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Conserved domains on  [gi|817233824|ref|WP_046543862|]
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MULTISPECIES: CpaF family protein [Burkholderia]

Protein Classification

CpaF family protein( domain architecture ID 10008984)

CpaF family protein is an ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer; similar to Aggregatibacter actinomycetemcomitans TadA, a predicted secretion NTPase that is required for adherence

Gene Ontology:  GO:0005524|GO:0016887
PubMed:  11226268

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 15-329 1.24e-88

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: 270.50  E-value: 1.24e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  15 LGPLKDLFEDPAVTEVMVNPGGIVYAERAGEMIYIEDAGLAEVHITSAIRALA----KSVDESveanTPktFISASVEN- 89
Cdd:COG4962   56 LGPLEPLLDDPDVTDIMVNGPDEVFVERGGRLERTDVRFDSEEELRRLIERIAarvgRRLDES----SP--IVDARLPDg 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  90 LRIAGALSPASHGGPSLCIRKHQEEgaRPNLGELVEKGMLTNAQAELLEQLfVHEKKNVMVGGPTGSGKTTLANALCMRI 169
Cdd:COG4962  130 SRVNAVIPPVARDGPSLSIRKFRKR--PLTLEDLVALGSLTPEMAEFLRAA-VRARLNILVSGGTGSGKTTLLNALSGFI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 170 PPYERVISVEDSIELHPNLKHHVRYLT---NA--TKGVT-AQLVVQhTLRARPDRLIVGETRGAETFDLIRAFNSGHDGS 243
Cdd:COG4962  207 PPDERIVTIEDAAELQLQHPHVVRLETrppNVegAGEVTlRDLVRN-ALRMRPDRIIVGEVRGAEALDMLQAMNTGHDGS 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 244 LSTVHASSATDMLYAIEMLYQMSlppDASLSPEAVRGYIARAVHVCVHVTRsvkqGEDGKyyyvRRVNEIVRVNGVENGK 323
Cdd:COG4962  286 MSTLHANSARDALARLETLALMA---GENLPREAVRRQIASAIDLVVHLER----LRDGR----RRVTEIAEVTGMEGGR 354


                 ....*.
gi 817233824 324 YLLESL 329
Cdd:COG4962  355 VVLQPI 360
 
Name Accession Description Interval E-value
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 15-329 1.24e-88

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: 270.50  E-value: 1.24e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  15 LGPLKDLFEDPAVTEVMVNPGGIVYAERAGEMIYIEDAGLAEVHITSAIRALA----KSVDESveanTPktFISASVEN- 89
Cdd:COG4962   56 LGPLEPLLDDPDVTDIMVNGPDEVFVERGGRLERTDVRFDSEEELRRLIERIAarvgRRLDES----SP--IVDARLPDg 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  90 LRIAGALSPASHGGPSLCIRKHQEEgaRPNLGELVEKGMLTNAQAELLEQLfVHEKKNVMVGGPTGSGKTTLANALCMRI 169
Cdd:COG4962  130 SRVNAVIPPVARDGPSLSIRKFRKR--PLTLEDLVALGSLTPEMAEFLRAA-VRARLNILVSGGTGSGKTTLLNALSGFI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 170 PPYERVISVEDSIELHPNLKHHVRYLT---NA--TKGVT-AQLVVQhTLRARPDRLIVGETRGAETFDLIRAFNSGHDGS 243
Cdd:COG4962  207 PPDERIVTIEDAAELQLQHPHVVRLETrppNVegAGEVTlRDLVRN-ALRMRPDRIIVGEVRGAEALDMLQAMNTGHDGS 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 244 LSTVHASSATDMLYAIEMLYQMSlppDASLSPEAVRGYIARAVHVCVHVTRsvkqGEDGKyyyvRRVNEIVRVNGVENGK 323
Cdd:COG4962  286 MSTLHANSARDALARLETLALMA---GENLPREAVRRQIASAIDLVVHLER----LRDGR----RRVTEIAEVTGMEGGR 354


                 ....*.
gi 817233824 324 YLLESL 329
Cdd:COG4962  355 VVLQPI 360
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
 11-329 3.27e-58

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 190.34  E-value: 3.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  11 LKQNLGP-LKDLFEDPAVTEVMVNPGGIVYAERAGE-MIYIEDagLAEVHITSAIRALAKSVDESVEANTPKTFISASVE 88
Cdd:PRK13894  18 LERDMGPeLLAALNDPKTVEIMLNADGKLWQERLGEpMRCIGT--LRVAQAQAIIETIAGYHGKEVTRSKPILEGELPLD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  89 NLRIAGALSPASHGgPSLCIRKhqEEGARPNLGELVEKGMLTNAQAELLEQLfVHEKKNVMVGGPTGSGKTTLANALC-- 166
Cdd:PRK13894  96 GSRFAGQLPPVVPA-PTFAIRK--KAVAIFTLDQYVERGIMTAAQREAIIAA-VRAHRNILVIGGTGSGKTTLVNAIIne 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 167 -MRIPPYERVISVEDSIELHPNLKHHVRYLTnaTKGVTAQLVVQHTLRARPDRLIVGETRGAETFDLIRAFNSGHDGSLS 245
Cdd:PRK13894 172 mVIQDPTERVFIIEDTGEIQCAAENYVQYHT--SIDVNMTALLKTTLRMRPDRILVGEVRGPEALDLLMAWNTGHEGGAA 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 246 TVHASSATDMLYAIEMLYQMSlpPDAslsPEAVRGYIARAVHVCVHVTRSvkqgEDGkyyyvRRVNEIVRVNGVENGKYL 325
Cdd:PRK13894 250 TLHANNAKAGLDRLKSLISMH--PDA---PKPIEPLIGEAVHVVVHIART----PGG-----RRIQEILEVSGYANGQYI 315


                 ....
gi 817233824 326 LESL 329
Cdd:PRK13894 316 TKTL 319
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 133-316 4.19e-55

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: 177.35  E-value: 4.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 133 QAELLEQLfVHEKKNVMVGGPTGSGKTTLANALCMRIPPYERVISVEDSIELHPNLKHHVRYLTNATKG----VTAQLVV 208
Cdd:cd01130    1 MAAFLRLA-VRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGGGekgeVTMADLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 209 QHTLRARPDRLIVGETRGAETFDLIRAFNSGHDGSLSTVHASSATDMLYAIEMLYQMSlppDASLSPEAVRGYIARAVHV 288
Cdd:cd01130   80 KAALRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVLEA---GVNLDEEALRRLIASAIDV 156

                        170       180
                 ....*....|....*....|....*...
gi 817233824 289 CVHVTRSvkqgedgkYYYVRRVNEIVRV 316
Cdd:cd01130  157 IVHVKRL--------GDGVRRVTEIYEV 176
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
 22-294 1.90e-51

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: 172.54  E-value: 1.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   22 FEDPAVTEVMVNPGGIVYAERAGEMIYIEDAGLAEVHITSAIRALAKSVDESVEANTPktFISASVEN-LRIAGALSPAS 100
Cdd:TIGR02788   2 LDDEDVTEICINRPGEVWVEGPGGWQRFDVPDLTFSHLMRLARAIASFSKQSISEENP--ILSATLPGgERVQIVIPPAC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  101 HGG-PSLCIRKHQEegARPNLGELVEKGM----------LTNAQAELLE-----------QLFVHEKKNVMVGGPTGSGK 158
Cdd:TIGR02788  80 ENDtVSITIRKPSL--VDFSLDDYEEKGFfdtvraqsgtLSDNDEQLLElldagdikeflRLAIASRKNIIISGGTGSGK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  159 TTLANALCMRIPPYERVISVEDSIEL---HPNlKHHVRYLTNAT--KGVTAQLVVQHTLRARPDRLIVGETRGAETFDLI 233
Cdd:TIGR02788 158 TTFLKSLVDEIPKDERIITIEDTREIflpHPN-YVHLFYSKGGQglAKVTPKDLLQSCLRMRPDRIILGELRGDEAFDFI 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817233824  234 RAFNSGHDGSLSTVHASSATDmlyAIEMLYQMSLPPDAS--LSPEAVRGYIARAVHVCVHVTR 294
Cdd:TIGR02788 237 RAVNTGHPGSITTLHAGSPEE---AFEQLALMVKSSQAGlgLDFAYIVKLVREVIDIVVQINR 296
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
 14-271 5.49e-39

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: 138.96  E-value: 5.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   14 NLGPLKDLfeDPAVTEVMVNPGG--IVYAERAG----EMIYIEDAGLAEVhiTSAIRALAK-SVDES---VEANTPKTFI 83
Cdd:pfam00437   1 NLIPLEAL--DEGASDIHVEPPEriVWIRFRVDgvlrEIPFPDADALARL--ISRIKVMARlDISERrppQDGRLPLRIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   84 SASVEnLRIAgalSPASHGGPSLCIRKHQEEGARPNLGELVEKGMLTNAQAELLEQLfvheKKNVMVGGPTGSGKTTLAN 163
Cdd:pfam00437  77 GKGVR-VRVS---TLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQP----RGNILVTGPTGSGKTTTLY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  164 ALCMRIPPY-ERVISVEDSIELHPNLKHHVRylTNATKGVTAQLVVQHTLRARPDRLIVGETRGAETFDL-IRAFNSGHD 241
Cdd:pfam00437 149 AALGELNTRdENIVTVEDPVEIQLEGINQVQ--LNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIaLQAANTGHL 226

                         250       260       270
                  ....*....|....*....|....*....|
gi 817233824  242 GsLSTVHASSATDmlyAIEMLYQMSLPPDA 271
Cdd:pfam00437 227 V-LSTLHTNSAAG---ALTRLQDMGVPPFE 252
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
89-252 1.92e-15

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 74.79  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  89 NLRiagaLS--PASHGGPSLCIR-KHQEEGARPNLgelvekgmLTNAQAELLEQLFVHEKKNVMVGGPTGSGKTTLANAL 165
Cdd:NF041000  81 SLR----LStvGDFLGRESLVIRlLYQLEQIKPQL--------FFPEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 166 CMRIPPYERVISVEDSIElhpnlKHHVRYL---TNATKGVTAQLVVQHTLRARPDRLIVGETRGAETFDL-IRAFNSGHD 241
Cdd:NF041000 149 ARKLALNKQVITIEDPVE-----IKEPNFLqlqVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAaIRAALTGHL 223

                        170
                 ....*....|.
gi 817233824 242 gSLSTVHASSA 252
Cdd:NF041000 224 -VLSTVHAKSA 233
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 145-215 5.19e-05

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: 42.75  E-value: 5.19e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817233824   145 KKNVMVGGPTGSGKTTLANALCMRIPPYER---VISVEDSIELHPNLKHHVRYLTNATKGVTAQLVVQHTLRAR 215
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR 75
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 128-168 1.42e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 817233824 128 MLTNAQ-AELLEQLFVHEKKNVMVGGPTGSGKTTLANALCMR 168
Cdd:NF038214  72 GLDKAQiRELATLDFIERAENVLLLGPPGTGKTHLAIALGYA 113
 
Name Accession Description Interval E-value
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 15-329 1.24e-88

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: 270.50  E-value: 1.24e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  15 LGPLKDLFEDPAVTEVMVNPGGIVYAERAGEMIYIEDAGLAEVHITSAIRALA----KSVDESveanTPktFISASVEN- 89
Cdd:COG4962   56 LGPLEPLLDDPDVTDIMVNGPDEVFVERGGRLERTDVRFDSEEELRRLIERIAarvgRRLDES----SP--IVDARLPDg 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  90 LRIAGALSPASHGGPSLCIRKHQEEgaRPNLGELVEKGMLTNAQAELLEQLfVHEKKNVMVGGPTGSGKTTLANALCMRI 169
Cdd:COG4962  130 SRVNAVIPPVARDGPSLSIRKFRKR--PLTLEDLVALGSLTPEMAEFLRAA-VRARLNILVSGGTGSGKTTLLNALSGFI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 170 PPYERVISVEDSIELHPNLKHHVRYLT---NA--TKGVT-AQLVVQhTLRARPDRLIVGETRGAETFDLIRAFNSGHDGS 243
Cdd:COG4962  207 PPDERIVTIEDAAELQLQHPHVVRLETrppNVegAGEVTlRDLVRN-ALRMRPDRIIVGEVRGAEALDMLQAMNTGHDGS 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 244 LSTVHASSATDMLYAIEMLYQMSlppDASLSPEAVRGYIARAVHVCVHVTRsvkqGEDGKyyyvRRVNEIVRVNGVENGK 323
Cdd:COG4962  286 MSTLHANSARDALARLETLALMA---GENLPREAVRRQIASAIDLVVHLER----LRDGR----RRVTEIAEVTGMEGGR 354


                 ....*.
gi 817233824 324 YLLESL 329
Cdd:COG4962  355 VVLQPI 360
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
 11-329 3.27e-58

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 190.34  E-value: 3.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  11 LKQNLGP-LKDLFEDPAVTEVMVNPGGIVYAERAGE-MIYIEDagLAEVHITSAIRALAKSVDESVEANTPKTFISASVE 88
Cdd:PRK13894  18 LERDMGPeLLAALNDPKTVEIMLNADGKLWQERLGEpMRCIGT--LRVAQAQAIIETIAGYHGKEVTRSKPILEGELPLD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  89 NLRIAGALSPASHGgPSLCIRKhqEEGARPNLGELVEKGMLTNAQAELLEQLfVHEKKNVMVGGPTGSGKTTLANALC-- 166
Cdd:PRK13894  96 GSRFAGQLPPVVPA-PTFAIRK--KAVAIFTLDQYVERGIMTAAQREAIIAA-VRAHRNILVIGGTGSGKTTLVNAIIne 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 167 -MRIPPYERVISVEDSIELHPNLKHHVRYLTnaTKGVTAQLVVQHTLRARPDRLIVGETRGAETFDLIRAFNSGHDGSLS 245
Cdd:PRK13894 172 mVIQDPTERVFIIEDTGEIQCAAENYVQYHT--SIDVNMTALLKTTLRMRPDRILVGEVRGPEALDLLMAWNTGHEGGAA 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 246 TVHASSATDMLYAIEMLYQMSlpPDAslsPEAVRGYIARAVHVCVHVTRSvkqgEDGkyyyvRRVNEIVRVNGVENGKYL 325
Cdd:PRK13894 250 TLHANNAKAGLDRLKSLISMH--PDA---PKPIEPLIGEAVHVVVHIART----PGG-----RRIQEILEVSGYANGQYI 315


                 ....
gi 817233824 326 LESL 329
Cdd:PRK13894 316 TKTL 319
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 133-316 4.19e-55

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: 177.35  E-value: 4.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 133 QAELLEQLfVHEKKNVMVGGPTGSGKTTLANALCMRIPPYERVISVEDSIELHPNLKHHVRYLTNATKG----VTAQLVV 208
Cdd:cd01130    1 MAAFLRLA-VRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGGGekgeVTMADLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 209 QHTLRARPDRLIVGETRGAETFDLIRAFNSGHDGSLSTVHASSATDMLYAIEMLYQMSlppDASLSPEAVRGYIARAVHV 288
Cdd:cd01130   80 KAALRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVLEA---GVNLDEEALRRLIASAIDV 156

                        170       180
                 ....*....|....*....|....*...
gi 817233824 289 CVHVTRSvkqgedgkYYYVRRVNEIVRV 316
Cdd:cd01130  157 IVHVKRL--------GDGVRRVTEIYEV 176
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
 22-294 1.90e-51

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: 172.54  E-value: 1.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   22 FEDPAVTEVMVNPGGIVYAERAGEMIYIEDAGLAEVHITSAIRALAKSVDESVEANTPktFISASVEN-LRIAGALSPAS 100
Cdd:TIGR02788   2 LDDEDVTEICINRPGEVWVEGPGGWQRFDVPDLTFSHLMRLARAIASFSKQSISEENP--ILSATLPGgERVQIVIPPAC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  101 HGG-PSLCIRKHQEegARPNLGELVEKGM----------LTNAQAELLE-----------QLFVHEKKNVMVGGPTGSGK 158
Cdd:TIGR02788  80 ENDtVSITIRKPSL--VDFSLDDYEEKGFfdtvraqsgtLSDNDEQLLElldagdikeflRLAIASRKNIIISGGTGSGK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  159 TTLANALCMRIPPYERVISVEDSIEL---HPNlKHHVRYLTNAT--KGVTAQLVVQHTLRARPDRLIVGETRGAETFDLI 233
Cdd:TIGR02788 158 TTFLKSLVDEIPKDERIITIEDTREIflpHPN-YVHLFYSKGGQglAKVTPKDLLQSCLRMRPDRIILGELRGDEAFDFI 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817233824  234 RAFNSGHDGSLSTVHASSATDmlyAIEMLYQMSLPPDAS--LSPEAVRGYIARAVHVCVHVTR 294
Cdd:TIGR02788 237 RAVNTGHPGSITTLHAGSPEE---AFEQLALMVKSSQAGlgLDFAYIVKLVREVIDIVVQINR 296
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
 11-313 2.34e-47

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 162.62  E-value: 2.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  11 LKQNLGPLKDLFEDPAVTEVMVNPGGIVYAERAGEMIYIEDAGLAEVHITSAIRALAKSVDESVEANTPktFISASVEN- 89
Cdd:PRK13900   8 LETYLEPLKNIFAEDGVNEISINKPGEVWVEKKGDIRCEQIPELDLSHLKALGRLVAQATEQKISEEKP--LLSATLPNg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  90 LRIAGALSPASHGGP-SLCIRK----------HQEEGARPNLGELVEKGMLTNAQAELLEQ--------LFVHEKKNVMV 150
Cdd:PRK13900  86 YRIQIVFPPACEIGQiVYSIRKpsgmqltlddYEKMGAFDETATESLVDEDDVILNELLAEkkikefleHAVISKKNIII 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 151 GGPTGSGKTTLANALCMRIPPYERVISVEDSIEL----HPNLKHHVryltnATKG------VTAQLVVQHTLRARPDRLI 220
Cdd:PRK13900 166 SGGTSTGKTTFTNAALREIPAIERLITVEDAREIvlsnHPNRVHLL-----ASKGgqgrakVTTQDLIEACLRLRPDRII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 221 VGETRGAETFDLIRAFNSGHDGSLSTVHASSATdmlYAIEMLYQMSLPPDASLSPEAVRGYIARAVHVCVHvtrsVKQGE 300
Cdd:PRK13900 241 VGELRGAEAFSFLRAINTGHPGSISTLHADSPA---MAIEQLKLMVMQAGLGMPPDQIKKYILNVVDIVVQ----LKRGS 313

                        330
                 ....*....|...
gi 817233824 301 DGKyyyvRRVNEI 313
Cdd:PRK13900 314 GGK----RYVSEI 322
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
 15-321 3.84e-42

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: 151.77  E-value: 3.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  15 LGPLKDLFEDPAVTEVMVN-PGGIVYAE-RAGEM----IYIEDaglaEVHITSAIRALA----KSVDES---VEANTPkt 81
Cdd:COG0630  161 YGKLDPLMRDPNIEDISCNgVGIPVYVYhRDYERiptnIVFES----EEELDNFVVKLAqrsgKHISVArpiVDATLP-- 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  82 fisasvENLRIAGALSPA-SHGGPSLCIRKHQEEgarP-NLGELVEKGMLTNAQAELLeQLFVHEKKNVMVGGPTGSGKT 159
Cdd:COG0630  235 ------DGSRIALTLGPEvSRRGSSFTIRKFREV---PlTPIDLIEWGTLSPELAAYL-WLLLENGKSVLVAGGTASGKT 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 160 TLANALCMRIPPYERVISVEDSIELhpNLKHH--VRYLTNATKGVTAQLV-----VQHTLRARPDRLIVGETRGAETFDL 232
Cdd:COG0630  305 TLLNALLSFIPPDAKIVTIEDTREL--NLPHEnwISLVTRESFGGEEGDVtmfdlLKAALRQRPDYIVVGEVRGEEAYTL 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 233 IRAFNSGHdGSLSTVHASSATDMLYAIEMLyQMSLPpdaslspeavRGYIaRAVHVCVHVTRsVKQGEDGkyyyVRRVNE 312
Cdd:COG0630  383 FQAMATGH-GVLSTFHADSVESAINRLTSP-PINVP----------RTLL-QALDLVVFQKR-VRVGGKR----VRRVTS 444


                 ....*....
gi 817233824 313 IVRVNGVEN 321
Cdd:COG0630  445 IVEIVGYDP 453
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
 14-271 5.49e-39

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: 138.96  E-value: 5.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   14 NLGPLKDLfeDPAVTEVMVNPGG--IVYAERAG----EMIYIEDAGLAEVhiTSAIRALAK-SVDES---VEANTPKTFI 83
Cdd:pfam00437   1 NLIPLEAL--DEGASDIHVEPPEriVWIRFRVDgvlrEIPFPDADALARL--ISRIKVMARlDISERrppQDGRLPLRIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   84 SASVEnLRIAgalSPASHGGPSLCIRKHQEEGARPNLGELVEKGMLTNAQAELLEQLfvheKKNVMVGGPTGSGKTTLAN 163
Cdd:pfam00437  77 GKGVR-VRVS---TLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDEALLEFLRQP----RGNILVTGPTGSGKTTTLY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  164 ALCMRIPPY-ERVISVEDSIELHPNLKHHVRylTNATKGVTAQLVVQHTLRARPDRLIVGETRGAETFDL-IRAFNSGHD 241
Cdd:pfam00437 149 AALGELNTRdENIVTVEDPVEIQLEGINQVQ--LNARAGVTFADLLRAILRQDPDRIMVGEIRDLETAEIaLQAANTGHL 226

                         250       260       270
                  ....*....|....*....|....*....|
gi 817233824  242 GsLSTVHASSATDmlyAIEMLYQMSLPPDA 271
Cdd:pfam00437 227 V-LSTLHTNSAAG---ALTRLQDMGVPPFE 252
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
 23-329 6.46e-39

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 139.93  E-value: 6.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  23 EDPAVTEVMVNPGGIVYAER-------AGEMiyieDAGLAEVHITSAIRALaksvdeSVEANTPKTFISAS--VENLRIA 93
Cdd:PRK13833  27 DDATVVEIMLNPDGKLFIERlghgvapAGEM----SAAAAEVVIGSVAHAL------QSEADDERPIISGElpIGGHRFE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  94 GALSPAShGGPSLCIRKHQEEgaRPNLGELVEKGMLTNAQAELLEQLFVhEKKNVMVGGPTGSGKTTLANALCMRI---P 170
Cdd:PRK13833  97 GLLPPVV-SGPAFTIRRRASR--LIPLDDYVTSKIMTEAQASVIRSAID-SRLNIVISGGTGSGKTTLANAVIAEIvasA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 171 PYERVISVEDSIELHPNLKHHVRYLTNATkgVTAQLVVQHTLRARPDRLIVGETRGAETFDLIRAFNSGHDGSLSTVHAS 250
Cdd:PRK13833 173 PEDRLVILEDTAEIQCAAENAVALHTSDT--VDMARLLKSTMRLRPDRIIVGEVRDGAALTLLKAWNTGHPGGVTTIHSN 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 817233824 251 SATDMLYAIEMLyqmslppDASLSPEAVRGYIARAVHVCVHVTRSVKQgedgkyyyvRRVNEIVRVNGVENGKYLLESL 329
Cdd:PRK13833 251 TAMSALRRLEQL-------TAEASQQPMQEVIGEAVDLIVSIERTGKG---------RRVREVIHVEGFANGRYQTEHY 313
PRK13851 PRK13851
type IV secretion system protein VirB11; Provisional
 142-290 1.47e-23

type IV secretion system protein VirB11; Provisional


Pssm-ID: 172375  Cd Length: 344  Bit Score: 99.20  E-value: 1.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 142 VHEKKNVMVGGPTGSGKTTLANALCMRIPPYERVISVEDSIEL---HPNlkhHVRYLTN----ATKGVTAQLVVQHTLRA 214
Cdd:PRK13851 159 VVGRLTMLLCGPTGSGKTTMSKTLISAIPPQERLITIEDTLELvipHEN---HVRLLYSkngaGLGAVTAEHLLQASLRM 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817233824 215 RPDRLIVGETRGAETFDLIRAFNSGHDGSLSTVHASSATDMLYAIEMLYQMSlPPDASLSPEAVRGYIARAVHVCV 290
Cdd:PRK13851 236 RPDRILLGEMRDDAAWAYLSEVVSGHPGSISTIHGANPVQGFKKLFSLVKSS-AQGASLEDRTLIDMLATAIDVIV 310
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
 146-252 3.36e-21

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: 88.60  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 146 KNVMVGGPTGSGKTTLANALCMRIPPYERVISVEDSIELhpNLKHHVRYLTNATKG-VTAQLVVQHTLRARPDRLIVGET 224
Cdd:cd19477   11 KNVIVCGGTGSGKTTYIKSILEFIPKEERIISIEDTEEI--VFKHHKNYTQLFFGGnITSADCLKSCLRQRPDRIILGEL 88

                         90       100
                 ....*....|....*....|....*...
gi 817233824 225 RGAETFDLIRAFNSGHDGSLSTVHASSA 252
Cdd:cd19477   89 RSSEAYDFYNVLCSGHKGTLTTLHAGSS 116
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
89-252 1.92e-15

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 74.79  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  89 NLRiagaLS--PASHGGPSLCIR-KHQEEGARPNLgelvekgmLTNAQAELLEQLFVHEKKNVMVGGPTGSGKTTLANAL 165
Cdd:NF041000  81 SLR----LStvGDFLGRESLVIRlLYQLEQIKPQL--------FFPEQFQLLKQLLQRRSGLILFSGPTGSGKTTTMYSL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 166 CMRIPPYERVISVEDSIElhpnlKHHVRYL---TNATKGVTAQLVVQHTLRARPDRLIVGETRGAETFDL-IRAFNSGHD 241
Cdd:NF041000 149 ARKLALNKQVITIEDPVE-----IKEPNFLqlqVNEKAGMTYDTLLKAALRHRPDILIIGEIRDAETAKAaIRAALTGHL 223

                        170
                 ....*....|.
gi 817233824 242 gSLSTVHASSA 252
Cdd:NF041000 224 -VLSTVHAKSA 233
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
 148-270 3.31e-15

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: 72.13  E-value: 3.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 148 VMVGGPTGSGK-TTLANALCMRIPPYERVISVEDSIEL-HPNLKHhvrYLTNATKGVTAQLVVQHTLRARPDRLIVGETR 225
Cdd:cd01129   14 ILVTGPTGSGKtTTLYAMLRELNGPERNIITIEDPVEYqIPGINQ---SQVNEKIGLTFADALRAILRQDPDIIMVGEIR 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 817233824 226 GAETFDL-IRAFNSGHDgSLSTVHASSAtdmLYAIEMLYQMSLPPD 270
Cdd:cd01129   91 DAETAEIaIRAALTGHL-VLSTLHTNDA---LGAITRLLDMGIEPF 132
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
 134-251 1.28e-12

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: 65.09  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 134 AELLEQLFVHEKKnVMVGGPTGSGKTTLANAL---CM-RIPPYERVISVEDSIEL---HPNLKHHV-------RYLTNAT 199
Cdd:cd19516    1 PDLVEALFPREGL-VYVAGATGSGKSTLLAAIyryILeNDPPDRKIITYEDPIEFvydGIKSKHSIivqsqipRHFKSFA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 817233824 200 KGvtaqlvVQHTLRARPDRLIVGETRGAETFD-LIRAFNSGHDgSLSTVHASS 251
Cdd:cd19516   80 KA------VREALRRKPSLIGVGELRDQETISaAVEASLTGHP-VYSTVHTKS 125
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
 148-252 2.32e-11

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: 62.55  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 148 VMVGGPTGSGK-TTLA---NALCMRIPpyERVISVEDSIE-LHPNLKHHVRYLTNATKGVTAQLVVQHTLRARPDRLIVG 222
Cdd:cd01131   24 VLVTGPTGSGKsTTLAamiDYINETRS--KHIITIEDPIEfVHKHKKSLINQREVGRDTESFAAALRAALREDPDVILVG 101

                         90       100       110
                 ....*....|....*....|....*....|.
gi 817233824 223 ETRGAETFDL-IRAFNSGHDgSLSTVHASSA 252
Cdd:cd01131  102 EMRDLETIELaLTAAETGHL-VFSTLHTNSA 131
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
 148-256 1.01e-10

Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];


Pssm-ID: 442056  Cd Length: 342  Bit Score: 62.03  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 148 VMVGGPTGSGK-TTLA---NALCMRIPpyERVISVEDSIE-LHPNLK---------HHVRYLTNATKGVtaqlvvqhtLR 213
Cdd:COG2805  128 VLVTGPTGSGKsTTLAamiDYINETRA--KHIITIEDPIEfVHKHKKslinqrevgRDTPSFANALRAA---------LR 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 817233824 214 ARPDRLIVGETRGAETFDL-IRAFNSGHdgsL--STVHASSATDML 256
Cdd:COG2805  197 EDPDVILVGEMRDLETIEAaLTAAETGH---LvfATLHTNSAAQTI 239
PRK10436 PRK10436
hypothetical protein; Provisional
 148-268 2.02e-10

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 61.48  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 148 VMVGGPTGSGKT-TLANALCMRIPPYERVISVEDSIELhPnLKHHVRYLTNATKGVTAQLVVQHTLRARPDRLIVGETRG 226
Cdd:PRK10436 221 ILVTGPTGSGKTvTLYSALQTLNTAQINICSVEDPVEI-P-LAGINQTQIHPKAGLTFQRVLRALLRQDPDVIMVGEIRD 298

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 817233824 227 AETFDL-IRAFNSGHDgSLSTVHASSATDMLYaieMLYQMSLP 268
Cdd:PRK10436 299 GETAEIaIKAAQTGHL-VLSTLHTNSTSETLV---RLQQMGIA 337
pilT_fam TIGR01420
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ...
 135-252 6.03e-10

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: 59.64  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  135 ELLEQLFVHEKKNVMVGGPTGSGKTTLANALCMRIPPY--ERVISVEDSIE-LHPNLKH--HVRYLTNATKGVTAQLvvQ 209
Cdd:TIGR01420 112 PVLRELAERPRGLILVTGPTGSGKSTTLASMIDYINKNkaYHIITIEDPIEyVHTNKRSliNQREVGEDTLSFANAL--R 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 817233824  210 HTLRARPDRLIVGETRGAETFDL-IRAFNSGHDgSLSTVHASSA 252
Cdd:TIGR01420 190 AALREDPDVILIGEMRDLETVELaLTAAETGHL-VFGTLHTNSA 232
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
 98-283 9.11e-10

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: 59.44  E-value: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  98 PASHGgPSLCIRKHQEEGARPNLGELvekGMlTNAQAELLEQLFvhEKKN--VMVGGPTGSGK-TTLANALCMRIPPYER 174
Cdd:COG2804  271 PTVYG-EKVVLRILDKSAALLDLEQL---GF-SPDQLERLRRLI--RRPHgiILVTGPTGSGKtTTLYAALNELNTPERN 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 175 VISVEDSIElhpnlkHHVRYLT----NATKGVTAQLVVQHTLRARPDRLIVGETRGAETFDL-IRAFNSGHdGSLSTVHA 249
Cdd:COG2804  344 IITVEDPVE------YQLPGINqvqvNPKIGLTFASALRSILRQDPDVIMVGEIRDLETAEIaVQAALTGH-LVLSTLHT 416

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 817233824 250 SSATDmlyAIEMLYQMSLPPD--ASlspeAVRGYIA 283
Cdd:COG2804  417 NDAPS---AITRLLDMGVEPFllAS----SLLGVLA 445
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 145-215 5.19e-05

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: 42.75  E-value: 5.19e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817233824   145 KKNVMVGGPTGSGKTTLANALCMRIPPYER---VISVEDSIELHPNLKHHVRYLTNATKGVTAQLVVQHTLRAR 215
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGgviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR 75
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 129-162 1.87e-04

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 41.48  E-value: 1.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 817233824 129 LTNAQAELLEQLFvHEKKNVMVGGPTGSGKTTLA 162
Cdd:cd17921    2 LNPIQREALRALY-LSGDSVLVSAPTSSGKTLIA 34
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 152-195 7.42e-04

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 39.55  E-value: 7.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 817233824  152 GPTGSGKTTLANALCMRIPPYERVISVEDSIELHPNLKH---HVRYL 195
Cdd:pfam00005  18 GPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkEIGYV 64
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 148-215 7.66e-04

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 39.22  E-value: 7.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817233824  148 VMVGGPTGSGKTTLANALCMRiPPYERvISVEDSIE-LHPNLKHHVRYLTNATKGVTAQL--VVQHTLRAR 215
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEE-LGAVR-LSSDDERKrLFGEGRPSISYYTDATDRTYERLheLARIALRAG 70
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 140-195 1.16e-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: 38.77  E-value: 1.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 817233824 140 LFVHEKKNVMVGGPTGSGKTTLANALCMRIPPYERVISVED---SIELHPNLKHHVRYL 195
Cdd:cd00267   20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiAKLPLEELRRRIGYV 78
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
152-178 1.18e-03

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 39.28  E-value: 1.18e-03
                         10        20
                 ....*....|....*....|....*..
gi 817233824 152 GPTGSGKTTLANALCMRIPPYERVISV 178
Cdd:COG0194    9 GPSGAGKTTLVKALLERDPDLRFSVSA 35
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
134-168 1.22e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 1.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817233824 134 AELLEQLFVHEKKNVMVGGPTGSGKTTLANALCMR 168
Cdd:COG1484   88 LELATLDFIERGENLILLGPPGTGKTHLAIALGHE 122
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 142-180 1.23e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 39.37  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 817233824 142 VHEKKNVMVGGPTGSGKTTLANALCMRIPPYERVISVED 180
Cdd:cd03225   24 IKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG 62
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 137-184 1.40e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 38.70  E-value: 1.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 817233824 137 LEQLFVHEKKNVMVGGPTGSGKTTLANALCMRIPPY---ERVISVEDSIEL 184
Cdd:cd18032   12 LEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLEAnrkKRILFLAHREEL 62
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 128-168 1.42e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 817233824 128 MLTNAQ-AELLEQLFVHEKKNVMVGGPTGSGKTTLANALCMR 168
Cdd:NF038214  72 GLDKAQiRELATLDFIERAENVLLLGPPGTGKTHLAIALGYA 113
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 148-180 3.21e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 38.28  E-value: 3.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 817233824 148 VMVGGPTGSGKTTLANALCMRIPPYE-RVISVED 180
Cdd:COG0572   10 IGIAGPSGSGKTTFARRLAEQLGADKvVVISLDD 43
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 148-236 3.23e-03

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.


Pssm-ID: 428926  Cd Length: 192  Bit Score: 38.11  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824  148 VMVGGPTGSGKTTLANALCMRIPPYERVISV-EDSI-ELHPNLKHHVR-------YLTNATKGVTAQLVVQHTLRARPDR 218
Cdd:pfam06414  14 ILLGGQPGAGKTELARALLDELGRQGNVVRIdPDDFrELHPHYRELQAadpktasEYTQPDASRWVEKLLQHAIENGYNI 93

                          90
                  ....*....|....*....
gi 817233824  219 LIVGETRGAETFD-LIRAF 236
Cdd:pfam06414  94 ILEGTLRSPDVAKkIARAL 112
ResIII pfam04851
Type III restriction enzyme, res subunit;
126-184 3.34e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817233824  126 KGMLTNAQAELLE---QLFVHEKKNVMVGGPTGSGKTTLANALC---MRIPPYERVISVEDSIEL 184
Cdd:pfam04851   1 KLELRPYQIEAIEnllESIKNGQKRGLIVMATGSGKTLTAAKLIarlFKKGPIKKVLFLVPRKDL 65
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 139-171 4.36e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 37.37  E-value: 4.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 817233824  139 QLFVHEKKNVMVGGPTGSGKTTLANALCMRIPP 171
Cdd:pfam12775  25 DLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDK 57
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 148-213 5.49e-03

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including 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: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 37.63  E-value: 5.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824 148 VMVGGPTGSGKTTLANALCMRIPPYERV--ISVEDSIELHPNLKHHVRYL--TNATKGVTAQLVVQHTLR 213
Cdd:cd03233   36 VLVLGRPGSGCSTLLKALANRTEGNVSVegDIHYNGIPYKEFAEKYPGEIiyVSEEDVHFPTLTVRETLD 105
DEXDc smart00487
DEAD-like helicases superfamily;
129-225 6.91e-03

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 37.09  E-value: 6.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817233824   129 LTNAQAELLEQLfVHEKKNVMVGGPTGSGKTT-LANALCMRI--PPYERVISVEDSIELHPNLKHHVRYLTNATKGVTAQ 205
Cdd:smart00487   9 LRPYQKEAIEAL-LSGLRDVILAAPTGSGKTLaALLPALEALkrGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVG 87

                           90       100
                   ....*....|....*....|
gi 817233824   206 LVVQHTLRARPDRLIVGETR 225
Cdd:smart00487  88 LYGGDSKREQLRKLESGKTD 107
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 131-178 7.42e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 36.36  E-value: 7.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 817233824 131 NAQAELLEQLFVHEKKNVMVGGPTGSGKTTLANALCMRIPPYE-RVISV 178
Cdd:cd00009    5 EAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGaPFLYL 53
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 148-180 8.33e-03

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 36.92  E-value: 8.33e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 817233824 148 VMVGGPTGSGKTTLANALcMRIPPYERVISVED 180
Cdd:cd02024    2 VGISGVTNSGKTTLAKLL-QRILPNCCVIHQDD 33
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 147-166 8.64e-03

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 37.14  E-value: 8.64e-03
                         10        20
                 ....*....|....*....|
gi 817233824 147 NVMVGGPTGSGKTTLANALC 166
Cdd:cd01850    6 NIMVVGESGLGKSTFINTLF 25
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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