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Conserved domains on  [gi|55925351|ref|NP_001007432|]
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katanin p60 ATPase-containing subunit A-like 1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 207-376 2.02e-131

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: 377.79  E-value: 2.02e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 287 VRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVGGAQESEDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 55925351 367 RRRLEKRIYI 376
Cdd:cd19522 161 RRRLEKRIYI 170
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 5-72 3.37e-38

N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar proteins; This model represents the N-terminal domain (NTD) of katanin p60 ATPase-containing subunit A1 (also called p60 katanin 1 or katanin p60 subunit A1), which is organized into an antiparallel three-helix bundle and is responsible for tubulin binding. Katanin p60 subunit A1 plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. It is a microtubule-severing protein (MTSP) that maintains the density of spindle microtubules at the poles in mitotic cells. MSTPs are a group of microtubule-associated proteins essential for multiple microtubule-related processes, including mitosis and meiosis. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles allows depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. Katanin p60 has been implicated in several malignancies; it is aberrantly expressed in prostate cancer patients with bone metastasis where upregulation of katanin P60 inhibits cell proliferation but enhances cell migration. It promotes cell migration in breast cancer where high ketanin p60 expression in tumor tissue is correlated with lymph node metastasis and poor overall survival. Katanin p60 may also be a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer. Katanin is a heterodimer with an AAA catalytic subunit katanin P60 and a non-AAA subunit katanin P80. In ASPM (known as Asp in fly and ASPM-1 in worm), a microcephaly-associated protein family that regulates spindle architecture, the N-terminal domain of katanin p60 subunit (kp60-NTD) and C-terminal domain of katanin p80 subunit form a heterodimer, which then binds conserved motifs in ASPM, thus forming a complex that controls microtubule disassembly at spindle poles; misregulation of this process can lead to microcephaly. p60 katanin-like 1 has been shown to be predominantly enriched within oocytes and ovaries, and essential for oocyte meiosis and maturation. The N-terminal domain of mouse katanin p60 (kp60-NTD) also binds to tubulin; structure studies of kp60-NTD reveal a striking similarity to the microtubule interacting and trafficking (MIT) domains, although their sequence similarities are low.


:

Pssm-ID: 439297  Cd Length: 69  Bit Score: 133.47  E-value: 3.37e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55925351   5 EICDNAKKGREYALLGNYDSSMVYYQGVIQQIHKHCQSLRDPAQKVKWQQVRQELAEEYEQVKSIVST 72
Cdd:cd21748   2 EICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 400-444 2.22e-12

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: 61.40  E-value: 2.22e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 55925351   400 DVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGLSPEEIRA 444
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 448-486 2.00e-09

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


The actual alignment was detected with superfamily member pfam09336:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 53.65  E-value: 2.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 55925351   448 DELQMP-VTMEDFELALKKISKSVSAADLEKYESWMSEFG 486
Cdd:pfam09336  22 DKLLEPpVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 207-376 2.02e-131

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: 377.79  E-value: 2.02e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 287 VRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVGGAQESEDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 55925351 367 RRRLEKRIYI 376
Cdd:cd19522 161 RRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 158-469 1.48e-96

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 294.61  E-value: 1.48e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 158 AKEEKSKRNAQEGAADVEQKKFDGTGYDSDLVDALERdivsrnPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GI 235
Cdd:COG1222  36 VKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAES------PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGI 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 236 RRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRG 315
Cdd:COG1222 110 EPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRT 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 316 TSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLR 393
Cdd:COG1222 189 DDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLR 261

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55925351 394 EVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGlspeeiralskdelqmpVTMEDFELALKKISKS 469
Cdd:COG1222 262 DMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT-----------------VTMEDLEKAIEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 194-488 7.77e-79

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: 260.61  E-value: 7.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   194 RDIVSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVS 271
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVR 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   272 SSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVM 351
Cdd:TIGR01243 520 GPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGI-------QELSNVV 592

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   352 VLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMA 429
Cdd:TIGR01243 593 VIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAA 672

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   430 MRRRIQGLSPEEIRALSKDELQ-MPVTMEDFELALKKISKSVSAADLEKYESWMSEFGSV 488
Cdd:TIGR01243 673 LRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRL 732
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 201-468 2.18e-76

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 244.74  E-value: 2.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  201 PNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSK 278
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  279 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRR---GTSDEHEASRRVkSELLVQMDGVggaqeseDPSKMVMVLAA 355
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-------DPRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  356 TNFPwDI-DEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRR 432
Cdd:PRK03992 277 TNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 55925351  433 RiqglspeeiralsKDElqmpVTMEDFELALKKISK 468
Cdd:PRK03992 356 D-------------RTE----VTMEDFLKAIEKVMG 374
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 242-378 1.59e-55

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: 181.25  E-value: 1.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGtSDEHE 321
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG-SGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 55925351   322 ASRRVKSELLVQMDGVggaqesEDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPL 378
Cdd:pfam00004  80 ESRRVVNQLLTELDGF------TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 5-72 3.37e-38

N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar proteins; This model represents the N-terminal domain (NTD) of katanin p60 ATPase-containing subunit A1 (also called p60 katanin 1 or katanin p60 subunit A1), which is organized into an antiparallel three-helix bundle and is responsible for tubulin binding. Katanin p60 subunit A1 plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. It is a microtubule-severing protein (MTSP) that maintains the density of spindle microtubules at the poles in mitotic cells. MSTPs are a group of microtubule-associated proteins essential for multiple microtubule-related processes, including mitosis and meiosis. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles allows depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. Katanin p60 has been implicated in several malignancies; it is aberrantly expressed in prostate cancer patients with bone metastasis where upregulation of katanin P60 inhibits cell proliferation but enhances cell migration. It promotes cell migration in breast cancer where high ketanin p60 expression in tumor tissue is correlated with lymph node metastasis and poor overall survival. Katanin p60 may also be a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer. Katanin is a heterodimer with an AAA catalytic subunit katanin P60 and a non-AAA subunit katanin P80. In ASPM (known as Asp in fly and ASPM-1 in worm), a microcephaly-associated protein family that regulates spindle architecture, the N-terminal domain of katanin p60 subunit (kp60-NTD) and C-terminal domain of katanin p80 subunit form a heterodimer, which then binds conserved motifs in ASPM, thus forming a complex that controls microtubule disassembly at spindle poles; misregulation of this process can lead to microcephaly. p60 katanin-like 1 has been shown to be predominantly enriched within oocytes and ovaries, and essential for oocyte meiosis and maturation. The N-terminal domain of mouse katanin p60 (kp60-NTD) also binds to tubulin; structure studies of kp60-NTD reveal a striking similarity to the microtubule interacting and trafficking (MIT) domains, although their sequence similarities are low.


Pssm-ID: 439297  Cd Length: 69  Bit Score: 133.47  E-value: 3.37e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55925351   5 EICDNAKKGREYALLGNYDSSMVYYQGVIQQIHKHCQSLRDPAQKVKWQQVRQELAEEYEQVKSIVST 72
Cdd:cd21748   2 EICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 238-380 7.24e-18

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: 80.50  E-value: 7.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351    238 PWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYAPT 300
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351    301 TIFIDEIDSICgrrgtsdeheasrRVKSELLVQMDGVGGAQESEDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 379
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147


                   .
gi 55925351    380 T 380
Cdd:smart00382 148 L 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 400-444 2.22e-12

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: 61.40  E-value: 2.22e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 55925351   400 DVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGLSPEEIRA 444
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 448-486 2.00e-09

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 53.65  E-value: 2.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 55925351   448 DELQMP-VTMEDFELALKKISKSVSAADLEKYESWMSEFG 486
Cdd:pfam09336  22 DKLLEPpVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 242-307 9.15e-04

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 39.78  E-value: 9.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55925351  242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYAPTTIFIDEI 307
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINVNLElsrrllELPEKQR--ALRAPRLLDEIAEKSSGDVVLLDNI 88
 
Name Accession Description Interval E-value
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 207-376 2.02e-131

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: 377.79  E-value: 2.02e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 287 VRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVGGAQESEDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 55925351 367 RRRLEKRIYI 376
Cdd:cd19522 161 RRRLEKRIYI 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 208-376 6.96e-97

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: 289.25  E-value: 6.96e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 208 IADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLV 287
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 288 RLLFEMARFYAPTTIFIDEIDSICGRRGtSDEHEASRRVKSELLVQMDGVGGaqeseDPSKMVMVLAATNFPWDIDEALR 367
Cdd:cd19509  81 RALFALARELQPSIIFIDEIDSLLSERG-SGEHEASRRVKTEFLVQMDGVLN-----KPEDRVLVLGATNRPWELDEAFL 154


                ....*....
gi 55925351 368 RRLEKRIYI 376
Cdd:cd19509 155 RRFEKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 158-469 1.48e-96

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 294.61  E-value: 1.48e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 158 AKEEKSKRNAQEGAADVEQKKFDGTGYDSDLVDALERdivsrnPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GI 235
Cdd:COG1222  36 VKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAES------PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGI 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 236 RRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRG 315
Cdd:COG1222 110 EPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRT 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 316 TSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLR 393
Cdd:COG1222 189 DDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLR 261

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55925351 394 EVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGlspeeiralskdelqmpVTMEDFELALKKISKS 469
Cdd:COG1222 262 DMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT-----------------VTMEDLEKAIEKVKKK 320
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 201-376 6.80e-80

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: 245.93  E-value: 6.80e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 201 PNIHWDDIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYR 280
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 281 GESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGtSDEHEASRRVKSELLVQMDGVGGAQESedpskmVMVLAATNFPW 360
Cdd:cd19521  82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRG-EGESEASRRIKTELLVQMNGVGNDSQG------VLVLGATNIPW 154

                       170
                ....*....|....*.
gi 55925351 361 DIDEALRRRLEKRIYI 376
Cdd:cd19521 155 QLDSAIRRRFEKRIYI 170
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 194-488 7.77e-79

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: 260.61  E-value: 7.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   194 RDIVSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVS 271
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVR 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   272 SSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVM 351
Cdd:TIGR01243 520 GPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGI-------QELSNVV 592

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   352 VLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMA 429
Cdd:TIGR01243 593 VIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAA 672

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   430 MRRRIQGLSPEEIRALSKDELQ-MPVTMEDFELALKKISKSVSAADLEKYESWMSEFGSV 488
Cdd:TIGR01243 673 LRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRL 732
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 190-466 3.63e-77

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: 247.13  E-value: 3.63e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 190 DALERDIVSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTF 267
Cdd:COG0464 141 IGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPL 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 268 FNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHeASRRVKSELLVQMDGVggaqesEDPs 347
Cdd:COG0464 220 IEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL------RSD- 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 348 kmVMVLAATNFPWDIDEALRRRLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASM 427
Cdd:COG0464 292 --VVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAAL 369

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 55925351 428 MAMRrriqglspeeiralskdELQMPVTMEDFELALKKI 466
Cdd:COG0464 370 QALR-----------------LGREPVTTEDLLEALERE 391
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 201-468 2.18e-76

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 244.74  E-value: 2.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  201 PNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSK 278
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  279 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRR---GTSDEHEASRRVkSELLVQMDGVggaqeseDPSKMVMVLAA 355
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-------DPRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  356 TNFPwDI-DEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRR 432
Cdd:PRK03992 277 TNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 55925351  433 RiqglspeeiralsKDElqmpVTMEDFELALKKISK 468
Cdd:PRK03992 356 D-------------RTE----VTMEDFLKAIEKVMG 374
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 185-376 2.38e-75

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: 234.88  E-value: 2.38e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 185 DSDLVDALERDIVSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECG 264
Cdd:cd19525   1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 265 TTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSdEHEASRRVKSELLVQMDGVGGAqese 344
Cdd:cd19525  81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-EHESSRRIKTEFLVQLDGATTS---- 155

                       170       180       190
                ....*....|....*....|....*....|..
gi 55925351 345 dPSKMVMVLAATNFPWDIDEALRRRLEKRIYI 376
Cdd:cd19525 156 -SEDRILVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 207-376 1.13e-63

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: 203.93  E-value: 1.13e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 287 VRLLFEMARFYAPTTIFIDEIDSICGRRGTSdEHEASRRVKSELLVQMDGVGGaqeseDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSEG-EHEASRRLKTEFLIEFDGVQS-----NGDDRVLVMGATNRPQELDDAV 154

                       170
                ....*....|
gi 55925351 367 RRRLEKRIYI 376
Cdd:cd19524 155 LRRFTKRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 191-469 3.25e-62

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: 215.93  E-value: 3.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   191 ALERDIVSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFF 268
Cdd:TIGR01243 163 PVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAGAYFI 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   269 NVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRgtsDE--HEASRRVKSELLVQMDGVGGAQEsedp 346
Cdd:TIGR01243 242 SINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR---EEvtGEVEKRVVAQLLTLMDGLKGRGR---- 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   347 skmVMVLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRD 424
Cdd:TIGR01243 315 ---VIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKE 391

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 55925351   425 ASMMAMRRRIQ----GLSPEEIRALSKDELQmpVTMEDFELALKKISKS 469
Cdd:TIGR01243 392 AAMAALRRFIRegkiNFEAEEIPAEVLKELK--VTMKDFMEALKMVEPS 438
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 242-378 1.59e-55

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: 181.25  E-value: 1.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGtSDEHE 321
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG-SGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 55925351   322 ASRRVKSELLVQMDGVggaqesEDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPL 378
Cdd:pfam00004  80 ESRRVVNQLLTELDGF------TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 207-376 5.31e-55

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: 181.47  E-value: 5.31e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIR--RPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 285 KLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDeHEASRRVKSELLVQMDGVggaqeSEDPSKMVMVLAATNFPWDIDE 364
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTD-HEATAMMKAEFMSLWDGL-----STDGNCRVIVMGATNRPQDLDE 154

                       170
                ....*....|..
gi 55925351 365 ALRRRLEKRIYI 376
Cdd:cd19520 155 AILRRMPKRFHI 166
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 214-376 6.11e-55

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 180.94  E-value: 6.11e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 214 AKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLF 291
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 292 EMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVGGAQEsedpskmVMVLAATNFPWDIDEALRR--R 369
Cdd:cd19511  80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESLKG-------VVVIAATNRPDMIDPALLRpgR 152


                ....*..
gi 55925351 370 LEKRIYI 376
Cdd:cd19511 153 LDKLIYV 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
205-477 1.35e-54

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 183.16  E-value: 1.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 205 WDDIADLEDAKKLLREAVvlpmwmpDFFKGIRRP-----W--KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTS 277
Cdd:COG1223   1 LDDVVGQEEAKKKLKLII-------KELRRRENLrkfglWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 278 KYRGESEKLVRLLFEMARfYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGvggaqeseDPSKmVMVLAATN 357
Cdd:COG1223  74 SYLGETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDG--------LPSG-SVVIAATN 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 358 FPWDIDEALRRRLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDasmmAMRRRIqgL 437
Cdd:COG1223 144 HPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKT----ALKKAI--L 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 55925351 438 SPEEIralskdelqmpVTMEDFELALKKISKSVSAADLEK 477
Cdd:COG1223 218 EDREK-----------VTKEDLEEALKQRKERKKEPKKEG 246
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 207-376 4.13e-53

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 176.33  E-value: 4.13e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 285 KLVRLLFEMARFYAPTTIFIDEIDSICGRRGtSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVMVLAATNFPWDIDE 364
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKRE-EDQREVERRVVAQLLTLMDGM-------SSRGKVVVIAATNRPDAIDP 151

                       170
                ....*....|....
gi 55925351 365 ALRR--RLEKRIYI 376
Cdd:cd19503 152 ALRRpgRFDREVEI 165
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 214-376 4.18e-52

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 173.62  E-value: 4.18e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 214 AKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEM 293
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 294 ARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVggaqESEDPskmVMVLAATNFPWDIDEALRR--RLE 371
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGV----NSRSK---VLVIAATNRPDLLDPALLRpgRFD 153


                ....*
gi 55925351 372 KRIYI 376
Cdd:cd19481 154 EVIEF 158
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
196-466 2.63e-51

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 183.31  E-value: 2.63e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 196 IVSRNPNIHWDDIADLEDAKKLLREAVvlpmwmpDFFK--------GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTF 267
Cdd:COG0465 132 YDEDKPKVTFDDVAGVDEAKEELQEIV-------DFLKdpekftrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPF 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 268 FNVSSSTLTSKY------RgeseklVRLLFEMARFYAPTTIFIDEIDSIcGR-RGTS-----DEHEasrRVKSELLVQMD 335
Cdd:COG0465 204 FSISGSDFVEMFvgvgasR------VRDLFEQAKKNAPCIIFIDEIDAV-GRqRGAGlggghDERE---QTLNQLLVEMD 273

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 336 GVggaqeseDPSKMVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEG 412
Cdd:COG0465 274 GF-------EGNEGVIVIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPG 345

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 55925351 413 YSGADITNVCRDASMMAMRRRiqglspeeiralsKDElqmpVTMEDFELALKKI 466
Cdd:COG0465 346 FSGADLANLVNEAALLAARRN-------------KKA----VTMEDFEEAIDRV 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 197-432 3.09e-48

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 171.10  E-value: 3.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  197 VSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSST 274
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEqiGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  275 LTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRR---GTSDEHEAsRRVKSELLVQMDGVggaqeseDPSKMVM 351
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGADREV-QRILLELLNQMDGF-------DQTTNVK 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  352 VLAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMA 429
Cdd:PTZ00454 287 VIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQA 366


                 ...
gi 55925351  430 MRR 432
Cdd:PTZ00454 367 VRK 369
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 197-466 3.37e-48

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.88  E-value: 3.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  197 VSRNPNIHWDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSST 274
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  275 LTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRR--GTSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVMV 352
Cdd:PTZ00361 253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGF-------DSRGDVKV 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  353 LAATNFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAM 430
Cdd:PTZ00361 326 IMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 55925351  431 RRRiqglspeeiralskdelQMPVTMEDFELALKKI 466
Cdd:PTZ00361 406 RER-----------------RMKVTQADFRKAKEKV 424
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 205-374 3.66e-48

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: 163.66  E-value: 3.66e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 205 WDDIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGE 282
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 283 SEKLVRLLFEMARFYAPTTIFIDEIDSICGRR---GTSDEHEASRRVkSELLVQMDGVggaqeseDPSKMVMVLAATNFP 359
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTM-LELLNQLDGF-------DPRGNIKVIMATNRP 152

                       170
                ....*....|....*..
gi 55925351 360 WDIDEALRR--RLEKRI 374
Cdd:cd19502 153 DILDPALLRpgRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 214-376 1.26e-45

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 156.50  E-value: 1.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 214 AKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLF 291
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 292 EMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMDGVggaqeseDPSKMVMVLAATNFPWDIDEALRR--R 369
Cdd:cd19529  80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-------EEMNGVVVIAATNRPDIIDPALLRagR 152


                ....*..
gi 55925351 370 LEKRIYI 376
Cdd:cd19529 153 FDRLIYI 159
ftsH CHL00176
cell division protein; Validated
 203-442 1.69e-45

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 168.30  E-value: 1.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  203 IHWDDIADLEDAKKLLREAVVLpMWMPDFFKGI-RRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRG 281
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  282 ESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGT-----SDEHEasrRVKSELLVQMDGVGGaqesedpSKMVMVLAAT 356
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigggNDERE---QTLNQLLTEMDGFKG-------NKGVIVIAAT 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  357 NFPWDIDEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRI 434
Cdd:CHL00176 329 NRVDILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKK 408


                 ....*...
gi 55925351  435 QGLSPEEI 442
Cdd:CHL00176 409 ATITMKEI 416
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
207-452 1.76e-42

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 159.81  E-value: 1.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  207 DIADLEDAKKLLREAVVLpMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  285 KLVRLLFEMARFYAPTTIFIDEIDSICGRRGT--SDEHEASRRVKSELLVQMDGVGGaqesedpSKMVMVLAATNFPWDI 362
Cdd:PRK10733 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEG-------NEGIIVIAATNRPDVL 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  363 DEALRR--RLEKRIYIPLPTAKGRAELLKINLREVDVASDVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGLSPE 440
Cdd:PRK10733 304 DPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMV 383

                        250
                 ....*....|..
gi 55925351  441 EIRAlSKDELQM 452
Cdd:PRK10733 384 EFEK-AKDKIMM 394
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 207-377 5.85e-42

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 147.20  E-value: 5.85e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKaiGIKPP-RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 285 KLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSdEHEASRRVKSELLVQMDGVGGAQEsedpskmVMVLAATNFPWDIDE 364
Cdd:cd19519  80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT-HGEVERRIVSQLLTLMDGLKQRAH-------VIVMAATNRPNSIDP 151

                       170
                ....*....|....*
gi 55925351 365 ALRR--RLEKRIYIP 377
Cdd:cd19519 152 ALRRfgRFDREIDIG 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 215-376 5.29e-41

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: 144.19  E-value: 5.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 215 KKLLREAVVLPMWMPD-FFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEM 293
Cdd:cd19528   2 KRELQELVQYPVEHPDkFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 294 ARFYAPTTIFIDEIDSICGRRGTS--DEHEASRRVKSELLVQMDGVggaqeseDPSKMVMVLAATNFPWDIDEALRR--R 369
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNigDAGGAADRVINQILTEMDGM-------NTKKNVFIIGATNRPDIIDPAILRpgR 154


                ....*..
gi 55925351 370 LEKRIYI 376
Cdd:cd19528 155 LDQLIYI 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 207-376 1.04e-40

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: 143.49  E-value: 1.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 286
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 287 VRLLFEMARFYAPTTIFIDEIDSICGRRgtSDEHEASRRVKSELLVQMDGVGGAqesedPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19523  81 LQASFLAARCRQPSVLFISDLDALLSSQ--DDEASPVGRLQVELLAQLDGVLGS-----GEDGVLVVCTTSKPEEIDESL 153

                       170
                ....*....|
gi 55925351 367 RRRLEKRIYI 376
Cdd:cd19523 154 RRYFSKRLLV 163
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 203-376 2.45e-40

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: 142.76  E-value: 2.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 203 IHWDDIADLEDAKKLLREAVvlpmwmpDFFK--------GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSST 274
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVV-------EFLKnpekftklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 275 LTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGT--SDEHEASRRVKSELLVQMDGVGGaqesedpSKMVMV 352
Cdd:cd19501  73 FVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglGGGHDEREQTLNQLLVEMDGFES-------NTGVIV 145

                       170       180
                ....*....|....*....|....*.
gi 55925351 353 LAATNFPWDIDEALRR--RLEKRIYI 376
Cdd:cd19501 146 IAATNRPDVLDPALLRpgRFDRQVYV 171
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 211-376 2.56e-39

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 139.93  E-value: 2.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 211 LEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVR 288
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 289 LLFEMARFYAPTTIFIDEIDSICGRRGTSdEHEASRRVKSELLVQMDGVGGAQEsedpskmVMVLAATNFPWDIDEALRR 368
Cdd:cd19530  80 QVFQRARASAPCVIFFDEVDALVPKRGDG-GSWASERVVNQLLTEMDGLEERSN-------VFVIAATNRPDIIDPAMLR 151

                       170
                ....*....|
gi 55925351 369 --RLEKRIYI 376
Cdd:cd19530 152 pgRLDKTLYV 161
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 5-72 3.37e-38

N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar proteins; This model represents the N-terminal domain (NTD) of katanin p60 ATPase-containing subunit A1 (also called p60 katanin 1 or katanin p60 subunit A1), which is organized into an antiparallel three-helix bundle and is responsible for tubulin binding. Katanin p60 subunit A1 plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. It is a microtubule-severing protein (MTSP) that maintains the density of spindle microtubules at the poles in mitotic cells. MSTPs are a group of microtubule-associated proteins essential for multiple microtubule-related processes, including mitosis and meiosis. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles allows depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome. Microtubule release within the cell body of neurons may be required for their transport into neuronal processes by microtubule-dependent motor proteins. This transport is required for axonal growth. Katanin p60 has been implicated in several malignancies; it is aberrantly expressed in prostate cancer patients with bone metastasis where upregulation of katanin P60 inhibits cell proliferation but enhances cell migration. It promotes cell migration in breast cancer where high ketanin p60 expression in tumor tissue is correlated with lymph node metastasis and poor overall survival. Katanin p60 may also be a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer. Katanin is a heterodimer with an AAA catalytic subunit katanin P60 and a non-AAA subunit katanin P80. In ASPM (known as Asp in fly and ASPM-1 in worm), a microcephaly-associated protein family that regulates spindle architecture, the N-terminal domain of katanin p60 subunit (kp60-NTD) and C-terminal domain of katanin p80 subunit form a heterodimer, which then binds conserved motifs in ASPM, thus forming a complex that controls microtubule disassembly at spindle poles; misregulation of this process can lead to microcephaly. p60 katanin-like 1 has been shown to be predominantly enriched within oocytes and ovaries, and essential for oocyte meiosis and maturation. The N-terminal domain of mouse katanin p60 (kp60-NTD) also binds to tubulin; structure studies of kp60-NTD reveal a striking similarity to the microtubule interacting and trafficking (MIT) domains, although their sequence similarities are low.


Pssm-ID: 439297  Cd Length: 69  Bit Score: 133.47  E-value: 3.37e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55925351   5 EICDNAKKGREYALLGNYDSSMVYYQGVIQQIHKHCQSLRDPAQKVKWQQVRQELAEEYEQVKSIVST 72
Cdd:cd21748   2 EICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 207-374 1.27e-36

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: 132.91  E-value: 1.27e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFK--GIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQhlGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 285 KLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSdEHEASRRVKSELLVQMDGVGgaqESEDPSKMVMVLAATNFPWDIDE 364
Cdd:cd19518  80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESA-QREMERRIVSQLLTCMDELN---NEKTAGGPVLVIGATNRPDSLDP 155

                       170
                ....*....|..
gi 55925351 365 ALRR--RLEKRI 374
Cdd:cd19518 156 ALRRagRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 214-375 4.56e-36

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: 131.01  E-value: 4.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 214 AKKLLREAVVLPMWMPDFFKGIR-RPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFE 292
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPlRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 293 MARFYAPTTIFIDEIDSICGRRGtSDEHEASRRVKSELLVQMDGVGGAQEsedpskmVMVLAATNFPWDIDEALRR--RL 370
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRG-HDSTGVTDRVVNQLLTQLDGVEGLDG-------VYVLAATSRPDLIDPALLRpgRL 152


                ....*
gi 55925351 371 EKRIY 375
Cdd:cd19526 153 DKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 215-376 1.45e-34

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: 127.24  E-value: 1.45e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 215 KKLLREAVVLPMWMPDFF-KGIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEM 293
Cdd:cd19527   2 KKEILDTIQLPLEHPELFsSGLRKR-SGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 294 ARFYAPTTIFIDEIDSICGRRGTS-DEHEASRRVKSELLVQMDGVGGAQESedpskmVMVLAATNFPWDIDEALRR--RL 370
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMSSSGQD------VFVIGATNRPDLLDPALLRpgRF 154


                ....*.
gi 55925351 371 EKRIYI 376
Cdd:cd19527 155 DKLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 207-375 6.10e-32

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: 120.31  E-value: 6.10e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLLREAVVLPMWMPDFFKGIR-RPWKGVLMVGPPGTGKTMLAKAVATECGT-----TFFNVSSSTLTSKYR 280
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 281 GESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVkSELLVQMDGVGGAQEsedpskmVMVLAATNFPW 360
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIV-STLLALMDGLDNRGQ-------VVVIGATNRPD 152

                       170
                ....*....|....*..
gi 55925351 361 DIDEALRR--RLEKRIY 375
Cdd:cd19517 153 ALDPALRRpgRFDREFY 169
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 209-378 6.25e-26

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: 102.99  E-value: 6.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 209 ADLEDAKKLLREAVvlpmwmpdffkgIRRPWKGVLMVGPPGTGKTMLAKAVATEC---GTTFFNVSSSTLTSKYRGESEK 285
Cdd:cd00009   1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 286 ---LVRLLFEMARFYAPTTIFIDEIDSIcgrrgtsdeheaSRRVKSELLVQMDGVGGAQESEDPskmVMVLAATNFPW-- 360
Cdd:cd00009  69 ghfLVRLLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLETLNDLRIDREN---VRVIGATNRPLlg 133

                       170
                ....*....|....*...
gi 55925351 361 DIDEALRRRLEKRIYIPL 378
Cdd:cd00009 134 DLDRALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 238-380 7.24e-18

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: 80.50  E-value: 7.24e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351    238 PWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYAPT 300
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351    301 TIFIDEIDSICgrrgtsdeheasrRVKSELLVQMDGVGGAQESEDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 379
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147


                   .
gi 55925351    380 T 380
Cdd:smart00382 148 L 148
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 240-376 1.99e-17

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: 79.84  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 240 KGVLMVGPPGTGKTMLAKAVAtecgtTFFN------VSSSTLTSKYRGESEKLVRLLFEMA----RFYAPTT----IFID 305
Cdd:cd19504  36 KGILLYGPPGTGKTLMARQIG-----KMLNarepkiVNGPEILNKYVGESEANIRKLFADAeeeqRRLGANSglhiIIFD 110

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55925351 306 EIDSICGRRGTS-DEHEASRRVKSELLVQMDGVggaqeseDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYI 376
Cdd:cd19504 111 EIDAICKQRGSMaGSTGVHDTVVNQLLSKIDGV-------EQLNNILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 207-357 2.21e-17

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: 79.33  E-value: 2.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 207 DIADLEDAKKLL--REAVVLPmwmPDFFKGIRRPwKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESE 284
Cdd:cd19507   1 DVGGLDNLKDWLkkRKAAFSK---QASAYGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55925351 285 KLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDEHEASRRVKSELLVQMdgvggaQESEDPskmVMVLAATN 357
Cdd:cd19507  77 SRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWL------QEKKKP---VFVVATAN 140
ycf46 CHL00195
Ycf46; Provisional
 240-418 5.48e-13

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 70.82  E-value: 5.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  240 KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTSDE 319
Cdd:CHL00195 260 RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGD 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  320 HEASRRVKSELLVQMdgvggaqeSEDPSKMVMVLAATNFPWDIDEALRR-RLEKRIYIPLPTAKGRAELLKINLREV--D 396
Cdd:CHL00195 340 SGTTNRVLATFITWL--------SEKKSPVFVVATANNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKFrpK 411

                        170       180
                 ....*....|....*....|..
gi 55925351  397 VASDVDLTVFAEKIEGYSGADI 418
Cdd:CHL00195 412 SWKKYDIKKLSKLSNKFSGAEI 433
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 400-444 2.22e-12

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: 61.40  E-value: 2.22e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 55925351   400 DVDLTVFAEKIEGYSGADITNVCRDASMMAMRRRIQGLSPEEIRA 444
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 240-374 3.95e-12

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: 64.09  E-value: 3.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 240 KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGES--EKLVRLLFEMARFYAPTTIFIDEIDSICGRRGTS 317
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 55925351 318 DEHEAS-RRVKSELLVQMdgvggaqESEDPSKMVMVLAATNFPWDIDEALRRRLEKRI 374
Cdd:cd19506 107 TEKQLDpKRLKKDLPKIL-------KSLKPEDRVLIVGTTSRPFEADLKSFCKVYNKI 157
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 242-376 1.10e-10

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: 60.92  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 242 VLMVGPPGTGKTMLAKAVATECG---------TTFFNVSSSTLTSKYRGESEKLVRLLF----EMARFY-APTTIFIDEI 307
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKdALVFVLIDEV 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55925351 308 DSICGRRGTS---DEHEASRRVKSELLVQMDGVggaqESEDPskmVMVLAATNFPWDIDEALRRRLEKRIYI 376
Cdd:cd19508 135 ESLAAARSASssgTEPSDAIRVVNAVLTQIDRI----KRYHN---NVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 229-376 5.78e-10

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: 57.75  E-value: 5.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 229 PDFFKGIRRPWK-GVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTltskyRGESEKLVRLLfeMARFYAPTTIFIDEI 307
Cdd:cd19510  12 EDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDI 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55925351 308 D-SICGRRGTSDEHEA----SRRVKSELLVQMDGVGGAQESedpskmvMVLAATNFPWDIDEALRR--RLEKRIYI 376
Cdd:cd19510  85 DaAFESREHNKKNPSAygglSRVTFSGLLNALDGVASSEER-------IVFMTTNHIERLDPALIRpgRVDMKIYM 153
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 448-486 2.00e-09

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 53.65  E-value: 2.00e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 55925351   448 DELQMP-VTMEDFELALKKISKSVSAADLEKYESWMSEFG 486
Cdd:pfam09336  22 DKLLEPpVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 236-374 4.43e-09

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: 55.23  E-value: 4.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 236 RRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEmarfYAPTT-----IFIDEIDSI 310
Cdd:cd19512  19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFD----WANTSrrgllLFVDEADAF 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55925351 311 CGRRGTSDEHEASRRVKSELLVQMdgvggaqeSEDPSKMVMVLaATNFPWDIDEALRRRLEKRI 374
Cdd:cd19512  94 LRKRSTEKISEDLRAALNAFLYRT--------GEQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 240-336 4.42e-08

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: 53.15  E-value: 4.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 240 KGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTS-KYRG-ESEKLVRLLFEmarfyapTTIFIDEIDSICGRRGTS 317
Cdd:cd19498  47 KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGSS 119

                        90       100
                ....*....|....*....|
gi 55925351 318 DeHEASRR-VKSELLVQMDG 336
Cdd:cd19498 120 G-PDVSREgVQRDLLPIVEG 138
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
240-290 8.53e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.12  E-value: 8.53e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 55925351 240 KGVLMVGPPGTGKTMLAKAVATECG--TTFFNVSSSTLTSKYRGESEKLVRLL 290
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEIYSAELKKTEFLMQAL 117
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 242-390 2.15e-06

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: 49.40  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 242 VLMVGPPGTGKTMLAKAVATECGTTFFNVS-SSTL-------TSKYRGESEKLV---RLLFEmarfyapTTIFIDEIDsi 310
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQfTPDLlpsdilgTYIYDQQTGEFEfrpGPLFA-------NVLLADEIN-- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 311 cgRrgtsdeheASRRVKSELLVQMD----GVGGaqESEDPSKMVMVLAATNfPWDID------EALRRRLEKRIYIPLPT 380
Cdd:COG0714 105 --R--------APPKTQSALLEAMEerqvTIPG--GTYKLPEPFLVIATQN-PIEQEgtyplpEAQLDRFLLKLYIGYPD 171

                       170
                ....*....|
gi 55925351 381 akgRAELLKI 390
Cdd:COG0714 172 ---AEEEREI 178
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 243-393 5.94e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 48.69  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   243 LMVGPPGTGKTMLAKAVATE-CGTTFF------NVSSSTLTSKYRGESEKLVRLLFEMArfyAPTTIFIDEIDSICGRR- 314
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLGVLrkplvrEVSRADLIGQYIGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGy 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   315 GTSDEHEASrrVKSELLVQMDG------VGGAQESEDPSKMVmvlaatnfpwDIDEALRRRLEKRIYIPLPTAkgrAELL 388
Cdd:TIGR03922 393 GQKDPFGLE--AIDTLLARMENdrdrlvVIGAGYRKDLDKFL----------EVNEGLRSRFTRVIEFPSYSP---DELV 457


                  ....*
gi 55925351   389 KINLR 393
Cdd:TIGR03922 458 EIARR 462
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 212-310 1.43e-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: 46.44  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 212 EDAKKLLREAVVlpmwmpDFFKGIRRPWKG-----------VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLT-SKY 279
Cdd:cd19497  18 ERAKKVLSVAVY------NHYKRIRNNLKQkdddveleksnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 55925351 280 RGESEK--LVRLL----FEMARfyAPTTI-FIDEIDSI 310
Cdd:cd19497  92 VGEDVEniLLKLLqaadYDVER--AQRGIvYIDEIDKI 127
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 246-307 2.03e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 46.97  E-value: 2.03e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55925351 246 GPPGTGKTMLAKAVATECGTTFFNVsSSTLTSKyrgeseKLVRLLFEMARFYA----PTTIFIDEI 307
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVAL-SAVTSGV------KDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 246-307 2.23e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 46.62  E-value: 2.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55925351  246 GPPGTGKTMLAKAVATECGTTFFNVsSSTLTSKyrgeseKLVRLLFEMA---RFYAPTTI-FIDEI 307
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEAL-SAVTSGV------KDLREVIEEArqrRSAGRRTIlFIDEI 101
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 242-261 2.57e-05

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 46.57  E-value: 2.57e-05
                        10        20
                ....*....|....*....|
gi 55925351 242 VLMVGPPGTGKTMLAKAVAT 261
Cdd:COG0606 214 LLMIGPPGSGKTMLARRLPG 233
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 238-366 7.01e-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: 43.13  E-value: 7.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 238 PWKGVLMVGPPGTGKTMLAKAVATEC--------------GTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 303
Cdd:cd19505  11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPCIIW 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55925351 304 IDEIDSICGRRGTSDEhEASRRVKSELLVQMDGVGGaqeSEDPSKMVMVLAATNFPWDIDEAL 366
Cdd:cd19505  91 IPNIHELNVNRSTQNL-EEDPKLLLGLLLNYLSRDF---EKSSTRNILVIASTHIPQKVDPAL 149
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 242-311 8.37e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 42.95  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   242 VLMVGPPGTGKTMLAKAVA-----TECGTTFFNVSS---STLTSKYRGESEKLVR-----LLFEMARFYAPTTIFIDEID 308
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgDERALIRIDMSEymeEHSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85


                  ...
gi 55925351   309 SIC 311
Cdd:pfam07724  86 KAH 88
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 242-261 1.00e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 43.29  E-value: 1.00e-04
                          10        20
                  ....*....|....*....|
gi 55925351   242 VLMVGPPGTGKTMLAKAVAT 261
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
PRK04195 PRK04195
replication factor C large subunit; Provisional
 206-262 1.05e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.53  E-value: 1.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55925351  206 DDIADLEDAKKLLREavvlpmWMPDFFKGirRPWKGVLMVGPPGTGKTMLAKAVATE 262
Cdd:PRK04195  14 SDVVGNEKAKEQLRE------WIESWLKG--KPKKALLLYGPPGVGKTSLAHALAND 62
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 240-285 1.06e-04

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: 44.22  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 55925351   240 KGVLMVGPPGTGKTMLAKAVATECG--TTFFNVSSSTLtskYRGESEK 285
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV---YSLEMKK 95
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 241-370 2.41e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 41.12  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351   241 GVLMVGPPGTGKTMLAK--AVATECGTTFF-----NVSSSTLTSKYR---GESEKLVRLLFEMARfyAPTTIFIDEIDsi 310
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNidpGGASWVDGPLVRAAR--EGEIAVLDEIN-- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55925351   311 cgrrgtsdehEASRRVKSEL--------LVQMDGVGgaqESEDPSKMVMVLAATNFP----WDIDEALRRRL 370
Cdd:pfam07728  77 ----------RANPDVLNSLlsllderrLLLPDGGE---LVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 243-371 5.39e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.00  E-value: 5.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 243 LMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLtskyRGESE--------------KLVRLLFEmARFYAPtTIFIDEID 308
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGV----RDEAEirghrrtyvgampgRIIQALKK-AGTNNP-VFLLDEID 114

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55925351 309 SIcGRRGTSDEHEAsrrvkseLLVQMDgvgGAQESE----------DPSKmVMVLAATNFPWDIDEALRRRLE 371
Cdd:cd19500 115 KI-GSSFRGDPASA-------LLEVLD---PEQNSTfsdhyldvpfDLSK-VLFIATANSLDTIPGPLLDRME 175
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
242-307 7.76e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 7.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55925351  242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLtskyrgesEK---LVRLLfemarfyapTTI------FIDEI 307
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL--------EKpgdLAAIL---------TNLeegdvlFIDEI 111
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
242-310 8.19e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 41.68  E-value: 8.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  242 VLMVGPPGTGKTMLAKAVAtecgtTFFNV-----SSSTLT-SKYRGES-EK-LVRLL----FEMARfyAPTTI-FIDEID 308
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLA-----RILDVpfaiaDATTLTeAGYVGEDvENiLLKLLqaadYDVEK--AQRGIvYIDEID 183


                 ..
gi 55925351  309 SI 310
Cdd:PRK05342 184 KI 185
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 242-307 9.15e-04

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 39.78  E-value: 9.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55925351  242 VLMVGPPGTGKTMLAKAVATECGTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYAPTTIFIDEI 307
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINVNLElsrrllELPEKQR--ALRAPRLLDEIAEKSSGDVVLLDNI 88
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
240-263 1.52e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 1.52e-03
                        10        20
                ....*....|....*....|....
gi 55925351 240 KGVLMVGPPGTGKTMLAKAVATEC 263
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEA 123
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 242-310 1.98e-03

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.42  E-value: 1.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 242 VLMVGPPGTGKTMLAK----------AVA-----TECGttffnvssstltskYRGES-EK-LVRLL----FEMARfyAPT 300
Cdd:COG1219 112 ILLIGPTGSGKTLLAQtlarildvpfAIAdattlTEAG--------------YVGEDvENiLLKLLqaadYDVEK--AER 175

                        90
                ....*....|.
gi 55925351 301 TI-FIDEIDSI 310
Cdd:COG1219 176 GIiYIDEIDKI 186
44 PHA02544
clamp loader, small subunit; Provisional
 220-369 5.82e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.82  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  220 EAVVLPMWMPDFFKGIRRpwKG-----VLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKY-RGEsekLVRLLFEM 293
Cdd:PHA02544  21 DECILPAADKETFKSIVK--KGripnmLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFvRNR---LTRFASTV 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55925351  294 ARFYAPTTIFIDEIDsicgRRGTSDEHEASRRVksellvqmdgvggaqeSEDPSKMVMVLAATNFPWDIDEALRRR 369
Cdd:PHA02544  96 SLTGGGKVIIIDEFD----RLGLADAQRHLRSF----------------MEAYSKNCSFIITANNKNGIIEPLRSR 151
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 236-312 6.64e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.05  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351  236 RRPWKGVLMVGPPGTGKTMLAKAVA------------TECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 303
Cdd:PRK11034 204 RRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILF 283


                 ....*....
gi 55925351  304 IDEIDSICG 312
Cdd:PRK11034 284 IDEIHTIIG 292
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 242-295 8.55e-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: 36.90  E-value: 8.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55925351   242 VLMVGPPGTGKTMLAKAVATECGTTFfnVSSSTLTSKYRGE-----------SEKLVRLLFEMAR 295
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVR--LSSDDERKRLFGEgrpsisyytdaTDRTYERLHELAR 64
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
 361-484 8.59e-03

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 38.40  E-value: 8.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 361 DIDEALRRRLEKRIYIPLPTAKGRAELlKINLREVDVAsdVDLTVFA-------------EKIEGYSGA--DITNVcrda 425
Cdd:COG1527 143 SVEELVEALEGTPYYEALEEALEEYEE-TGDLFPIENA--LDRAYYEnllelakkkgkdrKLLLEYLGTeiDLLNL---- 215

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55925351 426 sMMAMRRRIQGLSPEEIRA--------LSKDELQMPVTMEDFELALKKISKSVSAADLEKYESWMSE 484
Cdd:COG1527 216 -RTILRLKRYGLSPEEIEAylipggyrISEKELKELAEAEDVEELLEALEGTPYGKLLSELEELEET 281
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
242-373 8.89e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 8.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55925351 242 VLMVGPPGTGKTMLAKAVATECGTTFFNV---------SSSTLTSKYRGESEKLVRLLFEMARFYApttifideidsicg 312
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRSdvvrkrlfgAGLAPLERSPEATARTYARLLALARELL-------------- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55925351 313 RRGTSdeheasrrvksellVQMDGVGGAQESEDpsKMVMVLAATNFPWDI------DEALRRRLEKR 373
Cdd:COG0645  68 AAGRS--------------VILDATFLRRAQRE--AFRALAEEAGAPFVLiwldapEEVLRERLEAR 118
 
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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