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Conserved domains on  [gi|517056578|ref|WP_018245396|]
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P-type DNA transfer ATPase VirB11 [Rhizobium leguminosarum]

Protein Classification

P-type DNA transfer ATPase VirB11( domain architecture ID 10021505)

P-type DNA transfer ATPase VirB11 is a major virulence determinant for subversion of human endothelial cell (HEC) function

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
 20-327 2.09e-165

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: 463.36  E-value: 2.09e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   20 FLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIPPATT 99
Cdd:TIGR02788   1 FLDDEDVTEICINRPGEVWVEGPGGWQRFDVPDLTFSHLMRLARAIASFSKQSISEENPILSATLPGGERVQIVIPPACE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  100 KGTVSITIRKPSSVSLSLNDLDQGGLFAEVAREDADVSAIDRRLLDLHRTGSYQAFLREAVYARKNIIISGATGSGKTTL 179
Cdd:TIGR02788  81 NDTVSITIRKPSLVDFSLDDYEEKGFFDTVRAQSGTLSDNDEQLLELLDAGDIKEFLRLAIASRKNIIISGGTGSGKTTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  180 SKALIRHIPSSERIISIEDTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFYYIRNVN 259
Cdd:TIGR02788 161 LKSLVDEIPKDERIITIEDTREIFLPHPNYVHLFYSKGGQGLAKVTPKDLLQSCLRMRPDRIILGELRGDEAFDFIRAVN 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517056578  260 SGHPGSITTVHADSARLAFEQLTLLVKESEGGRDLERDDIREMLKIAIDVIVQCKRIDGRFRVTEIYY 327
Cdd:TIGR02788 241 TGHPGSITTLHAGSPEEAFEQLALMVKSSQAGLGLDFAYIVKLVREVIDIVVQINRRGGGRKITEVYF 308
 
Name Accession Description Interval E-value
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
 20-327 2.09e-165

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: 463.36  E-value: 2.09e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   20 FLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIPPATT 99
Cdd:TIGR02788   1 FLDDEDVTEICINRPGEVWVEGPGGWQRFDVPDLTFSHLMRLARAIASFSKQSISEENPILSATLPGGERVQIVIPPACE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  100 KGTVSITIRKPSSVSLSLNDLDQGGLFAEVAREDADVSAIDRRLLDLHRTGSYQAFLREAVYARKNIIISGATGSGKTTL 179
Cdd:TIGR02788  81 NDTVSITIRKPSLVDFSLDDYEEKGFFDTVRAQSGTLSDNDEQLLELLDAGDIKEFLRLAIASRKNIIISGGTGSGKTTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  180 SKALIRHIPSSERIISIEDTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFYYIRNVN 259
Cdd:TIGR02788 161 LKSLVDEIPKDERIITIEDTREIFLPHPNYVHLFYSKGGQGLAKVTPKDLLQSCLRMRPDRIILGELRGDEAFDFIRAVN 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517056578  260 SGHPGSITTVHADSARLAFEQLTLLVKESEGGRDLERDDIREMLKIAIDVIVQCKRIDGRFRVTEIYY 327
Cdd:TIGR02788 241 TGHPGSITTLHAGSPEEAFEQLALMVKSSQAGLGLDFAYIVKLVREVIDIVVQINRRGGGRKITEVYF 308
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
 14-327 2.09e-97

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 291.66  E-value: 2.09e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  14 LVPLSPFLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIV 93
Cdd:PRK13900  12 LEPLKNIFAEDGVNEISINKPGEVWVEKKGDIRCEQIPELDLSHLKALGRLVAQATEQKISEEKPLLSATLPNGYRIQIV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  94 IPPATTKGTVSITIRKPSSVSLSLNDLDQGGLFAEVAREDaDVSAIDRRLLDLHRTGSYQAFLREAVYARKNIIISGATG 173
Cdd:PRK13900  92 FPPACEIGQIVYSIRKPSGMQLTLDDYEKMGAFDETATES-LVDEDDVILNELLAEKKIKEFLEHAVISKKNIIISGGTS 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 174 SGKTTLSKALIRHIPSSERIISIEDTPELVIP-QPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAF 252
Cdd:PRK13900 171 TGKTTFTNAALREIPAIERLITVEDAREIVLSnHPNRVHLLASKGGQGRAKVTTQDLIEACLRLRPDRIIVGELRGAEAF 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517056578 253 YYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKESEGGrdLERDDIREMLKIAIDVIVQCKRIDGRFR-VTEIYY 327
Cdd:PRK13900 251 SFLRAINTGHPGSISTLHADSPAMAIEQLKLMVMQAGLG--MPPDQIKKYILNVVDIVVQLKRGSGGKRyVSEIYF 324
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 16-325 2.05e-83

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: 257.79  E-value: 2.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  16 PLSPFLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIP 95
Cdd:COG4962   58 PLEPLLDDPDVTDIMVNGPDEVFVERGGRLERTDVRFDSEEELRRLIERIAARVGRRLDESSPIVDARLPDGSRVNAVIP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  96 PATTKGTvSITIRKPSSVSLSLNDLDQGGLFAEVAREdadvsaidrrlldlhrtgsyqaFLREAVYARKNIIISGATGSG 175
Cdd:COG4962  138 PVARDGP-SLSIRKFRKRPLTLEDLVALGSLTPEMAE----------------------FLRAAVRARLNILVSGGTGSG 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 176 KTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLF-YSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFYY 254
Cdd:COG4962  195 KTTLLNALSGFIPPDERIVTIEDAAELQLQHPHVVRLEtRPPNVEGAGEVTLRDLVRNALRMRPDRIIVGEVRGAEALDM 274

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056578 255 IRNVNSGHPGSITTVHADSARLAFEQLTLLVkeSEGGRDLERDDIREMLKIAIDVIVQCKRI-DGRFRVTEI 325
Cdd:COG4962  275 LQAMNTGHDGSMSTLHANSARDALARLETLA--LMAGENLPREAVRRQIASAIDLVVHLERLrDGRRRVTEI 344
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 154-327 6.07e-81

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: 243.99  E-value: 6.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 154 AFLREAVYARKNIIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESC 233
Cdd:cd01130    3 AFLRLAVRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGGGEKGEVTMADLLKAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 234 LRMRPDRILLQELRDGTAFYYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKesEGGRDLERDDIREMLKIAIDVIVQC 313
Cdd:cd01130   83 LRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVL--EAGVNLDEEALRRLIASAIDVIVHV 160

                        170
                 ....*....|....*
gi 517056578 314 KRI-DGRFRVTEIYY 327
Cdd:cd01130  161 KRLgDGVRRVTEIYE 175
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
 14-307 8.78e-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: 162.07  E-value: 8.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   14 LVPLSPFLGDKSlyEIIINWP-TQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLP-----GD 87
Cdd:pfam00437   2 LIPLEALDEGAS--DIHVEPPeRIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPlriggKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   88 ERIQIVIPPATTKGTVSITIRKPSSVSLSLNDLDQGGLFAEvaredadvsaidrrlldlhrtgSYQAFLReavYARKNII 167
Cdd:pfam00437  80 VRVRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDE----------------------ALLEFLR---QPRGNIL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  168 ISGATGSGKTTLSKALIRHIP-SSERIISIEDTPELVIPQPNHVRLfYSKGGqglakVGAKDLLESCLRMRPDRILLQEL 246
Cdd:pfam00437 135 VTGPTGSGKTTTLYAALGELNtRDENIVTVEDPVEIQLEGINQVQL-NARAG-----VTFADLLRAILRQDPDRIMVGEI 208

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056578  247 RDG-TAFYYIRNVNSGHPGsITTVHADSARLAFEQLTLLVkeseggrdLERDDIREMLKIAI 307
Cdd:pfam00437 209 RDLeTAEIALQAANTGHLV-LSTLHTNSAAGALTRLQDMG--------VPPFELASSLLLVI 261
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
166-275 7.38e-12

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 64.78  E-value: 7.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIP-----QPNHVrlfyskggqglAKVGAKDLLESCLRMRPDR 240
Cdd:NF041000 131 ILFSGPTGSGKTTTMYSLARKLALNKQVITIEDPVEIKEPnflqlQVNEK-----------AGMTYDTLLKAALRHRPDI 199

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517056578 241 ILLQELRDG-TAFYYIRNVNSGHPgSITTVHADSAR 275
Cdd:NF041000 200 LIIGEIRDAeTAKAAIRAALTGHL-VLSTVHAKSAA 234
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 163-246 3.80e-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: 43.13  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   163 RKNIIISGATGSGKTTLSKALIRHI-PSSERIISIE-DTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDR 240
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81


                   ....*.
gi 517056578   241 ILLQEL 246
Cdd:smart00382  82 LILDEI 87
 
Name Accession Description Interval E-value
VirB11 TIGR02788
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ...
 20-327 2.09e-165

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: 463.36  E-value: 2.09e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   20 FLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIPPATT 99
Cdd:TIGR02788   1 FLDDEDVTEICINRPGEVWVEGPGGWQRFDVPDLTFSHLMRLARAIASFSKQSISEENPILSATLPGGERVQIVIPPACE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  100 KGTVSITIRKPSSVSLSLNDLDQGGLFAEVAREDADVSAIDRRLLDLHRTGSYQAFLREAVYARKNIIISGATGSGKTTL 179
Cdd:TIGR02788  81 NDTVSITIRKPSLVDFSLDDYEEKGFFDTVRAQSGTLSDNDEQLLELLDAGDIKEFLRLAIASRKNIIISGGTGSGKTTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  180 SKALIRHIPSSERIISIEDTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFYYIRNVN 259
Cdd:TIGR02788 161 LKSLVDEIPKDERIITIEDTREIFLPHPNYVHLFYSKGGQGLAKVTPKDLLQSCLRMRPDRIILGELRGDEAFDFIRAVN 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517056578  260 SGHPGSITTVHADSARLAFEQLTLLVKESEGGRDLERDDIREMLKIAIDVIVQCKRIDGRFRVTEIYY 327
Cdd:TIGR02788 241 TGHPGSITTLHAGSPEEAFEQLALMVKSSQAGLGLDFAYIVKLVREVIDIVVQINRRGGGRKITEVYF 308
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
 14-327 2.09e-97

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 291.66  E-value: 2.09e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  14 LVPLSPFLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIV 93
Cdd:PRK13900  12 LEPLKNIFAEDGVNEISINKPGEVWVEKKGDIRCEQIPELDLSHLKALGRLVAQATEQKISEEKPLLSATLPNGYRIQIV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  94 IPPATTKGTVSITIRKPSSVSLSLNDLDQGGLFAEVAREDaDVSAIDRRLLDLHRTGSYQAFLREAVYARKNIIISGATG 173
Cdd:PRK13900  92 FPPACEIGQIVYSIRKPSGMQLTLDDYEKMGAFDETATES-LVDEDDVILNELLAEKKIKEFLEHAVISKKNIIISGGTS 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 174 SGKTTLSKALIRHIPSSERIISIEDTPELVIP-QPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAF 252
Cdd:PRK13900 171 TGKTTFTNAALREIPAIERLITVEDAREIVLSnHPNRVHLLASKGGQGRAKVTTQDLIEACLRLRPDRIIVGELRGAEAF 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517056578 253 YYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKESEGGrdLERDDIREMLKIAIDVIVQCKRIDGRFR-VTEIYY 327
Cdd:PRK13900 251 SFLRAINTGHPGSISTLHADSPAMAIEQLKLMVMQAGLG--MPPDQIKKYILNVVDIVVQLKRGSGGKRyVSEIYF 324
PRK13851 PRK13851
type IV secretion system protein VirB11; Provisional
 10-331 8.44e-87

type IV secretion system protein VirB11; Provisional


Pssm-ID: 172375  Cd Length: 344  Bit Score: 265.22  E-value: 8.44e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  10 VRELLVPLSPFLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPeLSFDKLMRLARAVASFSNQAIDETRPILSATLPGDER 89
Cdd:PRK13851   7 LRFLLKPVLEWLDDPRTEEVAINRPGEAFVRQAGVFTKFPLP-LSYDDLEDIAILAGALRKQDVGPRNPLCATELPGGER 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  90 IQIVIPPATTKGTVSITIRKPSSVSLSLNDLD---QGGLFAEVAREDADVSAIDRRLLDLHRTGSYQAFLREAVYARKNI 166
Cdd:PRK13851  86 LQICLPPTVPSGTVSLTIRRPSSRVSELKEVSsryDASRWNQWQERRKRRDQLDEAILRHYDNGDLEAFLHACVVGRLTM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 167 IISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDRILLQEL 246
Cdd:PRK13851 166 LLCGPTGSGKTTMSKTLISAIPPQERLITIEDTLELVIPHENHVRLLYSKNGAGLGAVTAEHLLQASLRMRPDRILLGEM 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 247 RDGTAFYYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKESEGGRDLERDDIREMLKIAIDVIVQCKRIDGRFRVTEIY 326
Cdd:PRK13851 246 RDDAAWAYLSEVVSGHPGSISTIHGANPVQGFKKLFSLVKSSAQGASLEDRTLIDMLATAIDVIVPFRAYGDVYEVGEIW 325


                 ....*
gi 517056578 327 YRAAA 331
Cdd:PRK13851 326 LAADA 330
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 16-325 2.05e-83

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: 257.79  E-value: 2.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  16 PLSPFLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIP 95
Cdd:COG4962   58 PLEPLLDDPDVTDIMVNGPDEVFVERGGRLERTDVRFDSEEELRRLIERIAARVGRRLDESSPIVDARLPDGSRVNAVIP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  96 PATTKGTvSITIRKPSSVSLSLNDLDQGGLFAEVAREdadvsaidrrlldlhrtgsyqaFLREAVYARKNIIISGATGSG 175
Cdd:COG4962  138 PVARDGP-SLSIRKFRKRPLTLEDLVALGSLTPEMAE----------------------FLRAAVRARLNILVSGGTGSG 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 176 KTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLF-YSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFYY 254
Cdd:COG4962  195 KTTLLNALSGFIPPDERIVTIEDAAELQLQHPHVVRLEtRPPNVEGAGEVTLRDLVRNALRMRPDRIIVGEVRGAEALDM 274

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056578 255 IRNVNSGHPGSITTVHADSARLAFEQLTLLVkeSEGGRDLERDDIREMLKIAIDVIVQCKRI-DGRFRVTEI 325
Cdd:COG4962  275 LQAMNTGHDGSMSTLHANSARDALARLETLA--LMAGENLPREAVRRQIASAIDLVVHLERLrDGRRRVTEI 344
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 154-327 6.07e-81

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: 243.99  E-value: 6.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 154 AFLREAVYARKNIIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESC 233
Cdd:cd01130    3 AFLRLAVRARKNILISGGTGSGKTTLLNALLSFIPPDERIVTIEDTRELQLPHPNVVHLLTRPGGGEKGEVTMADLLKAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 234 LRMRPDRILLQELRDGTAFYYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKesEGGRDLERDDIREMLKIAIDVIVQC 313
Cdd:cd01130   83 LRMRPDRIIVGEVRGGEAYDMLQAMNTGHPGSITTIHANSAEDAIDRLATLVL--EAGVNLDEEALRRLIASAIDVIVHV 160

                        170
                 ....*....|....*
gi 517056578 314 KRI-DGRFRVTEIYY 327
Cdd:cd01130  161 KRLgDGVRRVTEIYE 175
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
 14-307 8.78e-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: 162.07  E-value: 8.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   14 LVPLSPFLGDKSlyEIIINWP-TQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLP-----GD 87
Cdd:pfam00437   2 LIPLEALDEGAS--DIHVEPPeRIVWIRFRVDGVLREIPFPDADALARLISRIKVMARLDISERRPPQDGRLPlriggKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   88 ERIQIVIPPATTKGTVSITIRKPSSVSLSLNDLDQGGLFAEvaredadvsaidrrlldlhrtgSYQAFLReavYARKNII 167
Cdd:pfam00437  80 VRVRVSTLPTAGGEKLVIRLLDPSNVALSLDELGMTGAQDE----------------------ALLEFLR---QPRGNIL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  168 ISGATGSGKTTLSKALIRHIP-SSERIISIEDTPELVIPQPNHVRLfYSKGGqglakVGAKDLLESCLRMRPDRILLQEL 246
Cdd:pfam00437 135 VTGPTGSGKTTTLYAALGELNtRDENIVTVEDPVEIQLEGINQVQL-NARAG-----VTFADLLRAILRQDPDRIMVGEI 208

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517056578  247 RDG-TAFYYIRNVNSGHPGsITTVHADSARLAFEQLTLLVkeseggrdLERDDIREMLKIAI 307
Cdd:pfam00437 209 RDLeTAEIALQAANTGHLV-LSTLHTNSAAGALTRLQDMG--------VPPFELASSLLLVI 261
TrbB_P TIGR02782
P-type conjugative transfer ATPase TrbB; The TrbB protein is found in the trb locus of ...
 20-325 3.11e-46

P-type conjugative transfer ATPase TrbB; The TrbB protein is found in the trb locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for plasmid conjugative transfer. TrbB is a homolog of the vir system VirB11 ATPase, and the Flp pilus sytem ATPase TadA. [Cellular processes, Conjugation]


Pssm-ID: 274297  Cd Length: 299  Bit Score: 159.14  E-value: 3.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   20 FLGDKSLYEIIINWPTQVVTEGTAGWQShDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGD-ERIQIVIPPAT 98
Cdd:TIGR02782  13 ALDDPGVVEIMLNPDGRLWVERLGSGMS-PLGEMSPADAQRIIGLVADYLGTEVDRDKPIVEGELPLDgSRFEGLIPPVV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   99 TKgtVSITIRKPSSVSLSLNDLDQGGLFAEVAREdadvsaidrrlldlhrtgsyqaFLREAVYARKNIIISGATGSGKTT 178
Cdd:TIGR02782  92 AA--PSFAIRKKAVAVFTLDDYVEAGIMTAAQRD----------------------VLREAVLARKNILVVGGTGSGKTT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  179 LSKALIRHIPSS---ERIISIEDTPELVIPQPNHVRLFYSKGGQGLAkvgakDLLESCLRMRPDRILLQELRDGTAFYYI 255
Cdd:TIGR02782 148 LANALLAEIAKNdptDRVVIIEDTRELQCAAPNVVQLRTSDDAISMT-----RLLKATLRLRPDRIIVGEVRGGEALDLL 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  256 RNVNSGHPGSITTVHADSARLAFEQLTLLVKEseggrdLERDDIREMLKIAIDVIVQCKRIDGRFRVTEI 325
Cdd:TIGR02782 223 KAWNTGHPGGIATIHANNAKAALDRLEQLIQE------VSVTPMQTLIAEAVDLVIFIARTPAGRRVQEI 286
heli_sec_ATPase TIGR03819
helicase/secretion neighborhood ATPase; Members of this protein family comprise a distinct ...
 16-325 7.17e-43

helicase/secretion neighborhood ATPase; Members of this protein family comprise a distinct clade of putative ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer. The association of most members with a nearby gene for a DEAH-box helicase suggests a role in conjugal transfer.


Pssm-ID: 200328  Cd Length: 340  Bit Score: 151.33  E-value: 7.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   16 PLSPFLGDKSLYEIIINWPTQVVTEGTAGWQSHDLPELSFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIP 95
Cdd:TIGR03819  54 PLEPLLADPGVTDVLVNGPDEVWVDRGRGLERTDVRFPDEAAVRRLAQRLAAAAGRRLDDAQPWVDARLPDGTRLHAVLP 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   96 PATTKGTVsITIRKPSSVSLSLNDLDQGGLFAEVARedadvsaidrrlldlhrtgsyqAFLREAVYARKNIIISGATGSG 175
Cdd:TIGR03819 134 PVATDGTC-LSLRVPRRRTFTLDELVAAGTIPPGVA----------------------RLLRALVAARLAFLVSGGTGSG 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  176 KTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLfYSKGG--QGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFY 253
Cdd:TIGR03819 191 KTTLLSALLALVPPDERIVLVEDAAELRPDHPHVVRL-EARPAnvEGAGAVTLTDLVRQALRMRPDRIVVGEVRGAEVVD 269

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517056578  254 YIRNVNSGHPGSITTVHADS-----ARLafEQLTLLvkeseGGrdLERDDIREMLKIAIDVIVQCKR-IDGRFRVTEI 325
Cdd:TIGR03819 270 LLAALNTGHDGGAGTLHANSpadvpARL--EALGAL-----AG--LDRAALHSQLAAALDVVLHVRRtPRGRRRVAEI 338
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
 54-326 2.24e-41

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: 150.23  E-value: 2.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  54 SFDKLMRLARAVASFSNQAIDETRPILSATLPGDERIQIVIPPATTKGTVSITIRKPSSVSLSLNDLDQGGLF-AEVAre 132
Cdd:COG0630  203 SEEELDNFVVKLAQRSGKHISVARPIVDATLPDGSRIALTLGPEVSRRGSSFTIRKFREVPLTPIDLIEWGTLsPELA-- 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 133 dadvsaidrrlldlhrtgsyqAFLREAVYARKNIIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRL 212
Cdd:COG0630  281 ---------------------AYLWLLLENGKSVLVAGGTASGKTTLLNALLSFIPPDAKIVTIEDTRELNLPHENWISL 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 213 F-YSKGGQGLAKVGAKDLLESCLRMRPDRILLQELRDGTAFYYIRNVNSGHPGsITTVHADSARLAFEQLTLlvkesegg 291
Cdd:COG0630  340 VtRESFGGEEGDVTMFDLLKAALRQRPDYIVVGEVRGEEAYTLFQAMATGHGV-LSTFHADSVESAINRLTS-------- 410

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 517056578 292 rdlerDDI---REMLKiAIDVIVQCKRID--GRF--RVTEIY 326
Cdd:COG0630  411 -----PPInvpRTLLQ-ALDLVVFQKRVRvgGKRvrRVTSIV 446
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
 65-325 5.36e-36

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 132.61  E-value: 5.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  65 VASFSNQAIDETRPILSATLP-GDERIQIVIPPATTKGtvSITIRKPSSVSLSLNDLDQGGLFAEvaredADVSAIdrrl 143
Cdd:PRK13833  69 VAHALQSEADDERPIISGELPiGGHRFEGLLPPVVSGP--AFTIRRRASRLIPLDDYVTSKIMTE-----AQASVI---- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 144 ldlhrtgsyqaflREAVYARKNIIISGATGSGKTTLSKALIRHIPSS---ERIISIEDTPELVIPQPNHVRLFYSKggqg 220
Cdd:PRK13833 138 -------------RSAIDSRLNIVISGGTGSGKTTLANAVIAEIVASapeDRLVILEDTAEIQCAAENAVALHTSD---- 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 221 laKVGAKDLLESCLRMRPDRILLQELRDGTAFYYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKESeggrdlERDDIR 300
Cdd:PRK13833 201 --TVDMARLLKSTMRLRPDRIIVGEVRDGAALTLLKAWNTGHPGGVTTIHSNTAMSALRRLEQLTAEA------SQQPMQ 272

                        250       260
                 ....*....|....*....|....*
gi 517056578 301 EMLKIAIDVIVQCKRIDGRFRVTEI 325
Cdd:PRK13833 273 EVIGEAVDLIVSIERTGKGRRVREV 297
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
 59-325 4.15e-30

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 116.76  E-value: 4.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  59 MRLARA------VASFSNQAIDETRPILSATLPGD-ERIQIVIPPATTKGTVSItiRKPSSVSLSLNDLDQGGLFaevar 131
Cdd:PRK13894  61 LRVAQAqaiietIAGYHGKEVTRSKPILEGELPLDgSRFAGQLPPVVPAPTFAI--RKKAVAIFTLDQYVERGIM----- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 132 edadvsaidrrlldlhrTGSYQAFLREAVYARKNIIISGATGSGKTTLSKALIRHI---PSSERIISIEDTPELVIPQPN 208
Cdd:PRK13894 134 -----------------TAAQREAIIAAVRAHRNILVIGGTGSGKTTLVNAIINEMviqDPTERVFIIEDTGEIQCAAEN 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 209 HVRLFYSkggqglAKVGAKDLLESCLRMRPDRILLQELRDGTAFYYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKES 288
Cdd:PRK13894 197 YVQYHTS------IDVNMTALLKTTLRMRPDRILVGEVRGPEALDLLMAWNTGHEGGAATLHANNAKAGLDRLKSLISMH 270

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 517056578 289 EGGrdleRDDIREMLKIAIDVIVQCKRIDGRFRVTEI 325
Cdd:PRK13894 271 PDA----PKPIEPLIGEAVHVVVHIARTPGGRRIQEI 303
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
 156-311 6.85e-28

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: 107.09  E-value: 6.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 156 LREAVYARKNIIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIPQP-NHVRLFYSkggqglAKVGAKDLLESCL 234
Cdd:cd19477    3 IKDGIAIGKNVIVCGGTGSGKTTYIKSILEFIPKEERIISIEDTEEIVFKHHkNYTQLFFG------GNITSADCLKSCL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517056578 235 RMRPDRILLQELRDGTAFYYIRNVNSGHPGSITTVHADSARLAFEQLTLLVKESEGGRDLERDDIREMLKIAIDVIV 311
Cdd:cd19477   77 RQRPDRIILGELRSSEAYDFYNVLCSGHKGTLTTLHAGSSEEAFIRLAN*SSSNSAARNIKFESLIEGFKDLIDGIV 153
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
 166-274 3.60e-18

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: 80.22  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSER-IISIEDTPELVIPQPNHVRLFySKGGQGLAkvgakDLLESCLRMRPDRILLQ 244
Cdd:cd01129   14 ILVTGPTGSGKTTTLYAMLRELNGPERnIITIEDPVEYQIPGINQSQVN-EKIGLTFA-----DALRAILRQDPDIIMVG 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 517056578 245 ELRDG-TAFYYIRNVNSGHPgSITTVHADSA 274
Cdd:cd01129   88 EIRDAeTAEIAIRAALTGHL-VLSTLHTNDA 117
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
166-275 7.38e-12

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 64.78  E-value: 7.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIP-----QPNHVrlfyskggqglAKVGAKDLLESCLRMRPDR 240
Cdd:NF041000 131 ILFSGPTGSGKTTTMYSLARKLALNKQVITIEDPVEIKEPnflqlQVNEK-----------AGMTYDTLLKAALRHRPDI 199

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517056578 241 ILLQELRDG-TAFYYIRNVNSGHPgSITTVHADSAR 275
Cdd:NF041000 200 LIIGEIRDAeTAKAAIRAALTGHL-VLSTVHAKSAA 234
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
 49-325 1.52e-11

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


Pssm-ID: 442056  Cd Length: 342  Bit Score: 64.34  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578  49 DLPELSFDKLMRLARAVASFSNQAI-DETRPI-LSATLPGDERIQIVIppATTKGTVSITIRKPSSVSLSLNDLdqgGLF 126
Cdd:COG2805   40 DDPPLTPEDLEALLKEILTEEQRERlEEEGELdFSYSLPGLGRFRVNI--FRQRGGVAAVLRLIPSEIPTLEEL---GLP 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 127 AEVaredadvsaidRRLLDLHRtGsyqafLreavyarknIIISGATGSGKTTLSKALIRHIPSSER--IISIEDTPELVI 204
Cdd:COG2805  115 PVL-----------KELAELPR-G-----L---------VLVTGPTGSGKSTTLAAMIDYINETRAkhIITIEDPIEFVH 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 205 PQPN----------HVRLFYSkggqglAkvgakdlLESCLRMRPDRILLQELRD----GTAfyyIRNVNSGHPgSITTVH 270
Cdd:COG2805  169 KHKKslinqrevgrDTPSFAN------A-------LRAALREDPDVILVGEMRDletiEAA---LTAAETGHL-VFATLH 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 271 ADSARLAFEQLtLLVKESEggrdlERDDIREMLKIAID-VIVQ--CKRIDGRFRV--TEI 325
Cdd:COG2805  232 TNSAAQTIDRI-IDVFPPE-----EQAQIRSQLAESLRgVISQrlLPRADGGGRVaaREI 285
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
 156-273 1.41e-09

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: 56.62  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 156 LREAVYARKNI-IISGATGSGKTTLSKALIRHI----PSSERIISIEDTPELVI--PQPNHVRLFYSKGGQGLAKVGAKd 228
Cdd:cd19516    3 LVEALFPREGLvYVAGATGSGKSTLLAAIYRYIlendPPDRKIITYEDPIEFVYdgIKSKHSIIVQSQIPRHFKSFAKA- 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 517056578 229 lLESCLRMRPDRILLQELRDG-TAFYYIRNVNSGHPgSITTVHADS 273
Cdd:cd19516   82 -VREALRRKPSLIGVGELRDQeTISAAVEASLTGHP-VYSTVHTKS 125
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
 166-325 1.71e-09

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: 57.16  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPS--SERIISIEDTPELVipqpnhvrlFYSKGG---Q---GLAKVGAKDLLESCLRMR 237
Cdd:cd01131   24 VLVTGPTGSGKSTTLAAMIDYINEtrSKHIITIEDPIEFV---------HKHKKSlinQrevGRDTESFAAALRAALRED 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 238 PDRILLQELRD-GTAFYYIRNVNSGHPgSITTVHADSARLAFEQLTLLVKESeggrdlERDDIREML-KIAIDVIVQ--C 313
Cdd:cd01131   95 PDVILVGEMRDlETIELALTAAETGHL-VFSTLHTNSAAQTIDRIIDVFPPE------QQEQVRIQLaSSLRGVISQrlL 167

                        170
                 ....*....|....
gi 517056578 314 KRIDGRFRV--TEI 325
Cdd:cd01131  168 PKKDGGGRVaaFEI 181
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
 166-205 7.70e-06

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: 45.78  E-value: 7.70e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSeRIISIED--TPELVIP 205
Cdd:cd02024    2 VGISGVTNSGKTTLAKLLQRILPNC-CVIHQDDffKPEDEIP 42
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
 166-251 2.11e-05

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: 45.95  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSER-IISIEDTPELVIP-----QPNHvrlfysKGGQGLAKVgakdlLESCLRMRPD 239
Cdd:COG2804  316 ILVTGPTGSGKTTTLYAALNELNTPERnIITVEDPVEYQLPginqvQVNP------KIGLTFASA-----LRSILRQDPD 384

                         90
                 ....*....|...
gi 517056578 240 RILLQELRDG-TA 251
Cdd:COG2804  385 VIMVGEIRDLeTA 397
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 163-246 3.80e-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: 43.13  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578   163 RKNIIISGATGSGKTTLSKALIRHI-PSSERIISIE-DTPELVIPQPNHVRLFYSKGGQGLAKVGAKDLLESCLRMRPDR 240
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81


                   ....*.
gi 517056578   241 ILLQEL 246
Cdd:smart00382  82 LILDEI 87
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
166-195 6.08e-05

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 43.13  E-value: 6.08e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSERIIS 195
Cdd:COG0194    5 IVLSGPSGAGKTTLVKALLERDPDLRFSVS 34
PRK10436 PRK10436
hypothetical protein; Provisional
 166-274 1.01e-04

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 43.76  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517056578 166 IIISGATGSGKT-TLSKALiRHIPSSER-IISIEDTPELVIPQPNHVRLfYSKGGQGLAKVgakdlLESCLRMRPDRILL 243
Cdd:PRK10436 221 ILVTGPTGSGKTvTLYSAL-QTLNTAQInICSVEDPVEIPLAGINQTQI-HPKAGLTFQRV-----LRALLRQDPDVIMV 293

                         90       100       110
                 ....*....|....*....|....*....|..
gi 517056578 244 QELRDG-TAFYYIRNVNSGHPgSITTVHADSA 274
Cdd:PRK10436 294 GEIRDGeTAEIAIKAAQTGHL-VLSTLHTNST 324
AAA_18 pfam13238
AAA domain;
166-214 5.07e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 39.33  E-value: 5.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 517056578  166 IIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELVIPQPNHVRLFY 214
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRESK 49
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 154-203 1.05e-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: 39.05  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517056578 154 AFLREAVYAR--KNIIISGATGSGKTTLSKALIRHIPSSERIISIEDTPELV 203
Cdd:cd00009    8 EALREALELPppKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLL 59
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 166-198 1.78e-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: 39.05  E-value: 1.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSSE-RIISIED 198
Cdd:COG0572   10 IGIAGPSGSGKTTFARRLAEQLGADKvVVISLDD 43
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 163-216 2.53e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 37.57  E-value: 2.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517056578  163 RKNIIISGATGSGKTTLSKALIRHIPSSERI--ISIEDTPELVIPQPNHVRLFYSK 216
Cdd:pfam13173   2 RKILVITGPRQVGKTTLLLQLIKELLPPENIlyINLDDPRLLKLADFELLELFLEL 57
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 151-204 2.62e-03

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs 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: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 38.33  E-value: 2.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517056578 151 SYQAFLREAVYARKNIIISGATGSGKTtlskaLIRHIPSSERIISIEDTPELVI 204
Cdd:cd17923    3 SHQAEAIEAARAGRSVVVTTGTASGKS-----LCYQLPILEALLRDPGSRALYL 51
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 166-190 4.87e-03

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 36.74  E-value: 4.87e-03
                         10        20
                 ....*....|....*....|....*
gi 517056578 166 IIISGATGSGKTTLSKALIRHIPSS 190
Cdd:cd00071    2 IVLSGPSGVGKSTLLKRLLEEFDPN 26
ResIII pfam04851
Type III restriction enzyme, res subunit;
151-203 5.74e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 36.88  E-value: 5.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517056578  151 SYQaflREAVYA--------RKNIIISGATGSGKTTLSKALIRHI---PSSERIISIEDTPELV 203
Cdd:pfam04851   6 PYQ---IEAIENllesikngQKRGLIVMATGSGKTLTAAKLIARLfkkGPIKKVLFLVPRKDLL 66
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 151-210 5.74e-03

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 38.60  E-value: 5.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517056578 151 SYQAFLREAVYARKN--IIISGATGSGKTTLSKALIRH---IPSSERIISIEDTPELVIPQPNHV 210
Cdd:cd14890   64 AYTQLIQSGVLDPSNqsIIISGESGAGKTEATKIIMQYlarITSGFAQGASGEGEAASEAIEQTL 128
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 151-187 5.92e-03

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 38.34  E-value: 5.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 517056578 151 SYQAFLREavyaRKN--IIISGATGSGKTTLSKALIRHI 187
Cdd:cd00124   64 AYRAMLRD----GQNqsILISGESGAGKTETTKLVLKYL 98
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 151-186 7.24e-03

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 37.25  E-value: 7.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 517056578 151 SYQAflrEAVYA--RKNIIISGATGSGKTTLSKALIRH 186
Cdd:cd18034    5 SYQL---ELFEAalKRNTIVVLPTGSGKTLIAVMLIKE 39
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 152-187 8.43e-03

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 37.91  E-value: 8.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 517056578   152 YQAFLREavyaRKN--IIISGATGSGKTTLSKALIRHI 187
Cdd:smart00242  83 YRNMLND----KENqsIIISGESGAGKTENTKKIMQYL 116
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 145-199 9.86e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 37.07  E-value: 9.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517056578 145 DLHRTGSYQAFLREAVYARKN----IIISGATGSGKTTLSKALIRHIPSSERIISIEDT 199
Cdd:COG3267   21 FLFLSPSHREALARLEYALAQgggfVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIPNP 79
 
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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