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Conserved domains on  [gi|665407420|ref|NP_001285800|]
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no mitochondrial derivative, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 18-183 9.06e-116

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: 329.77  E-value: 9.06e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRM 177
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 665407420 178 PAQFHI 183
Cdd:cd19520  161 PKRFHI 166
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 207-243 5.30e-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: 48.30  E-value: 5.30e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 665407420  207 DVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLITS 243
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
 
Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 18-183 9.06e-116

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: 329.77  E-value: 9.06e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRM 177
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 665407420 178 PAQFHI 183
Cdd:cd19520  161 PKRFHI 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 13-276 2.20e-81

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 248.38  E-value: 2.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  13 TVSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKW 92
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  93 YGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSR-NMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDK 171
Cdd:COG1222  153 IGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDP 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 172 AIVRrmPAQF----HIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNAsvyRMRQLITSRDps 247
Cdd:COG1222  231 ALLR--PGRFdrviEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEA---GMFAIREGRD-- 303

                        250       260
                 ....*....|....*....|....*....
gi 665407420 248 ataldrnnvRITMDDLLGSHLKIKESKMH 276
Cdd:COG1222  304 ---------TVTMEDLEKAIEKVKKKTET 323
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 14-275 1.91e-58

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: 198.59  E-value: 1.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGI-EPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLstNANSTVIVMGATNRPQDLDKAI 173
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGL--KGRGRVIVIGATNRPDALDPAL 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  174 vrRMPAQFH----IGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLIT--SRDPS 247
Cdd:TIGR01243 332 --RRPGRFDreivIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIRegKINFE 409

                         250       260       270
                  ....*....|....*....|....*....|.
gi 665407420  248 ATALDR---NNVRITMDDLLGSHLKIKESKM 275
Cdd:TIGR01243 410 AEEIPAevlKELKVTMKDFMEALKMVEPSAI 440
cell_div_CdvC NF041006
cell division protein CdvC;
14-264 2.87e-57

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 188.02  E-value: 2.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSklWqaPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFPLG--W--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  94 GESQKLTSAVFSLASRI-----EPCIIFIDEIDSFLRSRNmNDHEATAMMKTQFMMLWDGL-STNANSTVIVMGATNRPQ 167
Cdd:NF041006 176 GEAEKNVAKIFKKAREKskeegKPAIIFIDEIDALLGVYS-SEVGGEVRVRNQFLKEMDGLqDKSENYHVYVIGATNKPW 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 168 DLDKAIVRRMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLITSRDPS 247
Cdd:NF041006 255 RLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGE 334

                        250
                 ....*....|....*..
gi 665407420 248 ATAldrnnvrITMDDLL 264
Cdd:NF041006 335 PRP-------ITMEDFK 344
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 14-274 1.84e-56

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 186.19  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:PRK03992 128 VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNmndHEATA--------MMktQFMMLWDGLSTNANstVIVMGATNR 165
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT---DSGTSgdrevqrtLM--QLLAEMDGFDPRGN--VKIIAATNR 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 166 PQDLDKAIVRrmPAQF----HIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQli 241
Cdd:PRK03992 280 IDILDPAILR--PGRFdriiEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD-- 355

                        250       260       270
                 ....*....|....*....|....*....|...
gi 665407420 242 tsrdpsatalDRNnvRITMDDLLGSHLKIKESK 274
Cdd:PRK03992 356 ----------DRT--EVTMEDFLKAIEKVMGKE 376
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 55-185 6.52e-45

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: 148.51  E-value: 6.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   55 VLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEA 134
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665407420  135 TAMMKTQFMMLWDGLsTNANSTVIVMGATNRPQDLDKAIVRRMPAQFHIGL 185
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 52-186 2.43e-13

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: 66.24  E-value: 2.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420    52 PKGVLLHGPPGCGKTLIAKATAKEA-----GMRFINLD------------VAILTDKWYGESQKLTSAVFSLASRIEPCI 114
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppggGVIYIDGEdileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665407420   115 IFIDEIDSFLRSRnmndheaTAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRMpAQFHIGLP 186
Cdd:smart00382  82 LILDEITSLLDAE-------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR-FDRRIVLL 145
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 207-243 5.30e-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: 48.30  E-value: 5.30e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 665407420  207 DVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLITS 243
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
 
Name Accession Description Interval E-value
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 18-183 9.06e-116

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: 329.77  E-value: 9.06e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRM 177
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 665407420 178 PAQFHI 183
Cdd:cd19520  161 PKRFHI 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 13-276 2.20e-81

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 248.38  E-value: 2.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  13 TVSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKW 92
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  93 YGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSR-NMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDK 171
Cdd:COG1222  153 IGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGD--VLIIAATNRPDLLDP 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 172 AIVRrmPAQF----HIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNAsvyRMRQLITSRDps 247
Cdd:COG1222  231 ALLR--PGRFdrviEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEA---GMFAIREGRD-- 303

                        250       260
                 ....*....|....*....|....*....
gi 665407420 248 ataldrnnvRITMDDLLGSHLKIKESKMH 276
Cdd:COG1222  304 ---------TVTMEDLEKAIEKVKKKTET 323
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 19-183 5.49e-72

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: 218.76  E-value: 5.49e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  19 IAGLDSVIQELRESVVLPIQHKDLFKHSKLWqaPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQK 98
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGP--PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  99 LTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRMP 178
Cdd:cd19509   79 IVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFE 158


                 ....*
gi 665407420 179 AQFHI 183
Cdd:cd19509  159 KRIYI 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 16-264 2.12e-70

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: 222.48  E-value: 2.12e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  16 WADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGE 95
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYGL-PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  96 SQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNanstVIVMGATNRPQDLDKAIVR 175
Cdd:COG0464  235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD----VVVIAATNRPDLLDPALLR 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 176 RMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNAsvyrMRQlitsrdpsatALDRNN 255
Cdd:COG0464  311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRA----ALQ----------ALRLGR 376


                 ....*....
gi 665407420 256 VRITMDDLL 264
Cdd:COG0464  377 EPVTTEDLL 385
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 14-275 1.91e-58

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: 198.59  E-value: 1.91e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGI-EPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLstNANSTVIVMGATNRPQDLDKAI 173
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGL--KGRGRVIVIGATNRPDALDPAL 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  174 vrRMPAQFH----IGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLIT--SRDPS 247
Cdd:TIGR01243 332 --RRPGRFDreivIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIRegKINFE 409

                         250       260       270
                  ....*....|....*....|....*....|.
gi 665407420  248 ATALDR---NNVRITMDDLLGSHLKIKESKM 275
Cdd:TIGR01243 410 AEEIPAevlKELKVTMKDFMEALKMVEPSAI 440
cell_div_CdvC NF041006
cell division protein CdvC;
14-264 2.87e-57

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 188.02  E-value: 2.87e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSklWqaPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYPSKRPDLFPLG--W--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  94 GESQKLTSAVFSLASRI-----EPCIIFIDEIDSFLRSRNmNDHEATAMMKTQFMMLWDGL-STNANSTVIVMGATNRPQ 167
Cdd:NF041006 176 GEAEKNVAKIFKKAREKskeegKPAIIFIDEIDALLGVYS-SEVGGEVRVRNQFLKEMDGLqDKSENYHVYVIGATNKPW 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 168 DLDKAIVRRMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLITSRDPS 247
Cdd:NF041006 255 RLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEKGLGE 334

                        250
                 ....*....|....*..
gi 665407420 248 ATAldrnnvrITMDDLL 264
Cdd:NF041006 335 PRP-------ITMEDFK 344
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 14-273 8.48e-57

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: 194.36  E-value: 8.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGI-RPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEA-TAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKA 172
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSN--VVVIAATNRPDILDPA 606

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  173 IVRrmPAQF----HIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLITSrdPSA 248
Cdd:TIGR01243 607 LLR--PGRFdrliLVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS--PAK 682

                         250       260       270
                  ....*....|....*....|....*....|.
gi 665407420  249 TALD------RNNVRITMDDLLGSHLKIKES 273
Cdd:TIGR01243 683 EKLEvgeeefLKDLKVEMRHFLEALKKVKPS 713
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 14-274 1.84e-56

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 186.19  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:PRK03992 128 VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNmndHEATA--------MMktQFMMLWDGLSTNANstVIVMGATNR 165
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT---DSGTSgdrevqrtLM--QLLAEMDGFDPRGN--VKIIAATNR 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 166 PQDLDKAIVRrmPAQF----HIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQli 241
Cdd:PRK03992 280 IDILDPAILR--PGRFdriiEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD-- 355

                        250       260       270
                 ....*....|....*....|....*....|...
gi 665407420 242 tsrdpsatalDRNnvRITMDDLLGSHLKIKESK 274
Cdd:PRK03992 356 ----------DRT--EVTMEDFLKAIEKVMGKE 376
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 18-183 1.86e-55

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: 176.58  E-value: 1.86e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFkhSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRM 177
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRF 158


                 ....*.
gi 665407420 178 PAQFHI 183
Cdd:cd19524  159 TKRVYV 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 14-183 8.74e-55

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: 175.56  E-value: 8.74e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFkhSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAI 173
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAA 176

                        170
                 ....*....|
gi 665407420 174 VRRMPAQFHI 183
Cdd:cd19525  177 RRRLVKRLYI 186
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 18-181 4.08e-48

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 157.84  E-value: 4.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGL-KPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKAIvrRM 177
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGK--VVVIAATNRPDAIDPAL--RR 155


                 ....
gi 665407420 178 PAQF 181
Cdd:cd19503  156 PGRF 159
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 14-183 9.81e-48

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: 156.95  E-value: 9.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHS-KLWqapKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKW 92
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNrKPW---SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  93 YGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNaNSTVIVMGATNRPQDLDKA 172
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGND-SQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 665407420 173 IVRRMPAQFHI 183
Cdd:cd19521  160 IRRRFEKRIYI 170
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 10-263 3.82e-45

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: 158.99  E-value: 3.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   10 ADITVSWADIAGLDSVIQELRESVvlpiqhkDLFKHSKLWQA-----PKGVLLHGPPGCGKTLIAKATAKEAGMRFINLD 84
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIV-------DFLKNPSKFTKlgakiPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSIS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   85 VAILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNM-----NDH-EATAmmkTQFMMLWDGLSTNANstVI 158
Cdd:TIGR01241 121 GSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglgggNDErEQTL---NQLLVEMDGFGTNTG--VI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  159 VMGATNRPQDLDKAIVR--RMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASvyr 236
Cdd:TIGR01241 196 VIAATNRPDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAA--- 272

                         250       260
                  ....*....|....*....|....*..
gi 665407420  237 mrqLITSRdpsataldRNNVRITMDDL 263
Cdd:TIGR01241 273 ---LLAAR--------KNKTEITMNDI 288
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 55-185 6.52e-45

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: 148.51  E-value: 6.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   55 VLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEA 134
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665407420  135 TAMMKTQFMMLWDGLsTNANSTVIVMGATNRPQDLDKAIVRRMPAQFHIGL 185
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 25-183 1.38e-43

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: 145.89  E-value: 1.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  25 VIQELRESVVLPIQHKDLFKHSKLwqAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVF 104
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLG--LPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 105 SLASRIEPCIIFIDEIDSFLRSR-NMNDHEATAMMKTQFMMLWDGLstNANSTVIVMGATNRPQDLDKAIVRRMPAQFHI 183
Cdd:cd19481   79 ERARRLAPCILFIDEIDAIGRKRdSSGESGELRRVLNQLLTELDGV--NSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 18-183 4.98e-43

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: 145.13  E-value: 4.98e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKH-SKLWqapKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGES 96
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGiRRPW---KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  97 QKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMND-HEATAMMKTQFMMLWDGLS---TNANST--VIVMGATNRPQDLD 170
Cdd:cd19522   78 EKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEeHEASRRVKSELLVQMDGVGgasENDDPSkmVMVLAATNFPWDID 157

                        170
                 ....*....|...
gi 665407420 171 KAIVRRMPAQFHI 183
Cdd:cd19522  158 EALRRRLEKRIYI 170
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
16-232 5.16e-43

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 147.34  E-value: 5.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  16 WADIAGLDSVIQELRESVVLPIQHKDLFKHsKLWqAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGE 95
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKF-GLW-PPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  96 SQKLTSAVFSLASRiEPCIIFIDEIDSFLRSRNM-NDHEATAMMKTQFMMLWDGLstnaNSTVIVMGATNRPQDLDKAIV 174
Cdd:COG1223   79 TARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL----PSGSVVIAATNHPELLDSALW 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665407420 175 RRMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNA 232
Cdd:COG1223  154 RRFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 25-175 5.83e-43

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: 144.35  E-value: 5.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  25 VIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVF 104
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGI-RPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665407420 105 SLASRIEPCIIFIDEIDSFLRSR-NMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKAIVR 175
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIESLKG--VVVIAATNRPDMIDPALLR 149
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 14-195 2.42e-41

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 149.09  E-value: 2.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMR----------FINL 83
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELPFLHPELYREYGL-KPPKGVLLYGPPGCGKTLIAKAVANSLAARigaegggksyFLNI 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   84 DVAILTDKWYGESQKLTSAVFS----LASRIEPCIIFIDEIDSFLRSRNM---NDHEATAMmkTQFMMLWDGLSTNANst 156
Cdd:TIGR03689 258 KGPELLNKYVGETERQIRLIFQrareKASEGRPVIVFFDEMDSLFRTRGSgvsSDVETTVV--PQLLAEIDGVESLDN-- 333

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 665407420  157 VIVMGATNRPQDLDKAIVR--RMPAQFHIGLPSETQRKDIL 195
Cdd:TIGR03689 334 VIVIGASNREDMIDPAILRpgRLDVKIRIERPDAEAAADIF 374
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 18-181 2.48e-41

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: 140.65  E-value: 2.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGI-KPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKAIvrRM 177
Cdd:cd19519   80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAH--VIVMAATNRPNSIDPAL--RR 155


                 ....
gi 665407420 178 PAQF 181
Cdd:cd19519  156 FGRF 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 18-175 7.62e-41

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: 139.46  E-value: 7.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGV-EPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANST--VIVMGATNRPQDLDKAIVR 175
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAGgpVLVIGATNRPDSLDPALRR 159
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 22-175 2.24e-40

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: 138.00  E-value: 2.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  22 LDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTS 101
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGI-DLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665407420 102 AVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLStnANSTVIVMGATNRPQDLDKAIVR 175
Cdd:cd19530   80 QVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE--ERSNVFVIAATNRPDIIDPAMLR 151
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 15-181 3.85e-40

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: 137.47  E-value: 3.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  15 SWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLWQaPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYG 94
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEP-PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  95 ESQKLTSAVFSLASRIEPCIIFIDEIDSF----LRSRNMNDHEATAMMkTQFMMLWDGLSTNANSTVIvmGATNRPQDLD 170
Cdd:cd19502   80 EGARLVRELFEMAREKAPSIIFIDEIDAIgakrFDSGTGGDREVQRTM-LELLNQLDGFDPRGNIKVI--MATNRPDILD 156

                        170
                 ....*....|.
gi 665407420 171 KAIVRrmPAQF 181
Cdd:cd19502  157 PALLR--PGRF 165
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
6-263 1.03e-39

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 145.56  E-value: 1.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   6 LVVPADITVSWADIAGLDSVIQELRESVvlpiqhkDLFKHSKLWQA-----PKGVLLHGPPGCGKTLIAKATAKEAGMRF 80
Cdd:COG0465  131 LYDEDKPKVTFDDVAGVDEAKEELQEIV-------DFLKDPEKFTRlgakiPKGVLLVGPPGTGKTLLAKAVAGEAGVPF 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  81 inldvailtdkwygesqkltsavFSL-------------ASRIE----------PCIIFIDEIDSFLRSRNM-----ND- 131
Cdd:COG0465  204 -----------------------FSIsgsdfvemfvgvgASRVRdlfeqakknaPCIIFIDEIDAVGRQRGAglgggHDe 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 132 HEAT-----AMMktqfmmlwDGLSTNANstVIVMGATNRPQDLDKAIVRrmPAQF----HIGLPSETQRKDILKLILQSE 202
Cdd:COG0465  261 REQTlnqllVEM--------DGFEGNEG--VIVIAATNRPDVLDPALLR--PGRFdrqvVVDLPDVKGREAILKVHARKK 328

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665407420 203 EVSQDVDLNRLSKLTNGFSGSDLREMCRNASvyrmrqLITSRdpsataldRNNVRITMDDL 263
Cdd:COG0465  329 PLAPDVDLEVIARRTPGFSGADLANLVNEAA------LLAAR--------RNKKAVTMEDF 375
ftsH CHL00176
cell division protein; Validated
 10-253 1.69e-39

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 145.58  E-value: 1.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  10 ADITVSWADIAGLDSVIQELREsVVLPIQHKDLF-----KHsklwqaPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLD 84
Cdd:CHL00176 176 ADTGITFRDIAGIEEAKEEFEE-VVSFLKKPERFtavgaKI------PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSIS 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  85 VAILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNM-----NDHEATAMMktQFMMLWDGLStnANSTVIV 159
Cdd:CHL00176 249 GSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigggNDEREQTLN--QLLTEMDGFK--GNKGVIV 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 160 MGATNRPQDLDKAIVR--RMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRM 237
Cdd:CHL00176 325 IAATNRVDILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTA 404

                        250
                 ....*....|....*...
gi 665407420 238 RQLITSRDPSA--TALDR 253
Cdd:CHL00176 405 RRKKATITMKEidTAIDR 422
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 14-245 5.45e-39

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 140.67  E-value: 5.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY 93
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGI-DPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  94 GESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRnmNDHEATAMMKTQFMML-----WDGLSTNANSTVIVmgATNRPQD 168
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKR--FDAQTGADREVQRILLellnqMDGFDQTTNVKVIM--ATNRADT 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 169 LDKAIVR--RMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNA---SVYRMRQLITS 243
Cdd:PTZ00454 297 LDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAgmqAVRKNRYVILP 376


                 ..
gi 665407420 244 RD 245
Cdd:PTZ00454 377 KD 378
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 25-175 1.44e-38

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 133.02  E-value: 1.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  25 VIQELRESVVLPIQHKDLFkhSKLWQAP-KGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAV 103
Cdd:cd19528    1 VKRELQELVQYPVEHPDKF--LKFGMTPsKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665407420 104 FSLASRIEPCIIFIDEIDSFLRSRNMN---DHEATAMMKTQFMMLWDGLstNANSTVIVMGATNRPQDLDKAIVR 175
Cdd:cd19528   79 FDKARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGM--NTKKNVFIIGATNRPDIIDPAILR 151
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 14-181 1.36e-37

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: 130.82  E-value: 1.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  14 VSWADIAGLDSVIQELRESVvlpiqhkDLFKHSKLWQA-----PKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAIL 88
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVV-------EFLKNPEKFTKlgakiPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  89 TDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSR---NMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNR 165
Cdd:cd19501   74 VEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgagLGGGHDEREQTLNQLLVEMDGFESNTG--VIVIAATNR 151

                        170
                 ....*....|....*.
gi 665407420 166 PQDLDKAIVRrmPAQF 181
Cdd:cd19501  152 PDVLDPALLR--PGRF 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 25-175 2.09e-37

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: 129.92  E-value: 2.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  25 VIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVF 104
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGI-RPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665407420 105 SLASRIEPCIIFIDEIDSFLRSRNMN-DHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKAIVR 175
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGTTgDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLR 149
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 15-239 2.64e-36

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 134.51  E-value: 2.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  15 SWADIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYG 94
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELPLTHPELYDDIGI-KPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  95 ESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRnmNDHEATAMMKTQFMML-----WDGLSTNANSTVIVmgATNRPQDL 169
Cdd:PTZ00361 260 DGPKLVRELFRVAEENAPSIVFIDEIDAIGTKR--YDATSGGEKEIQRTMLellnqLDGFDSRGDVKVIM--ATNRIESL 335

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665407420 170 DKAIVR--RMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQ 239
Cdd:PTZ00361 336 DPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRE 407
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
12-238 3.01e-36

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 136.70  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  12 ITVSWADIAGLDSVIQELRESVvlpiqhkDLFKHSKLWQA-----PKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVA 86
Cdd:PRK10733 147 IKTTFADVAGCDEAKEEVAELV-------EYLREPSRFQKlggkiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  87 ILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNM---NDHEATAMMKTQFMMLWDGLStnANSTVIVMGAT 163
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE--GNEGIIVIAAT 297

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665407420 164 NRPQDLDKAIVR--RMPAQFHIGLPSETQRKDILKLILQSEEVSQDVDLNRLSKLTNGFSGSDLREMCRNASVYRMR 238
Cdd:PRK10733 298 NRPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 18-181 9.17e-34

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: 121.08  E-value: 9.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAG-----MRFINLDVAILTDKW 92
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKI-TPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  93 YGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKA 172
Cdd:cd19517   80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPA 157


                 ....*....
gi 665407420 173 IvrRMPAQF 181
Cdd:cd19517  158 L--RRPGRF 164
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 18-183 1.68e-32

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: 117.68  E-value: 1.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  18 DIAGLDSVIQELRESVVLPIQHKDLFkhSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQ 97
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAF--SGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  98 KLTSAVFSLASRIEPCIIFIDEIDSFLRSRnMNDHEATAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRM 177
Cdd:cd19523   79 KILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYF 157


                 ....*.
gi 665407420 178 PAQFHI 183
Cdd:cd19523  158 SKRLLV 163
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 25-175 2.87e-30

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: 111.37  E-value: 2.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  25 VIQELRESVVLPIQHKDLFKHSKLwQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVF 104
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPL-RLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665407420 105 SLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMKTQFMMLWDGLStnANSTVIVMGATNRPQDLDKAIVR 175
Cdd:cd19526   80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVE--GLDGVYVLAATSRPDLIDPALLR 148
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 25-181 5.18e-29

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: 108.37  E-value: 5.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  25 VIQELRESVVLPIQHKDLFkhSKLWQAPKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVF 104
Cdd:cd19527    1 VKKEILDTIQLPLEHPELF--SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVF 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665407420 105 SLASRIEPCIIFIDEIDSFLRSRNMNDHEATAMMK--TQFMMLWDGLSTnANSTVIVMGATNRPQDLDKAIVRrmPAQF 181
Cdd:cd19527   79 QKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDRvvSQLLAELDGMSS-SGQDVFVIGATNRPDLLDPALLR--PGRF 154
ycf46 CHL00195
Ycf46; Provisional
 51-227 8.17e-22

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 94.70  E-value: 8.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  51 APKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEID-SFLRSRNM 129
Cdd:CHL00195 258 TPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESK 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 130 NDHEATAMMKTQFMMlWdgLStNANSTVIVMGATNRPQDLDKAIVR--RMPAQFHIGLPSETQRKDILKLILQS--EEVS 205
Cdd:CHL00195 338 GDSGTTNRVLATFIT-W--LS-EKKSPVFVVATANNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKfrPKSW 413

                        170       180
                 ....*....|....*....|..
gi 665407420 206 QDVDLNRLSKLTNGFSGSDLRE 227
Cdd:CHL00195 414 KKYDIKKLSKLSNKFSGAEIEQ 435
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-185 1.72e-21

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: 88.36  E-value: 1.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  20 AGLDSVIQELRESVVLPiqhkdlfkhsklwqAPKGVLLHGPPGCGKTLIAKATAKEA---GMRFINLDVAILTDKWYGES 96
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  97 QKLTSAV---FSLASRIEPCIIFIDEIDSFLRsrnmndhEATAMMKTQFMMLWDGLSTNANstVIVMGATNRP--QDLDK 171
Cdd:cd00009   67 LFGHFLVrllFELAEKAKPGVLFIDEIDSLSR-------GAQNALLRVLETLNDLRIDREN--VRVIGATNRPllGDLDR 137

                        170
                 ....*....|....
gi 665407420 172 AIVRRMPAQFHIGL 185
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 51-176 1.15e-19

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: 83.57  E-value: 1.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  51 APKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGESQKLTSAVFSLASRIEPCIIFIDEIDSFLRSRNMN 130
Cdd:cd19507   30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSK 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 665407420 131 DHEATAMMKTQFMMLWdgLSTNaNSTVIVMGATNRPQDLDKAIVRR 176
Cdd:cd19507  110 GDSGTSSRVLGTFLTW--LQEK-KKPVFVVATANNVQSLPPELLRK 152
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 52-186 2.43e-13

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: 66.24  E-value: 2.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420    52 PKGVLLHGPPGCGKTLIAKATAKEA-----GMRFINLD------------VAILTDKWYGESQKLTSAVFSLASRIEPCI 114
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppggGVIYIDGEdileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665407420   115 IFIDEIDSFLRSRnmndheaTAMMKTQFMMLWDGLSTNANSTVIVMGATNRPQDLDKAIVRRMpAQFHIGLP 186
Cdd:smart00382  82 LILDEITSLLDAE-------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR-FDRRIVLL 145
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 39-182 1.14e-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: 61.39  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  39 HKDLFKHsklwqapkgVLLHGPPGCGKTLIAKATAKEAGMrfinlDVAILT--DKWYGESQKLTS--AVFSLASRIEP-C 113
Cdd:cd19512   18 NKGLYRN---------ILFYGPPGTGKTLFAKKLALHSGM-----DYAIMTggDVAPMGREGVTAihKVFDWANTSRRgL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 114 IIFIDEIDSFLRSRNMND-HEATAMMKTQFMMLwdgLSTNANSTVIVMgATNRPQDLDKAIVRRMPAQFH 182
Cdd:cd19512   84 LLFVDEADAFLRKRSTEKiSEDLRAALNAFLYR---TGEQSNKFMLVL-ASNQPEQFDWAINDRIDEMVE 149
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 53-183 2.76e-11

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: 60.97  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  53 KGVLLHGPPGCGKTLIAKATAKEAGMR---FINlDVAILtDKWYGESQKLTSAVFSLASRIEPC--------IIFIDEID 121
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNARepkIVN-GPEIL-NKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEID 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665407420 122 SFLRSR-NMNDHEATA-MMKTQFMMLWDGLSTNANstVIVMGATNRPQDLDKAIVR--RMPAQFHI 183
Cdd:cd19504  114 AICKQRgSMAGSTGVHdTVVNQLLSKIDGVEQLNN--ILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 55-183 2.03e-09

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: 56.30  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEAGMR---------FINLDVAILTDKWYGESQKLTSAVFSLASRI---EPCIIF--IDEI 120
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlIDEV 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665407420 121 DSFLRSRN--MNDHEATAMMK--TQFMMLWDGLSTNANstVIVMGATNRPQDLDKAIVRRMPAQFHI 183
Cdd:cd19508  135 ESLAAARSasSSGTEPSDAIRvvNAVLTQIDRIKRYHN--NVILLTSNLLEKIDVAFVDRADIKQYI 199
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 207-243 5.30e-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: 48.30  E-value: 5.30e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 665407420  207 DVDLNRLSKLTNGFSGSDLREMCRNASVYRMRQLITS 243
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 55-124 6.05e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.16  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEAGMRFINLdvailtdkwygesqkltSAVFS--------------LASRIEPCIIFIDEI 120
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEAL-----------------SAVTSgvkdlrevieearqRRSAGRRTILFIDEI 101

                         90
                 ....*....|..
gi 665407420 121 --------DSFL 124
Cdd:PRK13342 102 hrfnkaqqDALL 113
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 55-124 6.08e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.14  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEAGMRFINLdvailtdkwygesqkltSAVFS--------------LASRIEPCIIFIDEI 120
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVAL-----------------SAVTSgvkdirevieeareRRAYGRRTILFVDEI 114

                         90
                 ....*....|..
gi 665407420 121 --------DSFL 124
Cdd:COG2256  115 hrfnkaqqDALL 126
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 53-183 1.31e-07

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: 50.04  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  53 KGVLLHGPPGCGKTLIAKATAKEAGMRFINLDvaiLTDKwyGESQKLTSAVFSLASriEPCIIFIDEIDSFLRSRNMNDH 132
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGELDYDICDLN---LSEV--VLTDDRLNHLLNTAP--KQSIILLEDIDAAFESREHNKK 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665407420 133 EATA---MMKTQFMMLW---DGLsTNANSTVIVMgATNRPQDLDKAIVR--RMPAQFHI 183
Cdd:cd19510   97 NPSAyggLSRVTFSGLLnalDGV-ASSEERIVFM-TTNHIERLDPALIRpgRVDMKIYM 153
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 52-121 3.52e-06

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: 46.03  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   52 PKGV-LLHGPPGCGKTLIAKATAKEAGM---RFINLDVAILTDKW--------------YGESQKLTSAVfslaSRIEPC 113
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHsvsrligappgyvgYEEGGQLTEAV----RRKPYS 77


                  ....*...
gi 665407420  114 IIFIDEID 121
Cdd:pfam07724  78 IVLIDEIE 85
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 53-170 6.43e-06

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: 45.21  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  53 KGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYGES--QKLTSAVFSLASRIEPCIIFIDEID-SFLR---- 125
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEkTFYKkvpk 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 665407420 126 SRNMNDHEATAMMKTQFMMlwdglSTNANSTVIVMGATNRPQDLD 170
Cdd:cd19506  107 TEKQLDPKRLKKDLPKILK-----SLKPEDRVLIVGTTSRPFEAD 146
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 55-121 1.11e-05

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 45.67  E-value: 1.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWY-GES-----QKLTSAVFSLASRIEPCIIFIDEID 121
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYvGEDvenilLKLLQAADYDVERAQRGIVYIDEID 125
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 52-121 1.28e-05

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 44.68  E-value: 1.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  52 PKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKWYgESQKLTSAVFSLASRiepcIIFIDEID 121
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGY-VGRDVESIIRDLVEG----IVFIDEID 110
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 52-174 7.71e-05

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: 42.36  E-value: 7.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  52 PKGVLLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTDKW--------------YGESQKLTSAVFSLASRIEPCIIFI 117
Cdd:cd19505   12 SKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIWI 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665407420 118 DEIDSFLRSRNMNDHEATAmmKTQFMMLWDGLSTNA--NST--VIVMGATNRPQDLDKAIV 174
Cdd:cd19505   92 PNIHELNVNRSTQNLEEDP--KLLLGLLLNYLSRDFekSSTrnILVIASTHIPQKVDPALI 150
PRK04195 PRK04195
replication factor C large subunit; Provisional
 17-77 1.19e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 43.37  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665407420  17 ADIAGLDSVIQELRESVvlpiqhkDLFKHSKlwqAPKGVLLHGPPGCGKTLIAKATAKEAG 77
Cdd:PRK04195  14 SDVVGNEKAKEQLREWI-------ESWLKGK---PKKALLLYGPPGVGKTSLAHALANDYG 64
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
55-121 1.39e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.84  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEagmrfinLDV--AI-----LTDKWY-GES-----QKL-TSAVFSLAsRIEPCIIFIDEI 120
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARI-------LDVpfAIadattLTEAGYvGEDvenilLKLlQAADYDVE-KAQRGIVYIDEI 182


                 .
gi 665407420 121 D 121
Cdd:PRK05342 183 D 183
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 59-87 1.96e-04

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 41.00  E-value: 1.96e-04
                         10        20
                 ....*....|....*....|....*....
gi 665407420  59 GPPGCGKTLIAKATAKEAGMRFINLDVAI 87
Cdd:cd00464    6 GMMGAGKTTVGRLLAKALGLPFVDLDELI 34
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 54-177 2.26e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 40.35  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420   54 GVLLHGPPGCGKTLIAKATAK---------EAGMRFIN-------LDVAILTDKWygESQKLTSAVfslasrIEPCIIFI 117
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAalsnrpvfyVQLTRDTTeedlfgrRNIDPGGASW--VDGPLVRAA------REGEIAVL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  118 DEIdsflrsrNMNDHEATAMMKT-----QFMMLW-DGLSTNANSTVIVMGATNRP----QDLDKAIVRRM 177
Cdd:pfam07728  73 DEI-------NRANPDVLNSLLSllderRLLLPDgGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
47-120 2.64e-04

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 41.85  E-value: 2.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665407420  47 KLWQAPKGVLLHGPPGCGKTLIAKATAKE-AGMRFINLDVAILTDKWYGESQKLTSAVFSLASriEPCIIFIDEI 120
Cdd:COG1373   15 KLLDNRKAVVITGPRQVGKTTLLKQLAKElENILYINLDDPRLRALAEEDPDDLLEALKELYP--GKTYLFLDEI 87
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 59-87 2.80e-04

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 40.50  E-value: 2.80e-04
                         10        20
                 ....*....|....*....|....*....
gi 665407420  59 GPPGCGKTLIAKATAKEAGMRFINLDVAI 87
Cdd:COG0703    5 GMMGAGKSTVGRLLAKRLGLPFVDTDAEI 33
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
28-77 3.23e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 3.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 665407420  28 ELRESVVLPIQhkdLFKHSKLwqAPKGVLLHGPPGCGKTLIAKATAKEAG 77
Cdd:COG1224   45 EAREAAGIVVK---MIKEGKM--AGKGILIVGPPGTGKTALAVAIARELG 89
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 55-81 4.85e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.92  E-value: 4.85e-04
                         10        20
                 ....*....|....*....|....*..
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEAGMRFI 81
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFI 60
aroK PRK00131
shikimate kinase; Reviewed
 59-87 1.13e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.02  E-value: 1.13e-03
                         10        20
                 ....*....|....*....|....*....
gi 665407420  59 GPPGCGKTLIAKATAKEAGMRFINLDVAI 87
Cdd:PRK00131  11 GFMGAGKSTIGRLLAKRLGYDFIDTDHLI 39
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 55-120 1.26e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665407420   55 VLLHGPPGCGKTLIAKATAKEAGMRFinldvailtdkwygesqKLTSA--------VFSLASRIEPC-IIFIDEI 120
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-----------------RITSGpaierpgdLAAILTNLEPGdVLFIDEI 93
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 41-77 1.93e-03

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: 39.21  E-value: 1.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 665407420   41 DLFKHSKLwqAPKGVLLHGPPGCGKTLIAKATAKEAG 77
Cdd:pfam06068  41 EMIKEGKI--AGRAVLIAGPPGTGKTALAIAISKELG 75
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
15-74 1.99e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.02  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  15 SWADIAGLDSVIQELRESVvlpiqhkdlfKHSKLWQApkgVLLHGPPGCGKTLIAKATAK 74
Cdd:COG2812    8 TFDDVVGQEHVVRTLKNAL----------ASGRLAHA---YLFTGPRGVGKTTLARILAK 54
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 55-85 3.59e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 37.23  E-value: 3.59e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 665407420  55 VLLHGPPGCGKTLIAKATAKEAGMRFINLDV 85
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDD 32
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
49-219 4.72e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 38.03  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  49 WQAPKGVLLHGPPGCGKTLIAKATAKE---------------AGMRFINL---DVAILTDKWYGES------QKLTSAvF 104
Cdd:COG0470   15 GRLPHALLLHGPPGIGKTTLALALARDllcenpeggkacgqcHSRLMAAGnhpDLLELNPEEKSDQigidqiRELGEF-L 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420 105 SLASRIEPC-IIFIDEIDsflrsrNMNDHEATAMMKTqfmmlwdgLSTNANSTVIVMgATNRPQDLDKAIVRRMpAQFHI 183
Cdd:COG0470   94 SLTPLEGGRkVVIIDEAD------AMNEAAANALLKT--------LEEPPKNTPFIL-IANDPSRLLPTIRSRC-QVIRF 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 665407420 184 GLPSETQRKDILKlilqsEEVSQDVDLNRLSKLTNG 219
Cdd:COG0470  158 RPPSEEEALAWLR-----EEGVDEDALEAILRLAGG 188
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 55-87 4.80e-03

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


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 36.52  E-value: 4.80e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665407420   55 VLLHGPPGCGKTLIAKATAKEAGMRFINLDVAI 87
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDER 34
PRK13341 PRK13341
AAA family ATPase;
56-176 5.25e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 38.11  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  56 LLHGPPGCGKTLIAKATAKEAGMRFINLDvAILTdkwyGESQkLTSAVFSLASRIE----PCIIFIDEIDSFlrsrNmnd 131
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLN-AVLA----GVKD-LRAEVDRAKERLErhgkRTILFIDEVHRF----N--- 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 665407420 132 heatammKTQFMMLwdgLSTNANSTVIVMGAT--NRPQDLDKAIVRR 176
Cdd:PRK13341 123 -------KAQQDAL---LPWVENGTITLIGATteNPYFEVNKALVSR 159
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 47-77 7.31e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 37.83  E-value: 7.31e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 665407420  47 KLWQAPKGVLLHGPPGCGKTLIAKATAKEAG 77
Cdd:COG1401  216 AALKTKKNVILAGPPGTGKTYLARRLAEALG 246
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 56-90 7.42e-03

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 36.77  E-value: 7.42e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 665407420  56 LLHGPPGCGKTLIAKATAKEAGMRFINLDVAILTD 90
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRD 75
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 56-121 7.78e-03

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_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: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 36.39  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407420  56 LLHGPPGCGKTLIAKATAKE---AGMRFINLD---------VAILTDKW-----YGESQKLTSAVfslaSRIEPCIIFID 118
Cdd:cd19499   45 LFLGPTGVGKTELAKALAELlfgDEDNLIRIDmseymekhsVSRLIGAPpgyvgYTEGGQLTEAV----RRKPYSVVLLD 120


                 ...
gi 665407420 119 EID 121
Cdd:cd19499  121 EIE 123
 
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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