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Conserved domains on  [gi|164698506|ref|NP_033216|]
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vacuolar protein sorting-associated protein 4B [Mus musculus]

Protein Classification

vacuolar protein sorting-associated protein 4( domain architecture ID 15269737)

vacuolar protein sorting-associated protein 4 is an ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain.

CATH:  1.10.8.60
Gene Ontology:  GO:0005524|GO:0016887|GO:0007033|GO:0015031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 128-298 1.46e-126

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: 363.41  E-value: 1.46e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 128 RPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSK 207
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEAN-STFFSVSSSDLVSK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 208 WLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSA 287
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 164698506 288 IRRRFEKRIYI 298
Cdd:cd19521  160 IRRRFEKRIYI 170
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 381-441 1.23e-35

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 125.69  E-value: 1.23e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164698506  381 LTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTEDFG 441
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-69 2.34e-31

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


:

Pssm-ID: 239141  Cd Length: 75  Bit Score: 114.67  E-value: 2.34e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506   7 NLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGdKAKQSIRAKCTEYLDRA 69
Cdd:cd02678    2 FLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRA 63
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 325-366 6.83e-08

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: 48.69  E-value: 6.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164698506  325 DFQELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVR 366
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 128-298 1.46e-126

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: 363.41  E-value: 1.46e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 128 RPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSK 207
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEAN-STFFSVSSSDLVSK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 208 WLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSA 287
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 164698506 288 IRRRFEKRIYI 298
Cdd:cd19521  160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 50-355 3.91e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 271.49  E-value: 3.91e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  50 QGDKAKQSIRAKCTEYLDRAEKLKEYLKKKEKKPQKPVKEEQSGPVDEKGNDSDGEAESDDPEKKklqnqlqGAIVIERP 129
Cdd:COG1222    1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRG-------TAVPAESP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 130 NVKWSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSK 207
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELG-APFIRVRGSELVSK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 208 WLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSEN-ESEAARRIKTEFLVQMQGVGvDNDGILVLGATNIPWVLDS 286
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFE-SRGDVLIIAATNRPDLLDP 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164698506 287 AIRR--RFEKRIYIPLPEAHARAAMFRLHLGStQNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRK 355
Cdd:COG1222  231 ALLRpgRFDRVIEVPLPDEEAREEILKIHLRD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE 300
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 124-442 2.33e-67

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: 228.25  E-value: 2.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  124 IVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISS 201
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESG-ANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  202 SDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAAR-RIKTEFLVQMQGVgVDNDGILVLGATNI 280
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTdRIVNQLLTEMDGI-QELSNVVVIAATNR 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  281 PWVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHLGSTqNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRKVQS 358
Cdd:TIGR01243 600 PDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSM-PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIG 678

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  359 ATHFKKVRGPSRAdpncIVNDLltpcspgdpgaiemtwmdvpgdkllepVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTE 438
Cdd:TIGR01243 679 SPAKEKLEVGEEE----FLKDL---------------------------KVEMRHFLEALKKVKPSVSKEDMLRYERLAK 727


                  ....
gi 164698506  439 DFGQ 442
Cdd:TIGR01243 728 ELKR 731
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 125-355 6.50e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 210.84  E-value: 6.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 125 VIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFtgKR---TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISS 201
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF--EEvgiEPPKGVLLYGPPGTGKTLLAKAVAHETN-ATFIRVVG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 202 SDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAAR---RIKTEFLVQMQgvGVDNDG-ILVLGA 277
Cdd:PRK03992 199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMD--GFDPRGnVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 278 TNIPWVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHlgsTQN-SLTEA-DFQELGRKTDGYSGADISIIVRDALMQPV 353
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIH---TRKmNLADDvDLEELAELTEGASGADLKAICTEAGMFAI 353


                 ..
gi 164698506 354 RK 355
Cdd:PRK03992 354 RD 355
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 170-300 4.59e-57

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: 184.33  E-value: 4.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  170 ILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESE 249
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164698506  250 AARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPL 300
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 381-441 1.23e-35

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 125.69  E-value: 1.23e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164698506  381 LTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTEDFG 441
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-69 2.34e-31

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 114.67  E-value: 2.34e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506   7 NLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGdKAKQSIRAKCTEYLDRA 69
Cdd:cd02678    2 FLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRA 63
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 8-69 5.41e-23

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 91.83  E-value: 5.41e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506    8 LQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKyEAQGDKAKQSIRAKCTEYLDRA 69
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALK-ETKNEERRELLRAKIAEYLERA 61
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 166-302 4.31e-21

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: 89.35  E-value: 4.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506   166 PWRGILLFGPPGTGKSYLAKAVATEAN--NSTFFSISSSDL--------------VSKWLGESEKLVKNLFQLARENKPS 229
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506   230 IIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGvgvdndGILVLGATNIPWVLDSA-IRRRFEKRIYIPLPE 302
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
6-69 3.27e-19

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 81.59  E-value: 3.27e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506     6 TNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEaQGDKAKQSIRAKCTEYLDRA 69
Cdd:smart00745   3 DYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVE-SDSKRREALKAKAAEYLDRA 65
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 325-366 6.83e-08

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: 48.69  E-value: 6.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164698506  325 DFQELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVR 366
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 170-236 1.26e-06

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: 49.39  E-value: 1.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506 170 ILLFGPPGTGKSYLAKAV---ATEANNSTFFsISSSDLVSKW-LGESE-KLVKNLFQLARenkPSIIFIDEI 236
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALgyaACRQGYRVRF-TTAADLVEQLaQARADgRLGRLLRRLAR---YDLLIIDEL 160
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 128-298 1.46e-126

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: 363.41  E-value: 1.46e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 128 RPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSK 207
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEAN-STFFSVSSSDLVSK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 208 WLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSA 287
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 164698506 288 IRRRFEKRIYI 298
Cdd:cd19521  160 IRRRFEKRIYI 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 136-298 4.97e-95

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: 283.09  E-value: 4.97e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 136 VAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKL 215
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESG-STFFSISASSLVSKWVGESEKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 216 VKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGV-GVDNDGILVLGATNIPWVLDSAIRRRFEK 294
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRFEK 159


                 ....
gi 164698506 295 RIYI 298
Cdd:cd19509  160 RIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 50-355 3.91e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 271.49  E-value: 3.91e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  50 QGDKAKQSIRAKCTEYLDRAEKLKEYLKKKEKKPQKPVKEEQSGPVDEKGNDSDGEAESDDPEKKklqnqlqGAIVIERP 129
Cdd:COG1222    1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRG-------TAVPAESP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 130 NVKWSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSK 207
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELG-APFIRVRGSELVSK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 208 WLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSEN-ESEAARRIKTEFLVQMQGVGvDNDGILVLGATNIPWVLDS 286
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFE-SRGDVLIIAATNRPDLLDP 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164698506 287 AIRR--RFEKRIYIPLPEAHARAAMFRLHLGStQNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRK 355
Cdd:COG1222  231 ALLRpgRFDRVIEVPLPDEEAREEILKIHLRD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE 300
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 133-354 4.73e-75

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: 240.20  E-value: 4.73e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 133 WSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLG 210
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELG-LPLIEVDLSDLVSKYVG 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 211 ESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVgvdNDGILVLGATNIPWVLDSAIRR 290
Cdd:COG0464  234 ETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALLR 310

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506 291 RFEKRIYIPLPEAHARAAMFRLHLGSTQNSlTEADFQELGRKTDGYSGADISIIVRDALMQPVR 354
Cdd:COG0464  311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 135-298 4.12e-74

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: 229.87  E-value: 4.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEAnNSTFFSISSSDLVSKWLGESEK 214
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATEC-GTTFFNVSSSTLTSKYRGESEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 215 LVKNLFQLARENKPSIIFIDEIDSLCGSR-SENESEAARRIKTEFLVQMQGVG--VDNDG----ILVLGATNIPWVLDSA 287
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGgaSENDDpskmVMVLAATNFPWDIDEA 159

                        170
                 ....*....|.
gi 164698506 288 IRRRFEKRIYI 298
Cdd:cd19522  160 LRRRLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 120-298 1.77e-73

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: 228.72  E-value: 1.77e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 120 LQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSI 199
Cdd:cd19525    8 IMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG-ATFFSI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 200 SSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGV-DNDGILVLGAT 278
Cdd:cd19525   87 SASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTsSEDRILVVGAT 166

                        170       180
                 ....*....|....*....|
gi 164698506 279 NIPWVLDSAIRRRFEKRIYI 298
Cdd:cd19525  167 NRPQEIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 135-298 1.30e-70

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: 220.49  E-value: 1.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEK 214
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN-ATFFNISAASLTSKYVGEGEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 215 LVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGV-GVDNDGILVLGATNIPWVLDSAIRRRFE 293
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVqSNGDDRVLVMGATNRPQELDDAVLRRFT 159


                 ....*
gi 164698506 294 KRIYI 298
Cdd:cd19524  160 KRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 124-442 2.33e-67

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: 228.25  E-value: 2.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  124 IVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISS 201
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESG-ANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  202 SDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAAR-RIKTEFLVQMQGVgVDNDGILVLGATNI 280
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTdRIVNQLLTEMDGI-QELSNVVVIAATNR 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  281 PWVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHLGSTqNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRKVQS 358
Cdd:TIGR01243 600 PDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSM-PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIG 678

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  359 ATHFKKVRGPSRAdpncIVNDLltpcspgdpgaiemtwmdvpgdkllepVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTE 438
Cdd:TIGR01243 679 SPAKEKLEVGEEE----FLKDL---------------------------KVEMRHFLEALKKVKPSVSKEDMLRYERLAK 727


                  ....
gi 164698506  439 DFGQ 442
Cdd:TIGR01243 728 ELKR 731
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 125-355 6.50e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 210.84  E-value: 6.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 125 VIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFtgKR---TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISS 201
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF--EEvgiEPPKGVLLYGPPGTGKTLLAKAVAHETN-ATFIRVVG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 202 SDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAAR---RIKTEFLVQMQgvGVDNDG-ILVLGA 277
Cdd:PRK03992 199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMD--GFDPRGnVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 278 TNIPWVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHlgsTQN-SLTEA-DFQELGRKTDGYSGADISIIVRDALMQPV 353
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIH---TRKmNLADDvDLEELAELTEGASGADLKAICTEAGMFAI 353


                 ..
gi 164698506 354 RK 355
Cdd:PRK03992 354 RD 355
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 135-298 9.77e-58

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: 187.25  E-value: 9.77e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFTGKR--TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGES 212
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAG-ARFINLQVSSLTDKWYGES 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 213 EKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVD-NDGILVLGATNIPWVLDSAIRRR 291
Cdd:cd19520   80 QKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAILRR 159


                 ....*..
gi 164698506 292 FEKRIYI 298
Cdd:cd19520  160 MPKRFHI 166
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 170-300 4.59e-57

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: 184.33  E-value: 4.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  170 ILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESE 249
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164698506  250 AARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPL 300
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 142-298 1.04e-55

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: 181.71  E-value: 1.04e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 142 AKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKLVKNL 219
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAG-LNFISVKGPELFSKYVGESERAVREI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 220 FQLARENKPSIIFIDEIDSLCGSRS-ENESEAARRIKTEFLVQMQGVGVdNDGILVLGATNIPWVLDSAIRR--RFEKRI 296
Cdd:cd19511   79 FQKARQAAPCIIFFDEIDSLAPRRGqSDSSGVTDRVVSQLLTELDGIES-LKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                 ..
gi 164698506 297 YI 298
Cdd:cd19511  158 YV 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 113-370 1.37e-53

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: 186.34  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  113 KKKLQNQlqgaiviERPNVKWSDVAGLEGAKEALKEAVILpIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATE 190
Cdd:TIGR01241  41 KAKLLNE-------EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  191 ANNStFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDS--------LCGSRSENEseaarRIKTEFLVQM 262
Cdd:TIGR01241 112 AGVP-FFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAvgrqrgagLGGGNDERE-----QTLNQLLVEM 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  263 QGVGvDNDGILVLGATNIPWVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHLGSTQNSlTEADFQELGRKTDGYSGAD 340
Cdd:TIGR01241 186 DGFG-TNTGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLA-PDVDLKAVARRTPGFSGAD 263

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 164698506  341 ISIIVRDALMQPVRKVQSA---THFKKVR-----GPSR 370
Cdd:TIGR01241 264 LANLLNEAALLAARKNKTEitmNDIEEAIdrviaGPEK 301
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 135-298 4.53e-53

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: 175.17  E-value: 4.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGES 212
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAG-ANFLSISGPSIVSKYLGES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 213 EKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNdGILVLGATNIPWVLDSAIRR-- 290
Cdd:cd19503   79 EKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG-KVVVIAATNRPDAIDPALRRpg 157


                 ....*...
gi 164698506 291 RFEKRIYI 298
Cdd:cd19503  158 RFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 129-356 4.37e-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: 186.65  E-value: 4.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  129 PNVKWSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVS 206
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAG-AYFISINGPEIMS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  207 KWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGvDNDGILVLGATNIPWVLDS 286
Cdd:TIGR01243 251 KYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK-GRGRVIVIGATNRPDALDP 329

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506  287 AIRR--RFEKRIYIPLPEAHARAAMFRLHlgsTQNSL--TEADFQELGRKTDGYSGADISIIVRDALMQPVRKV 356
Cdd:TIGR01243 330 ALRRpgRFDREIVIRVPDKRARKEILKVH---TRNMPlaEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRF 400
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 127-355 1.02e-50

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 176.49  E-value: 1.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 127 ERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDL 204
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTT-ATFIRVVGSEF 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 205 VSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAAR---RIKTEFLVQMQGVGVDNDgILVLGATNIP 281
Cdd:PTZ00454 216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN-VKVIMATNRA 294

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698506 282 WVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLhLGSTQNSLTEADFQELGRKTDGYSGADISIIVRDALMQPVRK 355
Cdd:PTZ00454 295 DTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQT-ITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 142-298 5.01e-50

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: 167.07  E-value: 5.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 142 AKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNStFFSISSSDLVSKWLGESEKLVKNLFQ 221
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP-LIVVKLSSLLSKYVGESEKNLRKIFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 222 LARENKPSIIFIDEIDSLCGSRSEN-ESEAARRIKTEFLVQMQGVGVDNdGILVLGATNIPWVLDSAIRR--RFEKRIYI 298
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRS-KVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 131-298 2.24e-47

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: 160.48  E-value: 2.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 131 VKWSDVAGLEGAKEALKEAVILpIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANNStFFSISSSDLVSKW 208
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVP-FFSISGSDFVEMF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 209 LGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENES---EAARRIKTEFLVQMQGVGvDNDGILVLGATNIPWVLD 285
Cdd:cd19501   78 VGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGgghDEREQTLNQLLVEMDGFE-SNTGVIVIAATNRPDVLD 156

                        170
                 ....*....|....*
gi 164698506 286 SAIRR--RFEKRIYI 298
Cdd:cd19501  157 PALLRpgRFDRQVYV 171
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 133-296 2.04e-46

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: 157.88  E-value: 2.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 133 WSDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLG 210
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTD-ATFIRVVGSELVQKYIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 211 ESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAAR---RIKTEFLVQMQGVGVDNDgILVLGATNIPWVLDSA 287
Cdd:cd19502   80 EGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPA 158

                        170
                 ....*....|.
gi 164698506 288 IRR--RFEKRI 296
Cdd:cd19502  159 LLRpgRFDRKI 169
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 135-298 2.58e-46

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: 157.74  E-value: 2.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEAnNSTFFSISSSDLVSKWLGESEK 214
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQL-GATFLRLRGSTLVAKWAGEGEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 215 LVKNLFQLARENKPSIIFIDEIDSLCGSRSENESeAARRIKTEFLVQMQGV-GVDNDGILVLGATNIPWVLDSAIRRRFE 293
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEAS-PVGRLQVELLAQLDGVlGSGEDGVLVVCTTSKPEEIDESLRRYFS 158


                 ....*
gi 164698506 294 KRIYI 298
Cdd:cd19523  159 KRLLV 163
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
133-365 2.99e-46

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 160.05  E-value: 2.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 133 WSDVAGLEGAKEALKEAVI------LPIKFphlftGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVS 206
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKelrrreNLRKF-----GLWPP-RKILFYGPPGTGKTMLAEALAGELK-LPLLTVRLDSLIG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 207 KWLGESEKLVKNLFQLARENkPSIIFIDEIDSLCGSRS-ENESEAARRIKTEFLVQMQGvgvDNDGILVLGATNIPWVLD 285
Cdd:COG1223   74 SYLGETARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGdQNDVGEVKRVVNALLQELDG---LPSGSVVIAATNHPELLD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 286 SAIRRRFEKRIYIPLPEAHARAAMFRLHLGSTQNSLtEADFQELGRKTDGYSGADISIIVRDALMQPV---RKVQSATHF 362
Cdd:COG1223  150 SALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTALKKAIledREKVTKEDL 228


                 ...
gi 164698506 363 KKV 365
Cdd:COG1223  229 EEA 231
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
127-341 1.05e-45

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 166.75  E-value: 1.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 127 ERPNVKWSDVAGLEGAKEALKEAV-ILpiKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEAnNSTFFSISSSD 203
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEA-GVPFFSISGSD 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 204 LV--------SKwlgeseklVKNLFQLARENKPSIIFIDEIDSLCGSRSEN------ESEaarriKT--EFLVQMQGVGV 267
Cdd:COG0465  211 FVemfvgvgaSR--------VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdERE-----QTlnQLLVEMDGFEG 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 268 dNDGILVLGATNIPWVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLH-----LGStqnsltEADFQELGRKTDGYSGAD 340
Cdd:COG0465  278 -NEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHarkkpLAP------DVDLEVIARRTPGFSGAD 350


                 .
gi 164698506 341 I 341
Cdd:COG0465  351 L 351
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 142-298 8.93e-45

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: 153.42  E-value: 8.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 142 AKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKLVKNL 219
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESN-ANFISVKGPELLSKWVGESEKAIREI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 220 FQLARENKPSIIFIDEIDSLCGSR-SENESEAARRIKTEFLVQMQGVGVDNDgILVLGATNIPWVLDSAIRR--RFEKRI 296
Cdd:cd19529   79 FRKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG-VVVIAATNRPDIIDPALLRagRFDRLI 157


                 ..
gi 164698506 297 YI 298
Cdd:cd19529  158 YI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 135-299 1.31e-42

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: 147.97  E-value: 1.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFtgKR---TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGE 211
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELF--KAigiKPPRGILLYGPPGTGKTLIARAVANETG-AFFFLINGPEIMSKLAGE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 212 SEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDgILVLGATNIPWVLDSAIRR- 290
Cdd:cd19519   78 SESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPALRRf 156

                        170
                 ....*....|
gi 164698506 291 -RFEKRIYIP 299
Cdd:cd19519  157 gRFDREIDIG 166
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 129-348 5.50e-41

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 151.46  E-value: 5.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 129 PNVKWSDVAGLEGAKEALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVS 206
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETS-ATFLRVVGSELIQ 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 207 KWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKT---EFLVQMQGVGVDNDgILVLGATNIPWV 283
Cdd:PTZ00361 256 KYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRtmlELLNQLDGFDSRGD-VKVIMATNRIES 334

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698506 284 LDSAIRR--RFEKRIYIPLPEAHARAAMFRLHLgSTQNSLTEADFQELGRKTDGYSGADISIIVRDA 348
Cdd:PTZ00361 335 LDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHT-SKMTLAEDVDLEEFIMAKDELSGADIKAICTEA 400
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 139-298 1.94e-39

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: 139.16  E-value: 1.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 139 LEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKLV 216
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESG-ANFISVKGPELLNKYVGESERAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 217 KNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGvDNDGILVLGATNIPWVLDSAIRR--RFEK 294
Cdd:cd19530   79 RQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE-ERSNVFVIAATNRPDIIDPAMLRpgRLDK 157


                 ....
gi 164698506 295 RIYI 298
Cdd:cd19530  158 TLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 143-298 3.47e-39

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: 138.80  E-value: 3.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 143 KEALKEAVILPIKFPHLFTG-KRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGESEKLVKNLFQ 221
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQ-ANFISVKGPELLTMWFGESEANVRDIFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 222 LARENKPSIIFIDEIDSLCGSRSEN---ESEAARRIKTEFLVQMQGVGVDNDgILVLGATNIPWVLDSAIRR--RFEKRI 296
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGMNTKKN-VFIIGATNRPDIIDPAILRpgRLDQLI 159


                 ..
gi 164698506 297 YI 298
Cdd:cd19528  160 YI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 135-297 2.82e-38

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: 136.49  E-value: 2.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLFTG-KRTPWRGILLFGPPGTGKSYLAKAVATEA----NNSTFFSISSSDLVSKWL 209
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECskggQKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 210 GESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQgvGVDNDG-ILVLGATNIPWVLDSAI 288
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMD--GLDNRGqVVVIGATNRPDALDPAL 158

                        170
                 ....*....|.
gi 164698506 289 RR--RFEKRIY 297
Cdd:cd19517  159 RRpgRFDREFY 169
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
133-366 1.34e-37

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 144.79  E-value: 1.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 133 WSDVAGLEGAKEALKEAVIL---PIKFPHLftGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWL 209
Cdd:PRK10733 151 FADVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAK-VPFFTISGSDFVEMFV 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 210 GESEKLVKNLFQLARENKPSIIFIDEIDS--------LCGSRSENEseaarRIKTEFLVQMQGVGvDNDGILVLGATNIP 281
Cdd:PRK10733 227 GVGASRVRDMFEQAKKAAPCIIFIDEIDAvgrqrgagLGGGHDERE-----QTLNQMLVEMDGFE-GNEGIIVIAATNRP 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 282 WVLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHLGSTQNSlTEADFQELGRKTDGYSGADISIIVRDALMQPVR---KV 356
Cdd:PRK10733 301 DVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNEAALFAARgnkRV 379

                        250
                 ....*....|
gi 164698506 357 QSATHFKKVR 366
Cdd:PRK10733 380 VSMVEFEKAK 389
ftsH CHL00176
cell division protein; Validated
 131-355 1.62e-37

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 144.42  E-value: 1.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 131 VKWSDVAGLEGAKEALKEAVILpIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKW 208
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEAE-VPFFSISGSEFVEMF 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 209 LGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSEN------ESEaarRIKTEFLVQMQGVGvDNDGILVLGATNIPW 282
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGigggndERE---QTLNQLLTEMDGFK-GNKGVIVIAATNRVD 332

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698506 283 VLDSAIRR--RFEKRIYIPLPEAHARAAMFRLHLG----STQNSLTeadfqELGRKTDGYSGADISIIVRDALMQPVRK 355
Cdd:CHL00176 333 ILDAALLRpgRFDRQITVSLPDREGRLDILKVHARnkklSPDVSLE-----LIARRTPGFSGADLANLLNEAAILTARR 406
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 135-296 1.85e-37

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: 134.45  E-value: 1.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGES 212
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELK-VPFLKISATEIVSGVSGES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 213 EKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDND---GILVLGATNIPWVLDSAIR 289
Cdd:cd19518   79 EEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTaggPVLVIGATNRPDSLDPALR 158


                 ....*....
gi 164698506 290 R--RFEKRI 296
Cdd:cd19518  159 RagRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 142-297 7.17e-37

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: 132.55  E-value: 7.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 142 AKEALKEAVILPIKFPHLFTGKRTPWR-GILLFGPPGTGKSYLAKAVATEANNStFFSISSSDLVSKWLGESEKLVKNLF 220
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLN-FISVKGPELLNKYIGASEQNVRDLF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698506 221 QLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVdNDGILVLGATNIPWVLDSAIRR--RFEKRIY 297
Cdd:cd19526   80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEG-LDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 143-298 1.22e-36

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: 131.87  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 143 KEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEAnNSTFFSISSSDLVSKWLGESEKLVKNLFQL 222
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATEC-SLNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 223 ARENKPSIIFIDEIDSLCGSR--SENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRR--RFEKRIYI 298
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLLYL 160
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 381-441 1.23e-35

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 125.69  E-value: 1.23e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164698506  381 LTPCSPGDPGAIEMTWMDVPGDKLLEPVVSMWDMLRSLSSTKPTVNEQDLLKLKKFTEDFG 441
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-69 2.34e-31

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 114.67  E-value: 2.34e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506   7 NLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGdKAKQSIRAKCTEYLDRA 69
Cdd:cd02678    2 FLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRA 63
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 137-300 6.64e-29

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: 110.70  E-value: 6.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 137 AGLEGAKEALKEAVilpikfphlftgKRTPWRGILLFGPPGTGKSYLAKAVATEA--NNSTFFSISSSDLVSKWLGESEK 214
Cdd:cd00009    1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 215 ---LVKNLFQLARENKPSIIFIDEIDSLcgsrseneSEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWV--LDSAIR 289
Cdd:cd00009   69 ghfLVRLLFELAEKAKPGVLFIDEIDSL--------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLgdLDRALY 140

                        170
                 ....*....|.
gi 164698506 290 RRFEKRIYIPL 300
Cdd:cd00009  141 DRLDIRIVIPL 151
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 8-69 5.41e-23

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 91.83  E-value: 5.41e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506    8 LQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKyEAQGDKAKQSIRAKCTEYLDRA 69
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALK-ETKNEERRELLRAKIAEYLERA 61
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 166-302 4.31e-21

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: 89.35  E-value: 4.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506   166 PWRGILLFGPPGTGKSYLAKAVATEAN--NSTFFSISSSDL--------------VSKWLGESEKLVKNLFQLARENKPS 229
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506   230 IIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGvgvdndGILVLGATNIPWVLDSA-IRRRFEKRIYIPLPE 302
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 7-69 2.45e-20

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 84.67  E-value: 2.45e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506   7 NLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQgDKAKQSIRAKCTEYLDRA 69
Cdd:cd02656    2 LLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKE-PKLRKLLRKKVKEYLDRA 63
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 168-298 1.76e-19

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: 85.62  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPS--------IIFIDEIDSL 239
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506 240 CGSR--SENESEAARRIKTEFLVQMQGVGVDNDgILVLGATNIPWVLDSAIRR--RFEKRIYI 298
Cdd:cd19504  116 CKQRgsMAGSTGVHDTVVNQLLSKIDGVEQLNN-ILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
6-69 3.27e-19

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 81.59  E-value: 3.27e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506     6 TNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEaQGDKAKQSIRAKCTEYLDRA 69
Cdd:smart00745   3 DYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVE-SDSKRREALKAKAAEYLDRA 65
ycf46 CHL00195
Ycf46; Provisional
 112-344 8.43e-18

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 85.46  E-value: 8.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 112 EKKKLQNQLQgaiVIE--RPNVKWSDVAGLEGAKEALKeavilpiKFPHLFT------GKRTPwRGILLFGPPGTGKSYL 183
Cdd:CHL00195 207 EKKQIISQTE---ILEfySVNEKISDIGGLDNLKDWLK-------KRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLT 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 184 AKAVATEAN--------NSTFFSIsssdlvskwLGESEKLVKNLFQLARENKPSIIFIDEID-SLCGSRSENESEAARRI 254
Cdd:CHL00195 276 AKAIANDWQlpllrldvGKLFGGI---------VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRV 346

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 255 KTEFLV----QMQGVGVdndgilVLGATNIPWVLDSAIRR-RFEKRIYIPLPEAHARAAMFRLHLGSTQ-NSLTEADFQE 328
Cdd:CHL00195 347 LATFITwlseKKSPVFV------VATANNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKFRpKSWKKYDIKK 420

                        250
                 ....*....|....*...
gi 164698506 329 LGRKTDGYSGADI--SII 344
Cdd:CHL00195 421 LSKLSNKFSGAEIeqSII 438
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 135-263 4.87e-16

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: 75.10  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKE---AVILPIKFPHLftgkrTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSISSSDLVSKWLGE 211
Cdd:cd19507    1 DVGGLDNLKDWLKKrkaAFSKQASAYGL-----PTPKGLLLVGIQGTGKSLTAKAIAGVWQ-LPLLRLDMGRLFGGLVGE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164698506 212 SEKLVKNLFQLARENKPSIIFIDEIDS-LCGSRSENESEAARRIKTEFLVQMQ 263
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEKgFSNADSKGDSGTSSRVLGTFLTWLQ 127
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 168-298 1.47e-14

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: 72.09  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATEAN--------NSTFFSISSSDLVSKWLGESEKLVKNLFQLARE---NKPSIIF--ID 234
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSirlssryrYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQElidDKDALVFvlID 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698506 235 EIDSLCGSR----SENESEAARRIKTEFLVQMQGVGvDNDGILVLGATNIPWVLDSAIRRRFEKRIYI 298
Cdd:cd19508  133 EVESLAAARsassSGTEPSDAIRVVNAVLTQIDRIK-RYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 164-296 2.06e-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: 61.77  E-value: 2.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 164 RTPWRGILLFGPPGTGKSYLAKAVATEANNStfFSISSSDLVSKWLGESEKLVKNLFQLA-RENKPSIIFIDEIDS-LCG 241
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMD--YAIMTGGDVAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAfLRK 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164698506 242 SRSENESEAARRIKTEFLVQMqgvGVDNDGILVLGATNIPWVLDSAIRRRFEKRI 296
Cdd:cd19512   97 RSTEKISEDLRAALNAFLYRT---GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 166-288 2.12e-11

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: 62.01  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 166 PWRGILLFGPPGTGKSYLAKAVATEA--------------NNSTFFSISSSDLVSKWlGESEKLVKNLFQLARENKPSII 231
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLIL-KESLHRLNLQFELAKAMSPCII 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 232 FIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDND---GILVLGATNIPWVLDSAI 288
Cdd:cd19505   90 WIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSstrNILVIASTHIPQKVDPAL 149
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-69 5.59e-11

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239147  Cd Length: 75  Bit Score: 58.29  E-value: 5.59e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506   7 NLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKaKQSIRAKCTEYLDRA 69
Cdd:cd02684    2 SLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQR-KEALRQKVLQYVSRA 63
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 168-298 9.09e-09

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: 54.46  E-value: 9.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATEAnNSTFFSISSSDLVSKWLGES--EKLVKNLFQLARENKPSIIFIDEIDSLCGSRSE 245
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTET-GANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVP 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 164698506 246 NESEA--ARRIKTEFLVQMQGVGVDnDGILVLGATNIPWVLD-SAIRRRFEKRIYI 298
Cdd:cd19506  106 KTEKQldPKRLKKDLPKILKSLKPE-DRVLIVGTTSRPFEADlKSFCKVYNKIILI 160
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 146-298 2.17e-08

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: 53.12  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 146 LKEAVILPIKFPHLFTGKRTPW-RGILLFGPPGTGKSYLAKAVATEANNSTF-FSISSSDLvskwlgeSEKLVKNLfqLA 223
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYrRGYLLYGPPGTGKSSFIAALAGELDYDICdLNLSEVVL-------TDDRLNHL--LN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 224 RENKPSIIFIDEIDSLCGSRSENESEaarRIKTEFLVQMQGVGVDN--DGI------LVLGATNIPWVLDSAIRR--RFE 293
Cdd:cd19510   72 TAPKQSIILLEDIDAAFESREHNKKN---PSAYGGLSRVTFSGLLNalDGVasseerIVFMTTNHIERLDPALIRpgRVD 148


                 ....*
gi 164698506 294 KRIYI 298
Cdd:cd19510  149 MKIYM 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 325-366 6.83e-08

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: 48.69  E-value: 6.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164698506  325 DFQELGRKTDGYSGADISIIVRDALMQPVRKVQSATHFKKVR 366
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 169-292 2.82e-07

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: 49.60  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  169 GILLFGPPGTGKSYLAKAVATEANNSTFFSI------SSSDLVSKWL---GESEKLVKNLFQLAREnkPSIIFIDEIDSL 239
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVqltrdtTEEDLFGRRNidpGGASWVDGPLVRAARE--GEIAVLDEINRA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698506  240 cgsrsenESEAARRIKTEF----LVQMQG---VGVDNDGILVLGATNIP----WVLDSAIRRRF 292
Cdd:pfam07728  79 -------NPDVLNSLLSLLderrLLLPDGgelVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 170-236 1.26e-06

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: 49.39  E-value: 1.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506 170 ILLFGPPGTGKSYLAKAV---ATEANNSTFFsISSSDLVSKW-LGESE-KLVKNLFQLARenkPSIIFIDEI 236
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALgyaACRQGYRVRF-TTAADLVEQLaQARADgRLGRLLRRLAR---YDLLIIDEL 160
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 8-69 2.65e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 45.03  E-value: 2.65e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506   8 LQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEaqGDKAKQSI-RAKCTEYLDRA 69
Cdd:cd02677    3 LEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGD--SSPERREAvKRKIAEYLKRA 63
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 138-219 3.07e-06

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 48.84  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  138 GLEGAKEALKEA-VILpikfpHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNST-FFSISSSDLVSKWLGESEKL 215
Cdd:pfam06068  25 GLVGQEKAREAAgVIV-----EMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTpFTSISGSEVYSLEMKKTEAL 99


                  ....
gi 164698506  216 VKNL 219
Cdd:pfam06068 100 TQAF 103
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 170-236 3.69e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.93  E-value: 3.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506 170 ILLFGPPGTGKSYLAKAVATEAnNSTFFSISSS-----DLvskwlgesEKLVKNLFQLARENKPSIIFIDEI 236
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGAT-DAPFEALSAVtsgvkDL--------REVIEEARQRRSAGRRTILFIDEI 101
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 8-69 7.23e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239146  Cd Length: 77  Bit Score: 43.95  E-value: 7.23e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506   8 LQKAIDLaskaaqeDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKaKQSIRAKCTEYLDRA 69
Cdd:cd02683   10 LKRAVEL-------DQEGRFQEALVCYQEGIDLLMQVLKGTKDEAK-KKNLRQKISEYMDRA 63
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 170-236 1.12e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 47.36  E-value: 1.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506 170 ILLFGPPGTGKSYLAKAVATEAnNSTFFSIS--SSdlvskwlGESEklVKNLFQLAREN----KPSIIFIDEI 236
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANAT-DAEFVALSavTS-------GVKD--IREVIEEARERraygRRTILFVDEI 114
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 170-342 1.32e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.46  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 170 ILLFGPPGTGKSYLAKAVA---TEANNSTFFSI------SSSDLVskwLGESEKLVKNLFQL-----------AREN--K 227
Cdd:COG1401  224 VILAGPPGTGKTYLARRLAealGGEDNGRIEFVqfhpswSYEDFL---LGYRPSLDEGKYEPtpgiflrfclkAEKNpdK 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 228 PSIIFIDEIdslcgSRSENE---SEA-----ARRIKTEFLVQMQGVGVDN-----DGILVLGA-----TNIPwVLDSAIR 289
Cdd:COG1401  301 PYVLIIDEI-----NRANVEkyfGELlslleSDKRGEELSIELPYSGEGEefsipPNLYIIGTmntddRSLA-LSDKALR 374

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164698506 290 RRFEKrIYIPLPEAHARAAMFRLHLGSTQNSLTEADFQELGRKTDGYSGADIS 342
Cdd:COG1401  375 RRFTF-EFLDPDLDKLSNEEVVDLLEELNEILEKRDFQIGHRALLLLDGLLSG 426
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
168-236 1.85e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.93  E-value: 1.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATEA---NNSTFFsISSSDLVSKWL-----GESEKLVKnlfQLArenKPSIIFIDEI 236
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRF-TTAPDLVNELKearadGRLERLLK---RLA---KVDLLILDEL 169
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 168-299 2.08e-05

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: 46.76  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  168 RGILLFGPPGTGKSYLAKAVA------TEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLAREnkpSIIFIDEIDSLCG 241
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVE 389

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506  242 SRSENESEAARRIKTEFLVQMQGvgvDNDGILVLGA---TNIPWVLDS--AIRRRFEKRIYIP 299
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMEN---DRDRLVVIGAgyrKDLDKFLEVneGLRSRFTRVIEFP 449
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
168-215 3.59e-05

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 45.73  E-value: 3.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATEANNST-FFSISSSDLVSKWLGESEKL 215
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEDTpFVAISGSEIYSAELKKTEFL 113
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 170-237 4.86e-05

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: 43.72  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  170 ILLFGPPGTGKSYLAKAVATEANNS--TFFSISSSDL-----VSKWLGESEKLVK-----NLFQLARENKPSIIFIDEID 237
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGDerALIRIDMSEYmeehsVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
ycf2 CHL00206
Ycf2; Provisional
 165-268 6.93e-05

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 45.67  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  165 TPWRGILLFGPPGTGKSYLAKAVATeanNSTFFSIsssdlvskwlgeseKLVKNLFQlarENKPSIIFIDEIDSLCGSRS 244
Cdd:CHL00206 1628 SPSRGILVIGSIGTGRSYLVKYLAT---NSYVPFI--------------TVFLNKFL---DNKPKGFLIDDIDIDDSDDI 1687

                          90       100
                  ....*....|....*....|....
gi 164698506  245 ENESEAARRIKTEFLVQMQGVGVD 268
Cdd:CHL00206 1688 DDSDDIDRDLDTELLTMMNALTMD 1711
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
170-239 7.74e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.35  E-value: 7.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698506 170 ILLFGPPGTGKSYLAKAVATEANNStfFSISS-------SDLVSkwlgesekLVKNLfqlaRENkpSIIFIDEIDSL 239
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN--IRITSgpalekpGDLAA--------ILTNL----EEG--DVLFIDEIHRL 114
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 170-259 8.40e-05

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: 42.11  E-value: 8.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 170 ILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLvskwlgesEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESE 249
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDRSS 72

                         90
                 ....*....|
gi 164698506 250 AARRIKTEFL 259
Cdd:cd01120   73 ELLEDLAKLL 82
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
170-236 9.87e-05

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 44.55  E-value: 9.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698506 170 ILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLarENKPSIIFIDEI 236
Cdd:COG1373   23 VVITGPRQVGKTTLLKQLAKELENILYINLDDPRLRALAEEDPDDLLEALKEL--YPGKTYLFLDEI 87
clpC CHL00095
Clp protease ATP binding subunit
 168-298 2.43e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 43.51  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLV-----------SKWLGESEKLVKNLFQLARENKPSIIFIDEI 236
Cdd:CHL00095 201 NNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVitldiglllagTKYRGEFEERLKRIFDEIQENNNIILVIDEV 280

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698506 237 DSLCG-SRSENESEAARRIKTE-FLVQMQgvgvdndgilVLGATNIPWV-----LDSAIRRRFEKrIYI 298
Cdd:CHL00095 281 HTLIGaGAAEGAIDAANILKPAlARGELQ----------CIGATTLDEYrkhieKDPALERRFQP-VYV 338
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 170-236 3.34e-04

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 42.05  E-value: 3.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698506  170 ILLFGPPGTGKSYLAKAVATEA---NNSTFFsISSSDLVSKWLGESE--KLVKNLFQLARenkPSIIFIDEI 236
Cdd:pfam01695  95 VVLLGPPGVGKTHLAIALGVEAcraGYSVRF-TSAADLVNQLKRAHGdgKLTRKLQQLLK---PDVLILDEW 162
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 135-250 3.75e-04

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: 41.39  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 135 DVAGLEGAKEALKEavilpikfpHLFTGKRTP-WRG-ILLF-GPPGTGKSYLAKAVAtEANNSTFFSISssdlvskwLG- 210
Cdd:cd19500   11 DHYGLEDVKERILE---------YLAVRKLKGsMKGpILCLvGPPGVGKTSLGKSIA-RALGRKFVRIS--------LGg 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164698506 211 ---ESE--------------KLVKNLFQlARENKPsIIFIDEIDSLCGSRSENESEA 250
Cdd:cd19500   73 vrdEAEirghrrtyvgampgRIIQALKK-AGTNNP-VFLLDEIDKIGSSFRGDPASA 127
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 171-294 7.36e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.13  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 171 LLFGPPGTGKSYLAKAVA---TEAN------NSTFFSISSSDLV--SKWLGESEKLVKNLFQLARENKPSIIFIDEIDSL 239
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAwriVQGDvpevmaDCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698506 240 --CGSRSENESEAARRIKTEflvqmqgvgVDNDGILVLGAT------NIpWVLDSAIRRRFEK 294
Cdd:PRK11034 291 igAGAASGGQVDAANLIKPL---------LSSGKIRVIGSTtyqefsNI-FEKDRALARRFQK 343
PRK08116 PRK08116
hypothetical protein; Validated
 168-190 9.63e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.77  E-value: 9.63e-04
                         10        20
                 ....*....|....*....|...
gi 164698506 168 RGILLFGPPGTGKSYLAKAVATE 190
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANE 137
AAA_18 pfam13238
AAA domain;
170-255 9.68e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 38.95  E-value: 9.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  170 ILLFGPPGTGKSYLAKAVATEANNSTFFS--ISSSDLVSKWLGES-----------EKLVKNLFQLARENKPSIIFIDEI 236
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRdlALENGLVLGDDPETreskrldedklDRLLDLLEENAALEEGGNLIIDGH 80

                          90
                  ....*....|....*....
gi 164698506  237 dslcgsRSENESEAARRIK 255
Cdd:pfam13238  81 ------LAELEPERAKDLV 93
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 133-189 1.03e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.21  E-value: 1.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506  133 WSDVAGLEGAKEALKEAVIlpikfphlftgkrtpwrG---ILLFGPPGTGKSYLAKAVAT 189
Cdd:pfam01078   2 LADVKGQEQAKRALEIAAA-----------------GghnLLMIGPPGSGKTMLAKRLPG 44
PRK08181 PRK08181
transposase; Validated
 170-207 3.36e-03

transposase; Validated


Pssm-ID: 136670 [Multi-domain]  Cd Length: 269  Bit Score: 39.14  E-value: 3.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 164698506 170 ILLFGPPGTGKSYLAKAVA---TEANNSTFFSiSSSDLVSK 207
Cdd:PRK08181 109 LLLFGPPGGGKSHLAAAIGlalIENGWRVLFT-RTTDLVQK 148
MIT_calpain7_1 cd02681
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 11-69 4.23e-03

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.


Pssm-ID: 239144  Cd Length: 76  Bit Score: 36.03  E-value: 4.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 164698506  11 AIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRA 69
Cdd:cd02681    6 AVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGTLNDSHLKTIQEKSNEYLDRA 64
PRK04195 PRK04195
replication factor C large subunit; Provisional
 134-192 6.03e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 38.75  E-value: 6.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 164698506 134 SDVAGLEGAKEALKEAVIlpiKFPHlftgkRTPWRGILLFGPPGTGKSYLAKAVATEAN 192
Cdd:PRK04195  14 SDVVGNEKAKEQLREWIE---SWLK-----GKPKKALLLYGPPGVGKTSLAHALANDYG 64
PRK09183 PRK09183
transposase/IS protein; Provisional
 170-245 6.29e-03

transposase/IS protein; Provisional


Pssm-ID: 181681  Cd Length: 259  Bit Score: 38.15  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698506 170 ILLFGPPGTGKSYLAKAV---ATEANNSTFFsISSSDLVSKW-LGESEKLVKNLFQLAReNKPSIIFIDEIDSLCGSRSE 245
Cdd:PRK09183 105 IVLLGPSGVGKTHLAIALgyeAVRAGIKVRF-TTAADLLLQLsTAQRQGRYKTTLQRGV-MAPRLLIIDEIGYLPFSQEE 182
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
132-188 7.10e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 38.25  E-value: 7.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 164698506 132 KWSDVAGLEGAKEALKEAVILPiKFPH--LFTGkrtpwrgillfgPPGTGKSYLAKAVA 188
Cdd:COG2812    8 TFDDVVGQEHVVRTLKNALASG-RLAHayLFTG------------PRGVGKTTLARILA 53
PRK13341 PRK13341
AAA family ATPase;
171-236 9.02e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 38.50  E-value: 9.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698506 171 LLFGPPGTGKSYLAKAVATEAnNSTFFSISSSDLVSKWLGESEKLVKNlfQLARENKPSIIFIDEI 236
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHT-RAHFSSLNAVLAGVKDLRAEVDRAKE--RLERHGKRTILFIDEV 118
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 170-190 9.80e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 35.66  E-value: 9.80e-03
                          10        20
                  ....*....|....*....|.
gi 164698506  170 ILLFGPPGTGKSYLAKAVATE 190
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
 
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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