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Conserved domains on  [gi|294935264|ref|XP_002781356|]
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26S protease regulatory subunit, putative [Perkinsus marinus ATCC 50983]

Protein Classification

26S proteasome regulatory subunit 4( domain architecture ID 1002609)

26S proteasome regulatory subunit 4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins

Gene Ontology:  GO:0036402|GO:0016887|GO:0043161|GO:0005524

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PTZ00361 super family cl33178
26 proteosome regulatory subunit 4-like protein; Provisional
 31-384 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00361:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 617.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  31 APPPAHFGRRKKRvNKGPPGMSKIPTVVPTGKCRLRMLKLDRIKDYLLMEEEFINRQEAMKvGGEDRTEEERNKVDEIRG 110
Cdd:PTZ00361  25 SPPPPHEIKRKKK-RKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQK-PAQEKNEAELKKVDDLRG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 111 KPISVGNLEELIDDSHAIVSTSNGPEFYVNILSIVDQDQLEPGSSVLLHNKL---------------------------- 162
Cdd:PTZ00361 103 SPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKThsvvgilldevdplvsvmkvdkaplesy 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 ----------------------------------PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 208
Cdd:PTZ00361 183 adiggleqqiqeikeavelplthpelyddigikpPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 209 KLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRP 288
Cdd:PTZ00361 263 KLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRP 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 289 GRIDRKIEFPLPDINTKRRIFQIHTSKMTLADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKARE 368
Cdd:PTZ00361 343 GRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKE 422

                        410
                 ....*....|....*.
gi 294935264 369 KALYRKKGNIPEGMYL 384
Cdd:PTZ00361 423 KVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 31-384 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 617.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  31 APPPAHFGRRKKRvNKGPPGMSKIPTVVPTGKCRLRMLKLDRIKDYLLMEEEFINRQEAMKvGGEDRTEEERNKVDEIRG 110
Cdd:PTZ00361  25 SPPPPHEIKRKKK-RKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQK-PAQEKNEAELKKVDDLRG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 111 KPISVGNLEELIDDSHAIVSTSNGPEFYVNILSIVDQDQLEPGSSVLLHNKL---------------------------- 162
Cdd:PTZ00361 103 SPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKThsvvgilldevdplvsvmkvdkaplesy 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 ----------------------------------PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 208
Cdd:PTZ00361 183 adiggleqqiqeikeavelplthpelyddigikpPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 209 KLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRP 288
Cdd:PTZ00361 263 KLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRP 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 289 GRIDRKIEFPLPDINTKRRIFQIHTSKMTLADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKARE 368
Cdd:PTZ00361 343 GRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKE 422

                        410
                 ....*....|....*.
gi 294935264 369 KALYRKKGNIPEGMYL 384
Cdd:PTZ00361 423 KVLYRKKGNIPEGLYL 438
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 159-369 7.67e-104

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 309.24  E-value: 7.67e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 159 HNKLPP-GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTK 237
Cdd:COG1222  107 YGIEPPkGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAAR 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 238 RYDTTSGGEreIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMT 317
Cdd:COG1222  187 RTDDGTSGE--VQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMP 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 294935264 318 LADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREK 369
Cdd:COG1222  265 LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 163-297 3.17e-82

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 248.41  E-value: 3.17e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSG 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 243 SGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19502  117 TGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLRPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 161-376 2.13e-69

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 226.40  E-value: 2.13e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:TIGR01241  86 KIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  241 TTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLAD 320
Cdd:TIGR01241 166 GLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAP 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 294935264  321 DVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREKALY--RKKG 376
Cdd:TIGR01241 246 DVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAgpEKKS 303
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 166-299 2.15e-49

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 162.76  E-value: 2.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  166 VILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYdttSGG 245
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264  246 EREIQRTMLELLNQLDGFDQS-ADVKVILATNKIESLDPALLrpGRIDRKIEFPL 299
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 163-301 2.65e-16

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: 75.49  E-value: 2.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264   163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVV-----------------GSELIQKYLGDGPKLVREMFRVANEQAPSI 225
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294935264   226 VFIDEIDAVGTKrydttsggEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPgRIDRKIEFPLPD 301
Cdd:smart00382  82 LILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 166-243 5.16e-04

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: 41.30  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 166 VILYGAPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKYL---GDGpKLVREMFRVANeqaPSIVFIDEI-----D 232
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLAR---YDLLIIDELgylpfS 166

                         90
                 ....*....|....*....
gi 294935264 233 AVGT--------KRYDTTS 243
Cdd:NF038214 167 REGAnllfeliaDRYERGS 185
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 31-384 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 617.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  31 APPPAHFGRRKKRvNKGPPGMSKIPTVVPTGKCRLRMLKLDRIKDYLLMEEEFINRQEAMKvGGEDRTEEERNKVDEIRG 110
Cdd:PTZ00361  25 SPPPPHEIKRKKK-RKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQK-PAQEKNEAELKKVDDLRG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 111 KPISVGNLEELIDDSHAIVSTSNGPEFYVNILSIVDQDQLEPGSSVLLHNKL---------------------------- 162
Cdd:PTZ00361 103 SPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKThsvvgilldevdplvsvmkvdkaplesy 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 ----------------------------------PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 208
Cdd:PTZ00361 183 adiggleqqiqeikeavelplthpelyddigikpPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 209 KLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRP 288
Cdd:PTZ00361 263 KLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRP 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 289 GRIDRKIEFPLPDINTKRRIFQIHTSKMTLADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKARE 368
Cdd:PTZ00361 343 GRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKE 422

                        410
                 ....*....|....*.
gi 294935264 369 KALYRKKGNIPEGMYL 384
Cdd:PTZ00361 423 KVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 69-383 8.33e-123

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 359.92  E-value: 8.33e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  69 KLDRIKDYLLMEEEFINRQEAMKVGGEDRTEEERNKVDEIRGK-------PISVGNLEELIDDSHAIVSTSNGPEFYVNI 141
Cdd:PRK03992   2 RLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSEleklkspPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 142 LSIVDQDQLEPGSSVLLHNKL----------------------------------------------------------- 162
Cdd:PRK03992  82 SPFIDREKLKPGARVALNQQSlaivevlpsekdprvqameviespnvtyediggleeqirevreavelplkkpelfeevg 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 --PP-GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRY 239
Cdd:PRK03992 162 iePPkGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 240 DTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLA 319
Cdd:PRK03992 242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294935264 320 DDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREKAL---YRKKGNIPEGMY 383
Cdd:PRK03992 322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMgkeEKDSMEEPGVMF 388
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 65-375 6.38e-119

26S protease regulatory subunit 6B-like protein; Provisional


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 350.60  E-value: 6.38e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  65 LRMLKLDRIKDYLLMEEEFINRQEAMKVGGEDRTEEErnkVDEIRGKPISVGNLEELIDDSHAIVSTSNGPEFYVNILSI 144
Cdd:PTZ00454  22 EKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEE---VKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILST 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 145 VDQDQLEPGSSVLLH-------NKLPP----------------------------------------------------- 164
Cdd:PTZ00454  99 LNRELLKPNASVALHrhshavvDILPPeadssiqllqmsekpdvtysdiggldiqkqeireavelpltcpelyeqigidp 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 165 --GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:PTZ00454 179 prGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQ 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 243 SGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLADDV 322
Cdd:PTZ00454 259 TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEV 338

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 294935264 323 DLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAReKALYRKK 375
Cdd:PTZ00454 339 DLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGY-KTVVRKT 390
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 159-369 7.67e-104

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 309.24  E-value: 7.67e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 159 HNKLPP-GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTK 237
Cdd:COG1222  107 YGIEPPkGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAAR 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 238 RYDTTSGGEreIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMT 317
Cdd:COG1222  187 RTDDGTSGE--VQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMP 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 294935264 318 LADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREK 369
Cdd:COG1222  265 LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 163-297 3.17e-82

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 248.41  E-value: 3.17e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSG 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 243 SGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19502  117 TGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLRPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 161-376 2.13e-69

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 226.40  E-value: 2.13e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:TIGR01241  86 KIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  241 TTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLAD 320
Cdd:TIGR01241 166 GLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAP 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 294935264  321 DVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREKALY--RKKG 376
Cdd:TIGR01241 246 DVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAgpEKKS 303
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 161-369 1.78e-65

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 213.23  E-value: 1.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRyd 240
Cdd:COG0464  189 PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR-- 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 241 tTSGGEREIQRTMLELLNQLDGFdqSADVKVILATNKIESLDPALLRpgRIDRKIEFPLPDINTKRRIFQIHTSKMTLAD 320
Cdd:COG0464  267 -GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDE 341

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 294935264 321 DVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREK 369
Cdd:COG0464  342 DVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALER 390
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
161-369 1.83e-64

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 215.29  E-value: 1.83e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRyD 240
Cdd:COG0465  173 KIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQR-G 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 241 TTSGG---EREiqRTmlelLNQL----DGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHT 313
Cdd:COG0465  252 AGLGGghdERE--QT----LNQLlvemDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHA 325

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294935264 314 SKMTLADDVDLEE-------FvhskddlSGADIKAICTEAGMLALRERRMRVTAEDLRKAREK 369
Cdd:COG0465  326 RKKPLAPDVDLEViarrtpgF-------SGADLANLVNEAALLAARRNKKAVTMEDFEEAIDR 381
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 163-375 6.46e-60

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 206.30  E-value: 6.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRydTT 242
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GA 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  243 SGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLADDV 322
Cdd:TIGR01243 565 RFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDV 644

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 294935264  323 DLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREKALYRKK 375
Cdd:TIGR01243 645 DLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKDLK 697
ftsH CHL00176
cell division protein; Validated
 151-369 2.82e-55

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 192.19  E-value: 2.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 151 EPGSSVLLHNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDE 230
Cdd:CHL00176 204 KPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDE 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 231 IDAVGTKRYDTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQ 310
Cdd:CHL00176 284 IDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILK 363

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 294935264 311 IHTSKMTLADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREK 369
Cdd:CHL00176 364 VHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDR 422
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
151-371 9.04e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 188.32  E-value: 9.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 151 EPGSSVLLHNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDE 230
Cdd:PRK10733 173 EPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 231 IDAVGTKRYDTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQ 310
Cdd:PRK10733 253 IDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILK 332

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294935264 311 IHTSKMTLADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREKAL 371
Cdd:PRK10733 333 VHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIM 393
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 161-295 1.87e-53

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 174.73  E-value: 1.87e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:cd19501   35 KIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGA 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 241 TTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKI 295
Cdd:cd19501  115 GLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGRFDRQV 169
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 163-352 1.86e-52

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 185.88  E-value: 1.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:TIGR01243 212 PKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  243 sgGEREiQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLADDV 322
Cdd:TIGR01243 292 --GEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDV 368

                         170       180       190
                  ....*....|....*....|....*....|
gi 294935264  323 DLEEFVHSKDDLSGADIKAICTEAGMLALR 352
Cdd:TIGR01243 369 DLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 158-297 5.07e-52

proteases similar to RecA; 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: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 170.54  E-value: 5.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 158 LHNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTK 237
Cdd:cd19481   21 YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPCILFIDEIDAIGRK 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 238 RydTTSGGEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19481  101 R--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 166-299 2.15e-49

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 162.76  E-value: 2.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  166 VILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYdttSGG 245
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264  246 EREIQRTMLELLNQLDGFDQS-ADVKVILATNKIESLDPALLrpGRIDRKIEFPL 299
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
159-381 3.84e-48

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 163.52  E-value: 3.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 159 HNKLPPGVIL-YGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVAnEQAPSIVFIDEIDAVGTK 237
Cdd:COG1223   30 FGLWPPRKILfYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 238 RYDTTSGGerEIQRTMLELLNQLDGFDQsaDVKVILATNKIESLDPALLRpgRIDRKIEFPLPDINTKRRIFQIHTSKMT 317
Cdd:COG1223  109 RGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFP 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294935264 318 LADDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRKAREKALYRKKGNIPEG 381
Cdd:COG1223  183 LPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKERKKEPKKEG 246
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 163-297 4.07e-48

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 160.53  E-value: 4.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQ 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 243 SGGEReiqRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19503  114 REVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 161-295 1.67e-47

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 158.99  E-value: 1.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:cd19511   25 RPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFFDEIDSLAPRRGQ 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 241 TTSGGEREiqRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKI 295
Cdd:cd19511  105 SDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 161-295 4.33e-44

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 149.95  E-value: 4.33e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:cd19529   25 RPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFFDEIDSIAPRRGT 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 241 TTSGGEREiqRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKI 295
Cdd:cd19529  105 TGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 161-298 5.32e-43

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 147.58  E-value: 5.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:cd19519   32 KPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREK 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294935264 241 TTSGGEReiqRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFP 298
Cdd:cd19519  112 THGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREIDIG 166
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 161-295 6.58e-39

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 136.71  E-value: 6.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:cd19509   30 GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFIDEIDSLLSERGS 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 294935264 241 TTSGGEREIqRTmlELLNQLDGFDQSAD--VKVILATNKIESLDPALLRpgRIDRKI 295
Cdd:cd19509  110 GEHEASRRV-KT--EFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR--RFEKRI 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 165-295 1.33e-37

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 133.02  E-value: 1.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 165 GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTTSG 244
Cdd:cd19528   29 GVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFFDELDSIAKARGGNIGD 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 294935264 245 GEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKI 295
Cdd:cd19528  109 AGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 162-293 2.18e-37

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 132.61  E-value: 2.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 162 LPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDT 241
Cdd:cd19530   29 LPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFFDEVDALVPKRGDG 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 294935264 242 TSGGereIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDR 293
Cdd:cd19530  109 GSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 165-293 1.64e-33

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 122.24  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 165 GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDT-TS 243
Cdd:cd19527   28 GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFFDELDSLAPSRGNSgDS 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 294935264 244 GGerEIQRTMLELLNQLDGF-DQSADVKVILATNKIESLDPALLRPGRIDR 293
Cdd:cd19527  108 GG--VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 161-296 5.15e-33

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 121.00  E-value: 5.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKR-Y 239
Cdd:cd19526   25 RLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFDEFDSIAPKRgH 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 294935264 240 DTTSGGEREIQrtmlELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIE 296
Cdd:cd19526  105 DSTGVTDRVVN----QLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 163-295 1.40e-31

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 117.51  E-value: 1.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRydtt 242
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFIDEIDAITPKR---- 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294935264 243 SGGEREIQRTML-ELLNQLDGF----DQSADVKVILATNKIESLDPALLRPGRIDRKI 295
Cdd:cd19518  110 ESAQREMERRIVsQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRAGRFDREI 167
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 163-287 5.23e-31

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 115.72  E-value: 5.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:cd19524   33 ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGE 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 294935264 243 SGGEReiqRTMLELLNQLDGFDQSADVKVIL--ATNKIESLDPALLR 287
Cdd:cd19524  113 HEASR---RLKTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVLR 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 159-295 5.76e-31

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 116.11  E-value: 5.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 159 HNKLP-PGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTK 237
Cdd:cd19521   35 GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGT 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 294935264 238 RYDTTSGGEREIQRtmlELLNQLDGFDQSAD-VKVILATNKIESLDPALLRpgRIDRKI 295
Cdd:cd19521  115 RGEGESEASRRIKT---ELLVQMNGVGNDSQgVLVLGATNIPWQLDSAIRR--RFEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 163-287 3.94e-29

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 111.62  E-value: 3.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:cd19525   55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 294935264 243 SGGEREIQRtmlELLNQLDGFDQSADVKVIL--ATNKIESLDPALLR 287
Cdd:cd19525  135 HESSRRIKT---EFLVQLDGATTSSEDRILVvgATNRPQEIDEAARR 178
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 165-295 4.69e-29

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 110.84  E-value: 4.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 165 GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRydtTSG 244
Cdd:cd19522   35 GVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTS 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 294935264 245 GEREI-QRTMLELLNQLDGF-------DQSADVKVILATNKIESLDPALLRpgRIDRKI 295
Cdd:cd19522  112 EEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEALRR--RLEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 114-287 8.66e-29

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 109.82  E-value: 8.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 114 SVGNLEELIDDSHAIVstsngpefyvnILSIVDQDQLEpgSSVLLhnKLPPGVILYGAPGTGKTLLAKAVANETSATFLR 193
Cdd:cd19520    1 DIGGLDEVITELKELV-----------ILPLQRPELFD--NSRLL--QPPKGVLLYGPPGCGKTMLAKATAKEAGARFIN 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 194 VVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRydttSGGEREIQRTM-LELLNQLDGFDQSADVKVI 272
Cdd:cd19520   66 LQVSSLTDKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVI 141

                        170
                 ....*....|....*..
gi 294935264 273 L--ATNKIESLDPALLR 287
Cdd:cd19520  142 VmgATNRPQDLDEAILR 158
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 163-297 1.71e-28

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 109.52  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSA-----TFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTK 237
Cdd:cd19517   34 PRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPV 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 238 RYDTTSGGEREIQRTMLELLnqlDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19517  114 RSSKQEQIHASIVSTLLALM---DGLDNRGQVVVIGATNRPDALDPALRRPGRFDREFYF 170
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 157-299 1.22e-23

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: 95.68  E-value: 1.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 157 LLHNKLPPGVILYGAPGTGKTLLAKAVANET---SATFLRVVGSELIQKYLG---DGPKLVREMFRVANEQAPSIVFIDE 230
Cdd:cd00009   13 ALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDE 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 231 IDAVGtkrydttsggeREIQRTMLELLNQL-DGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEFPL 299
Cdd:cd00009   93 IDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
 163-366 2.22e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 101.25  E-value: 2.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYDTT 242
Cdd:CHL00195 259 PRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKG 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 243 -SGGEREIQRTMLELLNQldgfdQSADVKVILATNKIESLDPALLRPGRIDRKIEFPLPDINTKRRIFQIHTSKMTLA-- 319
Cdd:CHL00195 339 dSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKsw 413

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 294935264 320 DDVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRmRVTAEDLRKA 366
Cdd:CHL00195 414 KKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR-EFTTDDILLA 459
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 161-287 4.69e-23

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 94.57  E-value: 4.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 161 KLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEIDAVGTKRYD 240
Cdd:cd19523   31 RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQDD 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 294935264 241 ttsgGEREIQRTMLELLNQLDGFDQSAD--VKVILATNKIESLDPALLR 287
Cdd:cd19523  111 ----EASPVGRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 162-293 2.30e-21

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 89.74  E-value: 2.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 162 LPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFRVANEQAPSIVFIDEID-AVGTKRYD 240
Cdd:cd19507   30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSK 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 294935264 241 TTSGGEREIQRTMLELLNQldgfdQSADVKVILATNKIESLDPALLRPGRIDR 293
Cdd:cd19507  110 GDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 165-296 1.70e-20

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 87.93  E-value: 1.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 165 GVILYGAPGTGKTLLAKAVANETSATFLRVV-GSELIQKYLGDGPKLVREMFRVANEQAPS--------IVFIDEIDAVG 235
Cdd:cd19504   37 GILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAIC 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294935264 236 TKRydTTSGGEREIQRTML-ELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIE 296
Cdd:cd19504  117 KQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQME 176
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 165-297 3.72e-19

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. 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: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 83.55  E-value: 3.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 165 GVILYGAPGTGKTLLAKAVANETSATFLRVvgsELIQKYLGDgpKLVREMFRVANEQapSIVFIDEIDAVGTKRYDT--- 241
Cdd:cd19510   25 GYLLYGPPGTGKSSFIAALAGELDYDICDL---NLSEVVLTD--DRLNHLLNTAPKQ--SIILLEDIDAAFESREHNkkn 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 294935264 242 --TSGGEREIqrTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19510   98 psAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 163-301 2.65e-16

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: 75.49  E-value: 2.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264   163 PPGVILYGAPGTGKTLLAKAVANETSATFLRVV-----------------GSELIQKYLGDGPKLVREMFRVANEQAPSI 225
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294935264   226 VFIDEIDAVGTKrydttsggEREIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPALLRPgRIDRKIEFPLPD 301
Cdd:smart00382  82 LILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 154-285 9.62e-13

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 66.32  E-value: 9.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 154 SSVLLHNKLppgVILYGAPGTGKTLLAKAVANETS---------ATFLRVVGSELIQKYLGDGPKLVREMFR-----VAN 219
Cdd:cd19508   46 TNLITWNRL---VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDD 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294935264 220 EQAPSIVFIDEIDAVGTKRYDTTSGGE-REIQRTMLELLNQLDGFDQSADVKVILATNKIESLDPAL 285
Cdd:cd19508  123 KDALVFVLIDEVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 321-365 1.82e-11

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 58.32  E-value: 1.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 294935264  321 DVDLEEFVHSKDDLSGADIKAICTEAGMLALRERRMRVTAEDLRK 365
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 159-297 8.62e-11

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 59.85  E-value: 8.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 159 HNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQkyLG-DGPKLVREMFRVANEQAPS-IVFIDEIDAVGT 236
Cdd:cd19512   18 NKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294935264 237 KRydtTSGGEREIQRTMLELLNQLDGfDQSADVKVILATNKIESLDPALlrPGRIDRKIEF 297
Cdd:cd19512   96 KR---STEKISEDLRAALNAFLYRTG-EQSNKFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 155-370 9.13e-10

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 59.57  E-value: 9.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  155 SVLLHNKLPPGVILYGAPGTGKTLLAKAVANE----TSATFLRV---------------VGSELIQKYLGDGP------- 208
Cdd:TIGR02928  32 RPILRGSRPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVLVELANQLRGSGEevpttgl 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  209 ---KLVREMFRVANEQAPSIVFI-DEIDavgtkrYDTTSGGEREIQRTMLELLNQLDGfdqsADVKVILATNKI---ESL 281
Cdd:TIGR02928 112 stsEVFRRLYKELNERGDSLIIVlDEID------YLVGDDDDLLYQLSRARSNGDLDN----AKVGVIGISNDLkfrENL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  282 DPAL---LRPgridRKIEFPLPDINTKRRIFQiHTSKMTLADDVDLEEFVHSKDDLSGADI----KAICT--EAGMLALR 352
Cdd:TIGR02928 182 DPRVkssLCE----EEIIFPPYDAEELRDILE-NRAEKAFYDGVLDDGVIPLCAALAAQEHgdarKAIDLlrVAGEIAER 256

                         250
                  ....*....|....*...
gi 294935264  353 ERRMRVTAEDLRKAREKA 370
Cdd:TIGR02928 257 EGAERVTEDHVEKAQEKI 274
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 115-161 1.90e-09

Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 52.89  E-value: 1.90e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 294935264  115 VGNLEELIDDSHAIVSTSNGPEFYVNILSIVDQDQLEPGSSVLLHNK 161
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPR 47
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
157-370 1.46e-08

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 56.01  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 157 LLHNKLPPGVILYGAPGTGKTLLAKAVANE-----------------------TSATFLRVVGSELIQKYL----GDGPK 209
Cdd:COG1474   45 ALRGERPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergvdvrvvyvncrqasTRYRVLSRILEELGSGEDipstGLSTD 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 210 LVREMF--RVANEQAPSIVFIDEIDAVGTKRYDttsggerEIQRTMLELLNQLDGfdqsADVKVILATNKI---ESLDPA 284
Cdd:COG1474  125 ELFDRLyeALDERDGVLVVVLDEIDYLVDDEGD-------DLLYQLLRANEELEG----ARVGVIGISNDLeflENLDPR 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 285 L---LRPgridRKIEFP------LPDINTKRRifqihtsKMTLADDVdLEEfvhskD------DLSGADI----KAICT- 344
Cdd:COG1474  194 VkssLGE----EEIVFPpydadeLRDILEDRA-------ELAFYDGV-LSD-----EvipliaALAAQEHgdarKAIDLl 256

                        250       260
                 ....*....|....*....|....*..
gi 294935264 345 -EAGMLALRERRMRVTAEDLRKAREKA 370
Cdd:COG1474  257 rVAGEIAEREGSDRVTEEHVREAREKI 283
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 144-231 6.18e-08

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 54.29  E-value: 6.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 144 IVDQDQL-EPGS--SVLLHNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRV--VGSeliqkylgdGPKLVREMFRVA 218
Cdd:COG2256   27 VVGQEHLlGPGKplRRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEA 97

                         90
                 ....*....|....*..
gi 294935264 219 NEQA----PSIVFIDEI 231
Cdd:COG2256   98 RERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 144-231 8.51e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.55  E-value: 8.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 144 IVDQDQL-EPGS--SVLLHNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSEliqkylgDGPKLVREMFrvanE 220
Cdd:PRK13342  14 VVGQEHLlGPGKplRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVI----E 82

                         90
                 ....*....|....*....
gi 294935264 221 QAPS--------IVFIDEI 231
Cdd:PRK13342  83 EARQrrsagrrtILFIDEI 101
44 PHA02544
clamp loader, small subunit; Provisional
 164-301 2.41e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 48.83  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 164 PGVILY-GAPGTGKTLLAKAVANETSATFLRVVGSEliqkylgDGPKLVR-EMFRVAN----EQAPSIVFIDEIDAVGTK 237
Cdd:PHA02544  43 PNMLLHsPSPGTGKTTVAKALCNEVGAEVLFVNGSD-------CRIDFVRnRLTRFAStvslTGGGKVIIIDEFDRLGLA 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294935264 238 rydttsggerEIQRTMLELLNQLdgfdqSADVKVILATNKIESLDPALLrpGRIdRKIEFPLPD 301
Cdd:PHA02544 116 ----------DAQRHLRSFMEAY-----SKNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPT 161
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 110-368 3.68e-06

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 48.02  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 110 GKPISVGNLEELID--DSHAIVSTSNgpefYVNILSIVDQDQLEPGSsvllhnklppgVILYGAPGTGKTLLAKAVANE- 186
Cdd:COG2842   10 AKEIGNEKLEAKIArwEAPSFVETKN----VRRFAEALDEARALPGI-----------GVVYGESGVGKTTAAREYANRn 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 187 ------------TSATFLRVVGSELiqkYLGDGPKLVREMFRVANEQ---APSIVFIDEIDAVGTKrydttsggereiqr 251
Cdd:COG2842   75 pnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILERlagTGRLLIIDEADHLKPK-------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 252 tMLELLNQLdgFDQSaDVKVILATNkiESLdPALLRP-----GRIDRKIEF---PLPDIntkRRIFQIhtskMTLADDVD 323
Cdd:COG2842  138 -ALEELRDI--HDET-GVGVVLIGM--ERL-PAKLKRyeqlySRIGFWVEFkplSLEDV---RALAEA----WGELTDPD 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 294935264 324 LEEFVHskdDLSGADIKAICT---EAGMLALRERRMRVTAEDLRKARE 368
Cdd:COG2842  204 LLELLH---RITRGNLRRLDRtlrLAARAAKRNGLTKITLDHVRAAAL 248
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 166-229 6.22e-06

Protein of unknown function (DUF815); This family consists of several bacterial proteins of unknown function.


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 47.14  E-value: 6.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294935264  166 VILYGAPGTGKTLLAKAVANETSATFLRVVgsELIQKYLGDGPKLVREmfrVANEQAPSIVFID 229
Cdd:pfam05673  56 VLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLPDLVDL---LRDRPYRFILFCD 114
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 64-190 1.99e-05

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 46.30  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  64 RLRMLKLDRIKDYLLMEEEFINRQEAMKVGGEDRTEEERNKVDEIRGKPISVGNleelIDDSHAIVSTSNGPEFYVNILS 143
Cdd:COG1401  129 LEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELS----AAEELYSEDLESEDDYLKDLLR 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 294935264 144 IVDQDQLEPGSSVLlhnKLPPGVILYGAPGTGKTLLAKAVANETSAT 190
Cdd:COG1401  205 EKFEETLEAFLAAL---KTKKNVILAGPPGTGKTYLARRLAEALGGE 248
PRK04195 PRK04195
replication factor C large subunit; Provisional
 158-373 2.86e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 46.07  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 158 LHNKLPPGVILYGAPGTGKTLLAKAVANE--------------TSATFLRVVGSELIQKYLGDGPKlvremfrvaneqap 223
Cdd:PRK04195  34 LKGKPKKALLLYGPPGVGKTSLAHALANDygwevielnasdqrTADVIERVAGEAATSGSLFGARR-------------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 224 SIVFIDEIDAVgTKRYDTtsGGEREIqrtmLELLNQldgfdqsADVKVILATNKIESLDPALLRPgrIDRKIEF-PLPDI 302
Cdd:PRK04195 100 KLILLDEVDGI-HGNEDR--GGARAI----LELIKK-------AKQPIILTANDPYDPSLRELRN--ACLMIEFkRLSTR 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294935264 303 NTKRRIFQIHTSKMTLADDVDLEEFV-HSKDDLSGAdIKaicteagML-ALRERRMRVTAEDLR----KAREKALYR 373
Cdd:PRK04195 164 SIVPVLKRICRKEGIECDDEALKEIAeRSGGDLRSA-IN-------DLqAIAEGYGKLTLEDVKtlgrRDREESIFD 232
AAA_22 pfam13401
AAA domain;
166-274 9.18e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 9.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  166 VILYGAPGTGKTLLAKAVANE-----------------TSATFLRVVGSELIQKYLGDGPK--LVREMFRVANEQAPSIV 226
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLPLSGRLSKeeLLAALQQLLLALAVAVV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 294935264  227 F-IDEIDAvgtkrydttsggereIQRTMLELLNQLDGFDqSADVKVILA 274
Cdd:pfam13401  88 LiIDEAQH---------------LSLEALEELRDLLNLS-SKLLQLILV 120
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 166-232 9.97e-05

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 43.62  E-value: 9.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 166 VILYGAPGTGKTLLAKAVANETSATFLRV-----------VGSELIQKYLGD-----GPklvreMFRvaneqapSIVFID 229
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101


                 ...
gi 294935264 230 EID 232
Cdd:COG0714  102 EIN 104
PRK13341 PRK13341
AAA family ATPase;
167-231 1.58e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.89  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 167 ILYGAPGTGKTLLAKAVANETSATFLrVVGSELiqkylgDGPKLVREMFRVANEQAP-----SIVFIDEI 231
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKERLErhgkrTILFIDEV 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 165-287 1.82e-04

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 41.12  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  165 GVILYGAPGTGKTLLAKAVANETS-ATFLRVVGS------ELIQKY--------LGDGPkLVREMfrvaneQAPSIVFID 229
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRnidpggasWVDGP-LVRAA------REGEIAVLD 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294935264  230 EIDAvgtkrydttsgGEREIQRTMLELLN-----QLDGF----DQSADVKVILATN----KIESLDPALLR 287
Cdd:pfam07728  74 EINR-----------ANPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNpldrGLNELSPALRS 133
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 152-230 2.00e-04

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 41.36  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 152 PGSSVLLHNKLP--PGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG-DGPKLVREM-FRVANEQAPSIVF 227
Cdd:cd19506   13 PLGSQAVHEKAPlvKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGkNGLQMMLHLvLKVARQLQPSVIW 92


                 ...
gi 294935264 228 IDE 230
Cdd:cd19506   93 IGD 95
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 158-297 2.64e-04

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 41.21  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 158 LHNKLPP--GVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQ---KYLGDGPKLVREM-----------FRVANEQ 221
Cdd:cd19505    5 LRLGLSPskGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpDFGNDDWIDGMLIlkeslhrlnlqFELAKAM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 222 APSIVFIDEIDAVGTKRYDTTSGGEReiqRTMLELLNQLDGFDQSADVK----VILATNKIESLDPALLRPGRIDRKIEF 297
Cdd:cd19505   85 SPCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 162-257 4.02e-04

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 40.83  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 162 LPPGVILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQ-KYLGdgpKLVREMFRvanEQAPSIVFIDEIDAVGTKryD 240
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG---RDVESIIR---DLVEGIVFIDEIDKIAKR--G 116

                         90       100
                 ....*....|....*....|
gi 294935264 241 TTSGGE--RE-IQRTMLELL 257
Cdd:cd19498  117 GSSGPDvsREgVQRDLLPIV 136
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 166-243 5.16e-04

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: 41.30  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 166 VILYGAPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKYL---GDGpKLVREMFRVANeqaPSIVFIDEI-----D 232
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLAR---YDLLIIDELgylpfS 166

                         90
                 ....*....|....*....
gi 294935264 233 AVGT--------KRYDTTS 243
Cdd:NF038214 167 REGAnllfeliaDRYERGS 185
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 166-237 9.80e-04

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 40.28  E-value: 9.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 166 VILYGAPGTGKTLLAK----------AVANETSATFLRVVGSE---LIQKYLGDGpklvreMFRVANEQApSIVFIDEID 232
Cdd:cd19497   53 ILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGEDvenILLKLLQAA------DYDVERAQR-GIVYIDEID 125


                 ....*
gi 294935264 233 AVGTK 237
Cdd:cd19497  126 KIARK 130
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 167-298 1.00e-03

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 40.98  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  167 ILYGAPGTGKTLLAKAVANETSA-TFLR------VVGSELIQKYLGDGPKLVREMFRVAneqAPSIVFIDEIDAVGTKRY 239
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreVSRADLIGQYIGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGY 392

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294935264  240 DTTSGGEREIQRTMLELL-NQLD-----GFDQSADVKVILATNKiesldpaLLRpGRIDRKIEFP 298
Cdd:TIGR03922 393 GQKDPFGLEAIDTLLARMeNDRDrlvviGAGYRKDLDKFLEVNE-------GLR-SRFTRVIEFP 449
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
166-231 1.12e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.50  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 166 VILYGAPGTGKTLLAKAVANETSATfLRVVGSELIQKyLGDgpklvremfrVA----NEQAPSIVFIDEI 231
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD----------LAailtNLEEGDVLFIDEI 111
cdc6 PRK00411
ORC1-type DNA replication protein;
157-372 1.26e-03

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 40.60  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 157 LLHNKLPPGVILYGAPGTGKTLLAKAVANETSATFLRV---------------VGSELIQKYLGDGPKLV----REMFR- 216
Cdd:PRK00411  49 ALRGSRPLNVLIYGPPGTGKTTTVKKVFEELEEIAVKVvyvyincqidrtryaIFSEIARQLFGHPPPSSglsfDELFDk 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 217 -----VANEQAPsIVFIDEIDAVGTKRYDttsggerEIQRTMLELLNQLDGfdqsADVKVILATN---KIESLDP---AL 285
Cdd:PRK00411 129 iaeylDERDRVL-IVALDDINYLFEKEGN-------DVLYSLLRAHEEYPG----ARIGVIGISSdltFLYILDPrvkSV 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 286 LRPgridRKIEFP------LPDINTKRrifqihtSKMTLADDVDLEEFVHSKDDLSGADI----KAICT--EAGMLALRE 353
Cdd:PRK00411 197 FRP----EEIYFPpytadeIFDILKDR-------VEEGFYPGVVDDEVLDLIADLTAREHgdarVAIDLlrRAGLIAERE 265

                        250
                 ....*....|....*....
gi 294935264 354 RRMRVTAEDLRKAREKALY 372
Cdd:PRK00411 266 GSRKVTEEDVRKAYEKSEI 284
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 166-260 1.97e-03

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 37.87  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 166 VILYGAPGTGKTLLAKAVANETSATFLRVVGSELIQKYLgdgpklvREMFRVANEQAPSIVFIDEIDAVGTKRYDTTSGG 245
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                         90
                 ....*....|....*
gi 294935264 246 EREIQRTMLELLNQL 260
Cdd:cd01120   74 LLEDLAKLLRAARNT 88
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
165-231 1.98e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 1.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294935264 165 GVILYGAPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKY---LGDGpKLVREMFRVANeqaPSIVFIDEI 231
Cdd:COG1484  101 NLILLGPPGTGKTHLAIALGHEacragYRVRFTTA--PDLVNELkeaRADG-RLERLLKRLAK---VDLLILDEL 169
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 163-257 2.09e-03

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 38.72  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264  163 PPGVILY-GAPGTGKTLLAKAVANE---TSATFLRVVGSELIQKYLgdgpkLVREM----FRVANEQA-----------P 223
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHS-----VSRLIgappGYVGYEEGgqlteavrrkpY 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 294935264  224 SIVFIDEIDAVGtkrydttsggeREIQRTMLELL 257
Cdd:pfam07724  77 SIVLIDEIEKAH-----------PGVQNDLLQIL 99
PRK08116 PRK08116
hypothetical protein; Validated
 165-195 2.40e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 39.23  E-value: 2.40e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 294935264 165 GVILYGAPGTGKTLLAKAVANETSATFLRVV 195
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 166-231 3.43e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 3.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294935264  166 VILYGAPGTGKTLLAKAVANETSATFlRVVGSELIQKyLGDGPKLvremfrVANEQAPSIVFIDEI 231
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAI------LTNLEPGDVLFIDEI 93
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 168-286 3.44e-03

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which 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. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 38.31  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294935264 168 LYGAPGTGKTLLAKAVANETSATFLRV-VG-----SELI---QKYLGDGP-KLVREMfRVANEQAPSIVfIDEIDAVGTK 237
Cdd:cd19500   42 LVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPgRIIQAL-KKAGTNNPVFL-LDEIDKIGSS 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294935264 238 -RYDTTSGgereiqrtMLELL----------NQLD-GFDQSaDVKVILATNKIESLDPALL 286
Cdd:cd19500  120 fRGDPASA--------LLEVLdpeqnstfsdHYLDvPFDLS-KVLFIATANSLDTIPGPLL 171
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
157-186 4.22e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 38.80  E-value: 4.22e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 294935264 157 LLHNKLPPGVILYGAPGTGKTLLAKAVANE 186
Cdd:COG0470   12 AESGRLPHALLLHGPPGIGKTTLALALARD 41
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
166-194 9.79e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.43  E-value: 9.79e-03
                         10        20
                 ....*....|....*....|....*....
gi 294935264 166 VILYGAPGTGKTLLAKAVANETSATFLRV 194
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
 
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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