|
Name |
Accession |
Description |
Interval |
E-value |
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
1-324 |
3.80e-177 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 493.45 E-value: 3.80e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 1 MKLEEIVALSVKHNVSDLHLCNSAAPRWRRQGRLQPAPFP---APDIANLLNDWLDAAQLLHWQEHGQIDFALTLACGAR 77
Cdd:COG2805 3 MDLDELLKLAVEQGASDLHLTVGSPPMLRIDGELVPLDDPpltPEDLEALLKEILTEEQRERLEEEGELDFSYSLPGLGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 78 LRASAFAHTRGISLVLRLLPEQCPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLED 157
Cdd:COG2805 83 FRVNIFRQRGGVAAVLRLIPSEIPTLEELGLPPVLKELAELPRGLVLVTGPTGSGKSTTLAAMIDYINETRAKHIITIED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 158 PVEFIHHSERCLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERL 237
Cdd:COG2805 163 PIEFVHKHKKSLINQREVGRDTPSFANALRAALREDPDVILVGEMRDLETIEAALTAAETGHLVFATLHTNSAAQTIDRI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 238 IDVFPAEEKDQVRSQLAGSLCAVLAQKLLPARQG-GRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQS 316
Cdd:COG2805 243 IDVFPPEEQAQIRSQLAESLRGVISQRLLPRADGgGRVAAREILVNTPAVRNLIREGKTHQIPSLIQTGKKLGMQTMDQS 322
|
....*...
gi 489006021 317 FQQCVAAG 324
Cdd:COG2805 323 LAELVKEG 330
|
|
| pilT_fam |
TIGR01420 |
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ... |
2-324 |
3.30e-160 |
|
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: 451.00 E-value: 3.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 2 KLEEIVALSVKHNVSDLHLCNSAAPRWRRQGRLQP---APFPAPDIANLLNDWLDAAQLLHWQEHGQIDFALTLACGARL 78
Cdd:TIGR01420 1 SLEEILREAVKLGASDIHLTAGAPPAMRIDGDLVRiefEPLTPEDTQKLAREILSEKQREEFEENGELDFSFSLPGVGRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 79 RASAFAHTRGISLVLRLLPEQCPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLEDP 158
Cdd:TIGR01420 81 RVNAFYQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLASMIDYINKNKAYHIITIEDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 159 VEFIHHSERCLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLI 238
Cdd:TIGR01420 161 IEYVHTNKRSLINQREVGEDTLSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHLVFGTLHTNSAAQTIERII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 239 DVFPAEEKDQVRSQLAGSLCAVLAQKLLP-ARQGGRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQSF 317
Cdd:TIGR01420 241 DVFPAEEQEQIRTQLAESLVAIISQRLLPkADGGGRVLAVEILINTPAVRNLIREGKTHQIKSLIQTGQQLGMQTFDQHL 320
|
....*..
gi 489006021 318 QQCVAAG 324
Cdd:TIGR01420 321 AQLYKKG 327
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
100-321 |
1.52e-128 |
|
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: 366.09 E-value: 1.52e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 100 CPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLEDPVEFIHHSERCLIQQREVGRHC 179
Cdd:cd01131 1 IPTFEELGLPPVLKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINETRSKHIITIEDPIEFVHKHKKSLINQREVGRDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 180 PSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLIDVFPAEEKDQVRSQLAGSLCA 259
Cdd:cd01131 81 ESFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDVFPPEQQEQVRIQLASSLRG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489006021 260 VLAQKLLPARQG-GRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQSFQQCV 321
Cdd:cd01131 161 VISQRLLPKKDGgGRVAAFEILINTPAIRNLIREGKTHQIPSLIQTGARDGMQTMDQSLYELY 223
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
11-269 |
6.82e-48 |
|
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: 161.68 E-value: 6.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 11 VKHNVSDLHLC---NSAAPRWRRQGRLQPAPFPAPDIANLLNDWLDA-AQLLHWQEHGQIDFALTLAC---GARLRASAF 83
Cdd:pfam00437 8 LDEGASDIHVEppeRIVWIRFRVDGVLREIPFPDADALARLISRIKVmARLDISERRPPQDGRLPLRIggkGVRVRVSTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 84 AHTRGISLVLRLLPEQCPRL--DTLGAPPA----LSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLED 157
Cdd:pfam00437 88 PTAGGEKLVIRLLDPSNVALslDELGMTGAqdeaLLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTR-DENIVTVED 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 158 PVEF-IHHsercLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVER 236
Cdd:pfam00437 167 PVEIqLEG----INQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGALTR 242
|
250 260 270
....*....|....*....|....*....|....
gi 489006021 237 LID-VFPAEEkdqvrsqLAGSLCAVLAQKLLPAR 269
Cdd:pfam00437 243 LQDmGVPPFE-------LASSLLLVIAQRLVRKL 269
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
27-324 |
4.80e-33 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 126.97 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 27 RWRRQGRLQPAPFPAPDIANLLNDWLDAAQLLHWQEH-----GQidFALTLAcGAR--LRASAFAHTRGISLVLRLLP-- 97
Cdd:PRK10436 115 RLRIDGVLHPLPDPSPELGAALTARLKVLGNLDIAERrlpqdGQ--FTVELA-GNAysFRIATLPCRGGEKVVLRLLQqv 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 98 EQCPRLDTLGAPPA----LSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLEDPVEF---------IHH 164
Cdd:PRK10436 192 QQALDLETLGMTPAqlaqFRQALQQPQGLILVTGPTGSGKTVTLYSALQTLNTA-QINICSVEDPVEIplaginqtqIHP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 165 sercliqqrevgRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLidvfpaE 244
Cdd:PRK10436 271 ------------KAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRL------Q 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 245 EKDQVRSQLAGSLCAVLAQKL-----------------LPA--RQG------------------GRVALYELLVNTPAVA 287
Cdd:PRK10436 333 QMGIARWMLASALKLVIAQRLvrklcphcrqqasepihLPPniWPGplphwqavgcehcyhgyyGRTALFEVLPITPVLQ 412
|
330 340 350
....*....|....*....|....*....|....*..
gi 489006021 288 NLIREGkvHQLPGVMQTGMQAGMLTFTQSFQQCVAAG 324
Cdd:PRK10436 413 QAIASN--ASPEELETHARQQGMTTLFENGLLAVEQG 447
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
123-228 |
3.22e-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: 40.43 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 123 LLVTGATGSGKSTTLAAMVGHLN-QHLDGHILTLEDPVEFIHHSERCLIQQREV--GRHCPSFAAALRVALRQDPDVILL 199
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKasGSGELRLRLALALARKLKPDVLIL 84
|
90 100 110
....*....|....*....|....*....|..
gi 489006021 200 ---GELRDSETIRLALTAAETGHLVMATLHTR 228
Cdd:smart00382 85 deiTSLLDAEQEALLLLLEELRLLLLLKSEKN 116
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
1-324 |
3.80e-177 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 493.45 E-value: 3.80e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 1 MKLEEIVALSVKHNVSDLHLCNSAAPRWRRQGRLQPAPFP---APDIANLLNDWLDAAQLLHWQEHGQIDFALTLACGAR 77
Cdd:COG2805 3 MDLDELLKLAVEQGASDLHLTVGSPPMLRIDGELVPLDDPpltPEDLEALLKEILTEEQRERLEEEGELDFSYSLPGLGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 78 LRASAFAHTRGISLVLRLLPEQCPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLED 157
Cdd:COG2805 83 FRVNIFRQRGGVAAVLRLIPSEIPTLEELGLPPVLKELAELPRGLVLVTGPTGSGKSTTLAAMIDYINETRAKHIITIED 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 158 PVEFIHHSERCLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERL 237
Cdd:COG2805 163 PIEFVHKHKKSLINQREVGRDTPSFANALRAALREDPDVILVGEMRDLETIEAALTAAETGHLVFATLHTNSAAQTIDRI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 238 IDVFPAEEKDQVRSQLAGSLCAVLAQKLLPARQG-GRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQS 316
Cdd:COG2805 243 IDVFPPEEQAQIRSQLAESLRGVISQRLLPRADGgGRVAAREILVNTPAVRNLIREGKTHQIPSLIQTGKKLGMQTMDQS 322
|
....*...
gi 489006021 317 FQQCVAAG 324
Cdd:COG2805 323 LAELVKEG 330
|
|
| pilT_fam |
TIGR01420 |
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ... |
2-324 |
3.30e-160 |
|
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: 451.00 E-value: 3.30e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 2 KLEEIVALSVKHNVSDLHLCNSAAPRWRRQGRLQP---APFPAPDIANLLNDWLDAAQLLHWQEHGQIDFALTLACGARL 78
Cdd:TIGR01420 1 SLEEILREAVKLGASDIHLTAGAPPAMRIDGDLVRiefEPLTPEDTQKLAREILSEKQREEFEENGELDFSFSLPGVGRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 79 RASAFAHTRGISLVLRLLPEQCPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLEDP 158
Cdd:TIGR01420 81 RVNAFYQRGGVALVLRLIPSKIPTFEELGLPPVLRELAERPRGLILVTGPTGSGKSTTLASMIDYINKNKAYHIITIEDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 159 VEFIHHSERCLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLI 238
Cdd:TIGR01420 161 IEYVHTNKRSLINQREVGEDTLSFANALRAALREDPDVILIGEMRDLETVELALTAAETGHLVFGTLHTNSAAQTIERII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 239 DVFPAEEKDQVRSQLAGSLCAVLAQKLLP-ARQGGRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQSF 317
Cdd:TIGR01420 241 DVFPAEEQEQIRTQLAESLVAIISQRLLPkADGGGRVLAVEILINTPAVRNLIREGKTHQIKSLIQTGQQLGMQTFDQHL 320
|
....*..
gi 489006021 318 QQCVAAG 324
Cdd:TIGR01420 321 AQLYKKG 327
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
100-321 |
1.52e-128 |
|
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: 366.09 E-value: 1.52e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 100 CPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLEDPVEFIHHSERCLIQQREVGRHC 179
Cdd:cd01131 1 IPTFEELGLPPVLKDLALKPRGLVLVTGPTGSGKSTTLAAMIDYINETRSKHIITIEDPIEFVHKHKKSLINQREVGRDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 180 PSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLIDVFPAEEKDQVRSQLAGSLCA 259
Cdd:cd01131 81 ESFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIIDVFPPEQQEQVRIQLASSLRG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489006021 260 VLAQKLLPARQG-GRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQSFQQCV 321
Cdd:cd01131 161 VISQRLLPKKDGgGRVAAFEILINTPAIRNLIREGKTHQIPSLIQTGARDGMQTMDQSLYELY 223
|
|
| PilU |
COG5008 |
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures]; |
1-316 |
1.15e-117 |
|
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
Pssm-ID: 444032 Cd Length: 370 Bit Score: 344.00 E-value: 1.15e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 1 MKLEEIVALSVKHNVSDLHLCNSAAPRWRRQGRLQPA---PFPAPDIANLLNDWLDAAQLLHWQEHGQIDFALTLACGAR 77
Cdd:COG5008 1 MDLEDLLKLMVEKKASDLFITAGAPPSIKIDGKLTPLsqqPLTPEQVRELAYSIMNEEQREEFERTKECNFAISLPGVGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 78 LRASAFaHTRG-ISLVLRLLPEQCPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLDGHILTLE 156
Cdd:COG5008 81 FRVNAF-RQRGsVGMVLRRIETEIPTLDELGLPPVLKDLIMEKRGLVLFVGATGSGKSTTLAAMIDHRNENSSGHILTIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 157 DPVEFIHHSERCLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVER 236
Cdd:COG5008 160 DPIEFVHKHKKSIVTQREVGVDTESYEVALKNALRQAPDVILIGEIRDRETMEHAIAFAETGHLCLATLHANNANQALDR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 237 LIDVFPAEEKDQVRSQLAGSLCAVLAQKLLPARQGGRVALYELLVNTPAVANLIREGKVHQLPGVMQTGMQAGMLTFTQS 316
Cdd:COG5008 240 IINFFPEERRPQLLMDLSLNLRAIVSQRLVPTKDGGRVAAVEVLLNTPLIADLIRKGEIHEIKEAMEKSRELGMQTFDQA 319
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
110-281 |
1.77e-62 |
|
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: 196.44 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 110 PALSELLAEESGLLLVTGATGSGKSTTLAAMVGHL--NQHLDGHILTLEDPVEFIH---HSERCLIQQREVGRHCPSFAA 184
Cdd:cd19516 1 PDLVEALFPREGLVYVAGATGSGKSTLLAAIYRYIleNDPPDRKIITYEDPIEFVYdgiKSKHSIIVQSQIPRHFKSFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 185 ALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLIDVFPAEEKDQVRSQLAGSLCAVLAQK 264
Cdd:cd19516 81 AVREALRRKPSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLISLFPPEERDAAAYDLLSTLRFIIVQR 160
|
170
....*....|....*..
gi 489006021 265 LLPARQGGRVALYELLV 281
Cdd:cd19516 161 LVRTTDGKRVAVREYLV 177
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
112-281 |
5.03e-56 |
|
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: 179.22 E-value: 5.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 112 LSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLEDPVEFIHHSerclIQQREVGRHC-PSFAAALRVAL 190
Cdd:cd01129 3 LRRLIKRPHGLILVTGPTGSGKTTTLYAMLRELNGP-ERNIITIEDPVEYQIPG----INQSQVNEKIgLTFADALRAIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 191 RQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLIDVF-PAEEkdqvrsqLAGSLCAVLAQKLLpar 269
Cdd:cd01129 78 RQDPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGiEPFL-------LASALRGVIAQRLV--- 147
|
170
....*....|..
gi 489006021 270 qgGRVALYELLV 281
Cdd:cd01129 148 --GRTAIAEVLV 157
|
|
| plasmid_TraJ |
TIGR02525 |
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ... |
2-281 |
7.47e-52 |
|
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: 175.38 E-value: 7.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 2 KLEEIVALSVKHNVSDLHLcNSAAPRW-RRQGRLQPAP-FPAPDiANL--LNDWLDAAQLLHWQEHGQ-IDFALTLAC-- 74
Cdd:TIGR02525 11 TLRRFFVHCSRHEVSDIHL-QGGSPIVvERHGRQVPASsFPLDN-LELerLVDEVFGPEIKPTVKSGApVDRAIQLRGde 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 75 --------GARLR-------ASAFAHTRGISLVLRLLPEQCPRLDTLGAPPALSELLAEESGLLLVTGATGSGKSTTLAA 139
Cdd:TIGR02525 89 ngryglgrGERVRfrcnfiqATIGKLETAISLTLRVIPSDIPDLKQMGIEPDLFNSLLPAAGLGLICGETGSGKSTLAAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 140 MVGH-LNQHLDGHILTLEDPVEFIHHSERCLI--QQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAE 216
Cdd:TIGR02525 169 IYQHcGETYPDRKIVTYEDPIEYILGSPDDLLppAQSQIGRDVDSFANGIRLALRRAPKIIGVGEIRDLETFQAAVLAGQ 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489006021 217 TGHLVMATLHTRGAAPAVERLIDVFPAEEKDQVRSQLAGSLCAVLAQKLLPARQGGRVALYELLV 281
Cdd:TIGR02525 249 SGHFCLGTLHVKSPGEAISRCLQMYPPEMREAAAFDLLSILQYIIVQRLLRTTDGKRQAVREYIV 313
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
90-324 |
2.45e-50 |
|
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: 175.38 E-value: 2.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 90 SLVLRLLP--EQCPRLDTLGAPP----ALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLEDPVEFIH 163
Cdd:COG2804 277 KVVLRILDksAALLDLEQLGFSPdqleRLRRLIRRPHGIILVTGPTGSGKTTTLYAALNELNTP-ERNIITVEDPVEYQL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 164 HsercLIQQ----REVGRhcpSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLID 239
Cdd:COG2804 356 P----GINQvqvnPKIGL---TFASALRSILRQDPDVIMVGEIRDLETAEIAVQAALTGHLVLSTLHTNDAPSAITRLLD 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 240 --VFPAEekdqvrsqLAGSLCAVLAQKL-----------------------LPARQG--------------------GRV 274
Cdd:COG2804 429 mgVEPFL--------LASSLLGVLAQRLvrrlcphckepyepdpeelerlgLPPEELapltfyrgvgcehcngtgykGRT 500
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489006021 275 ALYELLVNTPAVANLIREGK-VHQLpgvMQTGMQAGMLTFTQSFQQCVAAG 324
Cdd:COG2804 501 GIYELLVIDDELRELIAEGAsAAEL---REAARKEGMRTLREDGLEKVLQG 548
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
11-269 |
6.82e-48 |
|
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: 161.68 E-value: 6.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 11 VKHNVSDLHLC---NSAAPRWRRQGRLQPAPFPAPDIANLLNDWLDA-AQLLHWQEHGQIDFALTLAC---GARLRASAF 83
Cdd:pfam00437 8 LDEGASDIHVEppeRIVWIRFRVDGVLREIPFPDADALARLISRIKVmARLDISERRPPQDGRLPLRIggkGVRVRVSTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 84 AHTRGISLVLRLLPEQCPRL--DTLGAPPA----LSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLED 157
Cdd:pfam00437 88 PTAGGEKLVIRLLDPSNVALslDELGMTGAqdeaLLEFLRQPRGNILVTGPTGSGKTTTLYAALGELNTR-DENIVTVED 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 158 PVEF-IHHsercLIQQREVGRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVER 236
Cdd:pfam00437 167 PVEIqLEG----INQVQLNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIALQAANTGHLVLSTLHTNSAAGALTR 242
|
250 260 270
....*....|....*....|....*....|....
gi 489006021 237 LID-VFPAEEkdqvrsqLAGSLCAVLAQKLLPAR 269
Cdd:pfam00437 243 LQDmGVPPFE-------LASSLLLVIAQRLVRKL 269
|
|
| type_II_gspE |
TIGR02533 |
type II secretion system protein E; This family describes GspE, the E protein of the type II ... |
6-325 |
5.28e-46 |
|
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: 162.55 E-value: 5.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 6 IVALSVKHNVSDLHLC---NSAAPRWRRQGRLQPAPFPAPDIANLLNDW------LDAAQLLHWQEhGQIdfalTLACGA 76
Cdd:TIGR02533 115 LLSRAVKERASDIHIEpfeKALVVRFRVDGVLRDVLSPPKKLHAALVSRvkimakLNIAEKRLPQD-GRI----SLRVGG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 77 R---LRASAFAHTRGISLVLRLLPEQCPRLD--TLGAPP----ALSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQH 147
Cdd:TIGR02533 190 RdidIRVSTVPTSHGERVVMRLLDKTAVRLDleTLGMSPellsRFERLIRRPHGIILVTGPTGSGKTTTLYAALSRLNTP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 148 lDGHILTLEDPVEFIHHSerclIQQREVG-RHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLH 226
Cdd:TIGR02533 270 -ERNILTVEDPVEYQIEG----IGQIQVNpKIGLTFAAGLRAILRQDPDIIMVGEIRDLETAQIAIQASLTGHLVLSTLH 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 227 TRGAAPAVERLID--VFPAeekdqvrsQLAGSLCAVLAQKLL-----------PARQG---------------------- 271
Cdd:TIGR02533 345 TNDAAGAVTRLIDmgVEPF--------LLASSLLGVLAQRLVrrlcphckepyEATPEeialfgispegpinlyrpvgcp 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489006021 272 --------GRVALYELLVNTPAVANLIREGKVHQlpGVMQTGMQAGMLTFTQSFQQCVAAGA 325
Cdd:TIGR02533 417 hcnhtgylGRTGIYELLIVDDDLRSLIHSRADEG--EIKEIARAAGMRTLRDDGLRKVLAGI 476
|
|
| type_IV_pilB |
TIGR02538 |
type IV-A pilus assembly ATPase PilB; This model describes a protein of type IV pilus ... |
11-324 |
2.30e-33 |
|
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: 128.98 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 11 VKHNVSDLHLC---NSAAPRWRRQGRLQPAPFPAPDIANLLNDWLDAAQLLHWQEH-----GQIDFALTLACGARLRASA 82
Cdd:TIGR02538 193 IRKGASDIHFEpyeKSYRVRFRIDGILHEVAQPPLALANRIAARIKVMSRLDIAEKripqdGRIKLKLSKSKAIDFRVST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 83 FAHTRGISLVLRLLPEQCPRLD--TLGAPPA----LSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLE 156
Cdd:TIGR02538 273 LPTLFGEKVVLRILDSSAAQLDidKLGFEPDqkalFLEAIHKPQGMVLVTGPTGSGKTVSLYTALNILNTE-EVNISTAE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 157 DPVEF----IHHserclIQQRE-VGRhcpSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAA 231
Cdd:TIGR02538 352 DPVEInlpgINQ-----VNVNPkIGL---TFAAALRSFLRQDPDIIMVGEIRDLETAEIAIKAAQTGHLVLSTLHTNDAP 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 232 PAVERLID--VFP---AEEKDQVRSQ-LAGSLC---------------------AVLAQKLLPARQG----------GRV 274
Cdd:TIGR02538 424 ETLARLVNmgIAPfniASSVNLIMAQrLARRLCshckapeevpaeallelgftqEDLADLKLYGPVGcdecsntgykGRV 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489006021 275 ALYELLVNTPAVANLIREGKvhqlpGVMQTGMQA---GMLTFTQSFQQCVAAG 324
Cdd:TIGR02538 504 GIYEVMPMSEEIAELILKGG-----NALQIAELAqkeGMRTLRRSGLLKVKQG 551
|
|
| PRK10436 |
PRK10436 |
hypothetical protein; Provisional |
27-324 |
4.80e-33 |
|
hypothetical protein; Provisional
Pssm-ID: 236694 Cd Length: 462 Bit Score: 126.97 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 27 RWRRQGRLQPAPFPAPDIANLLNDWLDAAQLLHWQEH-----GQidFALTLAcGAR--LRASAFAHTRGISLVLRLLP-- 97
Cdd:PRK10436 115 RLRIDGVLHPLPDPSPELGAALTARLKVLGNLDIAERrlpqdGQ--FTVELA-GNAysFRIATLPCRGGEKVVLRLLQqv 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 98 EQCPRLDTLGAPPA----LSELLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHlDGHILTLEDPVEF---------IHH 164
Cdd:PRK10436 192 QQALDLETLGMTPAqlaqFRQALQQPQGLILVTGPTGSGKTVTLYSALQTLNTA-QINICSVEDPVEIplaginqtqIHP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 165 sercliqqrevgRHCPSFAAALRVALRQDPDVILLGELRDSETIRLALTAAETGHLVMATLHTRGAAPAVERLidvfpaE 244
Cdd:PRK10436 271 ------------KAGLTFQRVLRALLRQDPDVIMVGEIRDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRL------Q 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 245 EKDQVRSQLAGSLCAVLAQKL-----------------LPA--RQG------------------GRVALYELLVNTPAVA 287
Cdd:PRK10436 333 QMGIARWMLASALKLVIAQRLvrklcphcrqqasepihLPPniWPGplphwqavgcehcyhgyyGRTALFEVLPITPVLQ 412
|
330 340 350
....*....|....*....|....*....|....*..
gi 489006021 288 NLIREGkvHQLPGVMQTGMQAGMLTFTQSFQQCVAAG 324
Cdd:PRK10436 413 QAIASN--ASPEELETHARQQGMTTLFENGLLAVEQG 447
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
121-239 |
8.13e-23 |
|
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: 92.84 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 121 GLLLVTGATGSGKSTTLAAMVGHLNQhlDGHILTLEDPVEFIHHSERCLIQQREVGRhcPSFAAALRVALRQDPDVILLG 200
Cdd:cd19477 11 KNVIVCGGTGSGKTTYIKSILEFIPK--EERIISIEDTEEIVFKHHKNYTQLFFGGN--ITSADCLKSCLRQRPDRIILG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489006021 201 ELRDSETiRLALTAAETGH-LVMATLHTRGAAPAVERLID 239
Cdd:cd19477 87 ELRSSEA-YDFYNVLCSGHkGTLTTLHAGSSEEAFIRLAN 125
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
124-238 |
1.62e-17 |
|
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: 78.74 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 124 LVTGATGSGKSTTLAAMVGHLnqHLDGHILTLEDPVEFIHHSERC--LIQQREVGRHCP-SFAAALRVALRQDPDVILLG 200
Cdd:cd01130 16 LISGGTGSGKTTLLNALLSFI--PPDERIVTIEDTRELQLPHPNVvhLLTRPGGGEKGEvTMADLLKAALRMRPDRIIVG 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 489006021 201 ELRDSEtIRLALTAAETGHL-VMATLHTRGAAPAVERLI 238
Cdd:cd01130 94 EVRGGE-AYDMLQAMNTGHPgSITTIHANSAEDAIDRLA 131
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
70-237 |
2.44e-14 |
|
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: 72.89 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 70 LTLACGARLRA-SAFAHTRGISLVLRLLPEQCPRLDTL---GA-PPALSELLAE--ESGL-LLVTGATGSGKSTTLAAMV 141
Cdd:COG4962 124 ARLPDGSRVNAvIPPVARDGPSLSIRKFRKRPLTLEDLvalGSlTPEMAEFLRAavRARLnILVSGGTGSGKTTLLNALS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 142 GHLNQHLdgHILTLEDPVE-FIHHsercliqqrevgRHCPSFAA---------------ALRVALRQDPDVILLGELRDS 205
Cdd:COG4962 204 GFIPPDE--RIVTIEDAAElQLQH------------PHVVRLETrppnvegagevtlrdLVRNALRMRPDRIIVGEVRGA 269
|
170 180 190
....*....|....*....|....*....|...
gi 489006021 206 ETIRLaLTAAETGHL-VMATLHTRGAAPAVERL 237
Cdd:COG4962 270 EALDM-LQAMNTGHDgSMSTLHANSARDALARL 301
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
115-239 |
7.48e-14 |
|
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: 71.65 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 115 LLAEESGLLLVTGATGSGKSTTLAAMVGHLNQHLdgHILTLEDPVE-FIHHSerclIQQREVGRhcPSFAAA-------- 185
Cdd:COG0630 285 LLLENGKSVLVAGGTASGKTTLLNALLSFIPPDA--KIVTIEDTRElNLPHE----NWISLVTR--ESFGGEegdvtmfd 356
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489006021 186 -LRVALRQDPDVILLGELRDSEtIRLALTAAETGHLVMATLHTRGAAPAVERLID 239
Cdd:COG0630 357 lLKAALRQRPDYIVVGEVRGEE-AYTLFQAMATGHGVLSTFHADSVESAINRLTS 410
|
|
| PRK13894 |
PRK13894 |
conjugal transfer ATPase TrbB; Provisional |
123-237 |
3.38e-08 |
|
conjugal transfer ATPase TrbB; Provisional
Pssm-ID: 184377 Cd Length: 319 Bit Score: 53.98 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 123 LLVTGATGSGKSTTLAAMVGHLNQHlDGH--ILTLEDPVEFIHHSERClIQQR---EVgrhcpSFAAALRVALRQDPDVI 197
Cdd:PRK13894 151 ILVIGGTGSGKTTLVNAIINEMVIQ-DPTerVFIIEDTGEIQCAAENY-VQYHtsiDV-----NMTALLKTTLRMRPDRI 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489006021 198 LLGELRDSETIRLaLTAAETGHL-VMATLHTRGAAPAVERL 237
Cdd:PRK13894 224 LVGEVRGPEALDL-LMAWNTGHEgGAATLHANNAKAGLDRL 263
|
|
| PRK13851 |
PRK13851 |
type IV secretion system protein VirB11; Provisional |
123-233 |
1.10e-04 |
|
type IV secretion system protein VirB11; Provisional
Pssm-ID: 172375 Cd Length: 344 Bit Score: 43.35 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 123 LLVTGATGSGKSTTLAAMVGHLNQHldGHILTLEDPVEFIHHSE---RCLIQQREVGRHCPSFAAALRVALRQDPDVILL 199
Cdd:PRK13851 165 MLLCGPTGSGKTTMSKTLISAIPPQ--ERLITIEDTLELVIPHEnhvRLLYSKNGAGLGAVTAEHLLQASLRMRPDRILL 242
|
90 100 110
....*....|....*....|....*....|....*
gi 489006021 200 GELRDsETIRLALTAAETGHL-VMATLHtrGAAPA 233
Cdd:PRK13851 243 GEMRD-DAAWAYLSEVVSGHPgSISTIH--GANPV 274
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
123-228 |
3.22e-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: 40.43 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 123 LLVTGATGSGKSTTLAAMVGHLN-QHLDGHILTLEDPVEFIHHSERCLIQQREV--GRHCPSFAAALRVALRQDPDVILL 199
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKasGSGELRLRLALALARKLKPDVLIL 84
|
90 100 110
....*....|....*....|....*....|..
gi 489006021 200 ---GELRDSETIRLALTAAETGHLVMATLHTR 228
Cdd:smart00382 85 deiTSLLDAEQEALLLLLEELRLLLLLKSEKN 116
|
|
| PRK13900 |
PRK13900 |
type IV secretion system ATPase VirB11; Provisional |
123-237 |
9.18e-04 |
|
type IV secretion system ATPase VirB11; Provisional
Pssm-ID: 184381 Cd Length: 332 Bit Score: 40.51 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489006021 123 LLVTGATGSGKSTTLAAMVGHLNQhlDGHILTLEDPVEFI--HHSERC--LIQQREVGRHCPSFAAALRVALRQDPDVIL 198
Cdd:PRK13900 163 IIISGGTSTGKTTFTNAALREIPA--IERLITVEDAREIVlsNHPNRVhlLASKGGQGRAKVTTQDLIEACLRLRPDRII 240
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489006021 199 LGELRDSETIRLaLTAAETGHL-VMATLHTRGAAPAVERL 237
Cdd:PRK13900 241 VGELRGAEAFSF-LRAINTGHPgSISTLHADSPAMAIEQL 279
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
122-152 |
8.15e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 37.06 E-value: 8.15e-03
10 20 30
....*....|....*....|....*....|.
gi 489006021 122 LLLVTGATGSGKSTTLAAMVGHLnQHLDGHI 152
Cdd:cd03250 33 LVAIVGPVGSGKSSLLSALLGEL-EKLSGSV 62
|
|
| |
