ILVTGPTGSGKTTTLySSLKQLATEQVNVCTIEDPIEMlepsfnQMQVNHAI-------------ELGFADGVRALMRQD 405
Cdd:COG4962 185 ILVSGGTGSGKTTLL-NALSGFIPPDERIVTIEDAAEL------QLQHPHVVrletrppnvegagEVTLRDLVRNALRMR 257
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446943652 406 PDIIMIGEIRDQDTANMaIQAALTGHL-VLSTLHTNDAPSSLTRLHDLG 453
Cdd:COG4962 258 PDRIIVGEVRGAEALDM-LQAMNTGHDgSMSTLHANSARDALARLETLA 305
|
|
| PRK13894 |
PRK13894 |
conjugal transfer ATPase TrbB; Provisional |
326-452 |
1.60e-10 |
|
conjugal transfer ATPase TrbB; Provisional
Pssm-ID: 184377 Cd Length: 319 Bit Score: 62.45 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 326 QQWQRITQ--NSHGIILVTGPTGSGKTT----TLYSSLKQLATEQvnVCTIEDPIEMLEPSFNQMQVNHAIELGFADGVR 399
Cdd:PRK13894 136 AQREAIIAavRAHRNILVIGGTGSGKTTlvnaIINEMVIQDPTER--VFIIEDTGEIQCAAENYVQYHTSIDVNMTALLK 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446943652 400 ALMRQDPDIIMIGEIRDQDTANMaIQAALTGHL-VLSTLHTNDAPSSLTRLHDL 452
Cdd:PRK13894 214 TTLRMRPDRILVGEVRGPEALDL-LMAWNTGHEgGAATLHANNAKAGLDRLKSL 266
|
|
| T2SSE_N |
pfam05157 |
Type II secretion system (T2SS), protein E, N-terminal domain; This domain is found at the ... |
60-165 |
1.74e-10 |
|
Type II secretion system (T2SS), protein E, N-terminal domain; This domain is found at the N-terminus of members of the Type II secretion system protein E. Proteins in this subfamily are typically involved in Type 4 pilus biogenesis, though some are involved in other processes; for instance aggregation in Myxococcus xanthus. The structure of this domain is now known.
Pssm-ID: 428339 [Multi-domain] Cd Length: 108 Bit Score: 58.12 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 60 QAHLSLNRLCQWFADRAQLPLFVIDPLKADVSALTQVmSQEFAIRNHILAVEVHADRIVIGTDQPFQTDWLNNLEKsLAP 139
Cdd:pfam05157 4 LGLLSEEQLAQALAEQLGLPFVDLEALEIDPELLRLL-PREFARRHRVLPLREDGGTLVVAVADPLDLALLDELRF-LTG 81
|
90 100
....*....|....*....|....*.
gi 446943652 140 KKIERVFLNPEQLQRYLREYYQVSRA 165
Cdd:pfam05157 82 KRVEPVLATPSDIRRALERLYGSEES 107
|
|
| VirB11 |
TIGR02788 |
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ... |
339-449 |
1.70e-09 |
|
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for DNA transfer. VirB11 is believed to be an ATPase. VirB11 is a homolog of the P-like conjugation system TrbB protein and the Flp pilus sytem protein TadA.
Pssm-ID: 274301 Cd Length: 308 Bit Score: 59.29 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 339 ILVTGPTGSGKTTTLYSSLKQLATEQvNVCTIEDPIEMLEPSFNQMQ------VNHAIELGFADGVRALMRQDPDIIMIG 412
Cdd:TIGR02788 147 IIISGGTGSGKTTFLKSLVDEIPKDE-RIITIEDTREIFLPHPNYVHlfyskgGQGLAKVTPKDLLQSCLRMRPDRIILG 225
|
90 100 110
....*....|....*....|....*....|....*...
gi 446943652 413 EIRDqDTANMAIQAALTGHL-VLSTLHTNDAPSSLTRL 449
Cdd:TIGR02788 226 ELRG-DEAFDFIRAVNTGHPgSITTLHAGSPEEAFEQL 262
|
|
| PRK13851 |
PRK13851 |
type IV secretion system protein VirB11; Provisional |
339-452 |
1.42e-08 |
|
type IV secretion system protein VirB11; Provisional
Pssm-ID: 172375 Cd Length: 344 Bit Score: 56.83 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 339 ILVTGPTGSGKTT---TLYSSLKQlateQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGV------RALMRQDPDII 409
Cdd:PRK13851 165 MLLCGPTGSGKTTmskTLISAIPP----QERLITIEDTLELVIPHENHVRLLYSKNGAGLGAVtaehllQASLRMRPDRI 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446943652 410 MIGEIRDqDTANMAIQAALTGHL-VLSTLHTNDAPSSLTRLHDL 452
Cdd:PRK13851 241 LLGEMRD-DAAWAYLSEVVSGHPgSISTIHGANPVQGFKKLFSL 283
|
|
| PRK13833 |
PRK13833 |
conjugal transfer protein TrbB; Provisional |
339-452 |
3.19e-07 |
|
conjugal transfer protein TrbB; Provisional
Pssm-ID: 172360 [Multi-domain] Cd Length: 323 Bit Score: 52.49 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 339 ILVTGPTGSGKTTTLYSSLKQL--ATEQVNVCTIEDPIEMlepsfnQMQVNHAIELGFADGV------RALMRQDPDIIM 410
Cdd:PRK13833 147 IVISGGTGSGKTTLANAVIAEIvaSAPEDRLVILEDTAEI------QCAAENAVALHTSDTVdmarllKSTMRLRPDRII 220
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446943652 411 IGEIRDqDTANMAIQAALTGHL-VLSTLHTNDAPSSLTRLHDL 452
Cdd:PRK13833 221 VGEVRD-GAALTLLKAWNTGHPgGVTTIHSNTAMSALRRLEQL 262
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
329-428 |
1.75e-04 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 42.13 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 329 QRITQNSHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMlepsfNQMQVNHAIELGFADGVRALMRQ-DPD 407
Cdd:cd00009 12 EALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLL-----EGLVVAELFGHFLVRLLFELAEKaKPG 86
|
90 100
....*....|....*....|.
gi 446943652 408 IIMIGEIrdqDTANMAIQAAL 428
Cdd:cd00009 87 VLFIDEI---DSLSRGAQNAL 104
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
335-414 |
4.50e-04 |
|
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: 40.82 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446943652 335 SHGIILVTGPTGSGKTTTLYSSLKQLATEQVNVCTIEDPIEMLEPSFNQMQVNHAIELGFADGV------RALMRQ-DPD 407
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrlaLALARKlKPD 80
|
....*..
gi 446943652 408 IIMIGEI 414
Cdd:smart00382 81 VLILDEI 87
|
|
| EHD |
cd09913 |
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
65-104 |
7.31e-04 |
|
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.
Pssm-ID: 206740 Cd Length: 241 Bit Score: 41.49 E-value: 7.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446943652 65 LNRLCQWFADRAQLPLFVIDPLKADVS-----ALTQVMSQEFAIR 104
Cdd:cd09913 112 FNAVCRWFAERADLIFLLFDPHKLDISdefrrVIEQLKGHESKIR 156
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
309-353 |
4.54e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 39.24 E-value: 4.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446943652 309 DVLVRSFQQLGFDQSLLQQwqritqnsHGIILVTGPTGSGKTTTL 353
Cdd:TIGR03499 175 EALEGMLPVKPEEDPILEQ--------GGVIALVGPTGVGKTTTL 211
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
331-370 |
6.22e-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: 38.14 E-value: 6.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446943652 331 ITQNSHgiILVTGPTGSGKTTTLYSSLKQLATEQVNVCTI 370
Cdd:pfam12775 28 LKNGKP--VLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFI 65
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
337-353 |
6.78e-03 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 38.16 E-value: 6.78e-03
|
| |
