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Conserved domains on  [gi|530383329|ref|XP_005266861|]
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katanin p60 ATPase-containing subunit A1 isoform X1 [Homo sapiens]

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 ...
 210-379 3.36e-129

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: 372.01  E-value: 3.36e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 530383329 370 RRRLEKRIYI 379
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 2.01e-33

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: 120.76  E-value: 2.01e-33
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383329   5 MISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKT 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 ...
 403-447 2.00e-13

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: 64.48  E-value: 2.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530383329  403 DVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRN 447
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 ...
 451-489 7.66e-08

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: 49.03  E-value: 7.66e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530383329  451 EEMHMPT-TMEDFEMALKKVSKSVSAADIERYEKWIFEFG 489
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 ...
 210-379 3.36e-129

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: 372.01  E-value: 3.36e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 530383329 370 RRRLEKRIYI 379
Cdd:cd19522  161 RRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 149-472 3.77e-98

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 298.84  E-value: 3.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 149 GKAVRCREKKEQNKGREEKNKSPAAVTEPETNKF-DSTGYDKDLVEALERdiisqnPNVRWDDIADLVEAKKLLKEAVVL 227
Cdd:COG1222   23 ERLGVELALLLQPVKALELLEEAPALLLNDANLTqKRLGTPRGTAVPAES------PDVTFDDIGGLDEQIEEIREAVEL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 228 PMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATI 305
Cdd:COG1222   97 PLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSII 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 306 FIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVggtsendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPS 383
Cdd:COG1222  176 FIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 384 AKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLtpeeirnlskeemhmptTMEDFE 463
Cdd:COG1222  249 EEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV-----------------TMEDLE 311


                 ....*....
gi 530383329 464 MALKKVSKS 472
Cdd:COG1222  312 KAIEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 189-489 2.88e-80

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: 264.46  E-value: 2.88e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  189 KDLVEALE-------RDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLA 259
Cdd:TIGR01243 426 KDFMEALKmvepsaiREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  260 KAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDG 339
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  340 VggtsendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYS 417
Cdd:TIGR01243 585 I-------QELSNVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383329  418 GADITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMH-MPTTMEDFEMALKKVSKSVSAADIERYEKWIFEFG 489
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 191-471 7.83e-78

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 248.59  E-value: 7.83e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 191 LVEALErdiISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKT 268
Cdd:PRK03992 116 RVQAME---VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNA 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 269 TFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRVkAELLVQMDGVggtse 345
Cdd:PRK03992 192 TFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF----- 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 346 ndDPSKMVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADIT 422
Cdd:PRK03992 266 --DPRGNVKIIAATNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLK 342

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530383329 423 NVCRDASLMAMRRRiegltPEEIrnlskeemhmptTMEDFEMALKKVSK 471
Cdd:PRK03992 343 AICTEAGMFAIRDD-----RTEV------------TMEDFLKAIEKVMG 374
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 245-381 3.35e-54

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: 178.17  E-value: 3.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHE 324
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG-GDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530383329  325 ASRRVKAELLVQMDGVGGTSENddpskmVMVLAATNFPWDIDEALRRRLEKRIYIPL 381
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSK------VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 5-72 2.01e-33

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: 120.76  E-value: 2.01e-33
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383329   5 MISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKT 72
Cdd:cd21748    2 EICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 241-382 3.43e-17

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: 78.57  E-value: 3.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329   241 PWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYSPA 303
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329   304 TIFIDEIDSICsrrgtseeheasrRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 382
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 403-447 2.00e-13

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: 64.48  E-value: 2.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530383329  403 DVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRN 447
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 451-489 7.66e-08

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: 49.03  E-value: 7.66e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530383329  451 EEMHMPT-TMEDFEMALKKVSKSVSAADIERYEKWIFEFG 489
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 ...
 245-310 5.54e-03

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: 37.47  E-value: 5.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383329 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYSPATIFIDEI 310
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 ...
 210-379 3.36e-129

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: 372.01  E-value: 3.36e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 530383329 370 RRRLEKRIYI 379
Cdd:cd19522  161 RRRLEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 149-472 3.77e-98

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 298.84  E-value: 3.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 149 GKAVRCREKKEQNKGREEKNKSPAAVTEPETNKF-DSTGYDKDLVEALERdiisqnPNVRWDDIADLVEAKKLLKEAVVL 227
Cdd:COG1222   23 ERLGVELALLLQPVKALELLEEAPALLLNDANLTqKRLGTPRGTAVPAES------PDVTFDDIGGLDEQIEEIREAVEL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 228 PMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATI 305
Cdd:COG1222   97 PLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSII 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 306 FIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVggtsendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPS 383
Cdd:COG1222  176 FIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-------ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 384 AKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLtpeeirnlskeemhmptTMEDFE 463
Cdd:COG1222  249 EEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV-----------------TMEDLE 311


                 ....*....
gi 530383329 464 MALKKVSKS 472
Cdd:COG1222  312 KAIEKVKKK 320
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 211-379 5.03e-94

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: 281.93  E-value: 5.03e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 211 IADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLV 290
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 291 RLLFEMARFYSPATIFIDEIDSICSRRGtSEEHEASRRVKAELLVQMDGVGgtsenDDPSKMVMVLAATNFPWDIDEALR 370
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERG-SGEHEASRRVKTEFLVQMDGVL-----NKPEDRVLVLGATNRPWELDEAFL 154


                 ....*....
gi 530383329 371 RRLEKRIYI 379
Cdd:cd19509  155 RRFEKRIYI 163
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 189-489 2.88e-80

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: 264.46  E-value: 2.88e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  189 KDLVEALE-------RDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLA 259
Cdd:TIGR01243 426 KDFMEALKmvepsaiREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLA 504

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  260 KAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDG 339
Cdd:TIGR01243 505 KAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDG 584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  340 VggtsendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYS 417
Cdd:TIGR01243 585 I-------QELSNVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYT 657

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383329  418 GADITNVCRDASLMAMRRRIEGLTPEEIRNLSKEEMH-MPTTMEDFEMALKKVSKSVSAADIERYEKWIFEFG 489
Cdd:TIGR01243 658 GADIEAVCREAAMAALRESIGSPAKEKLEVGEEEFLKdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 204-379 4.80e-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: 246.31  E-value: 4.80e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 204 PNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYR 283
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 284 GESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEhEASRRVKAELLVQMDGVGGTSENddpskmVMVLAATNFPW 363
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGES-EASRRIKTELLVQMNGVGNDSQG------VLVLGATNIPW 154

                        170
                 ....*....|....*.
gi 530383329 364 DIDEALRRRLEKRIYI 379
Cdd:cd19521  155 QLDSAIRRRFEKRIYI 170
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 191-471 7.83e-78

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 248.59  E-value: 7.83e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 191 LVEALErdiISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKT 268
Cdd:PRK03992 116 RVQAME---VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNA 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 269 TFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRVkAELLVQMDGVggtse 345
Cdd:PRK03992 192 TFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF----- 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 346 ndDPSKMVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADIT 422
Cdd:PRK03992 266 --DPRGNVKIIAATNRI-DIlDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLK 342

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530383329 423 NVCRDASLMAMRRRiegltPEEIrnlskeemhmptTMEDFEMALKKVSK 471
Cdd:PRK03992 343 AICTEAGMFAIRDD-----RTEV------------TMEDFLKAIEKVMG 374
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 198-469 3.13e-76

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: 244.82  E-value: 3.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 198 DIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSS 275
Cdd:COG0464  146 EELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 276 STLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHeASRRVKAELLVQMDGVggtseNDDpskmVMV 355
Cdd:COG0464  225 SDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL-----RSD----VVV 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 356 LAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRr 435
Cdd:COG0464  295 IAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR- 373

                        250       260       270
                 ....*....|....*....|....*....|....
gi 530383329 436 riegltpeeirnlskeEMHMPTTMEDFEMALKKV 469
Cdd:COG0464  374 ----------------LGREPVTTEDLLEALERE 391
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 188-379 4.19e-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: 234.50  E-value: 4.19e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 188 DKDLVEALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECK 267
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 268 TTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRVKAELLVQMDGVggtseND 347
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-EHESSRRIKTEFLVQLDGA-----TT 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 530383329 348 DPSKMVMVLAATNFPWDIDEALRRRLEKRIYI 379
Cdd:cd19525  155 SSEDRILVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 210-379 1.62e-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: 203.54  E-value: 1.62e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 290 VRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRVKAELLVQMDGVGGtsendDPSKMVMVLAATNFPWDIDEAL 369
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEG-EHEASRRLKTEFLIEFDGVQS-----NGDDRVLVMGATNRPQELDDAV 154

                        170
                 ....*....|
gi 530383329 370 RRRLEKRIYI 379
Cdd:cd19524  155 LRRFTKRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 193-472 4.25e-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: 215.54  E-value: 4.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  193 EALERDIISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTF 270
Cdd:TIGR01243 162 KPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAGAYF 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  271 FNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRgtsEE--HEASRRVKAELLVQMDGVGGTSEndd 348
Cdd:TIGR01243 241 ISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR---EEvtGEVEKRVVAQLLTLMDGLKGRGR--- 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  349 pskmVMVLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCR 426
Cdd:TIGR01243 315 ----VIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAK 390

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 530383329  427 DASLMAMRRRI-EGLTPEEIRNLSKEEM-HMPTTMEDFEMALKKVSKS 472
Cdd:TIGR01243 391 EAAMAALRRFIrEGKINFEAEEIPAEVLkELKVTMKDFMEALKMVEPS 438
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 217-379 1.71e-54

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: 179.79  E-value: 1.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 217 AKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLF 294
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 295 EMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGgtsenddPSKMVMVLAATNFPWDIDEALRR--R 372
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIE-------SLKGVVVIAATNRPDMIDPALLRpgR 152


                 ....*..
gi 530383329 373 LEKRIYI 379
Cdd:cd19511  153 LDKLIYV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 245-381 3.35e-54

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: 178.17  E-value: 3.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHE 324
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG-GDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530383329  325 ASRRVKAELLVQMDGVGGTSENddpskmVMVLAATNFPWDIDEALRRRLEKRIYIPL 381
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSK------VIVIAATNRPDKLDPALLGRFDRIIEFPL 130
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
202-469 1.59e-53

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 189.48  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 202 QNPNVRWDDIADLVEAKKLLKEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNV 273
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIV-------DFLKdpekftrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 274 SSSTLTSKY------RgeseklVRLLFEMARFYSPATIFIDEIDSICSRRGTS-----EEHE----AsrrvkaeLLVQMD 338
Cdd:COG0465  207 SGSDFVEMFvgvgasR------VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghDEREqtlnQ-------LLVEMD 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 339 GVgGTSENddpskmVMVLAATNFPwDI-DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEG 415
Cdd:COG0465  274 GF-EGNEG------VIVIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPG 345

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530383329 416 YSGADITNVCRDASLMAMRRRiegltpeeirnlsKEEMhmptTMEDFEMALKKV 469
Cdd:COG0465  346 FSGADLANLVNEAALLAARRN-------------KKAV----TMEDFEEAIDRV 382
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 210-379 3.52e-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: 176.71  E-value: 3.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRVKAELLVQMDGVggtsendDPSKMVMVLAATNFPWDIDE 367
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERRVVAQLLTLMDGM-------SSRGKVVVIAATNRPDAIDP 151

                        170
                 ....*....|....
gi 530383329 368 ALRR--RLEKRIYI 379
Cdd:cd19503  152 ALRRpgRFDREVEI 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 210-379 9.28e-52

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: 172.99  E-value: 9.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIR--RPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRgTSEEHEASRRVKAELLVQMDGVggtseNDDPSKMVMVLAATNFPWDIDE 367
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGL-----STDGNCRVIVMGATNRPQDLDE 154

                        170
                 ....*....|..
gi 530383329 368 ALRRRLEKRIYI 379
Cdd:cd19520  155 AILRRMPKRFHI 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 217-379 2.52e-51

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: 171.70  E-value: 2.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 217 AKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEM 296
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 297 ARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVGGTSEnddpskmVMVLAATNFPWDIDEALRR--RLE 374
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSK-------VLVIAATNRPDLLDPALLRpgRFD 153


                 ....*
gi 530383329 375 KRIYI 379
Cdd:cd19481  154 EVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
243-480 4.71e-51

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 173.92  E-value: 4.71e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARfYSPATIFIDEIDSICSRRGTSEE 322
Cdd:COG1223   36 RKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQND 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 323 HEASRRVKAELLVQMDGvggtsendDPSKmVMVLAATNFPWDIDEALRRRLEKRIYIPLPSAKGREELLRISLRELELAD 402
Cdd:COG1223  115 VGEVKRVVNALLQELDG--------LPSG-SVVIAATNHPELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF 185

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383329 403 DVDLASIAENMEGYSGADITNVCRDaslmAMRRRIegltpeeirnlskEEMHMPTTMEDFEMALKKVSKSVSAADIER 480
Cdd:COG1223  186 ELDLKKLAKKLEGLSGADIEKVLKT----ALKKAI-------------LEDREKVTKEDLEEALKQRKERKKEPKKEG 246
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 204-469 3.12e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 177.27  E-value: 3.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 204 PNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSK 281
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDdiGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQK 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 282 YRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR--GTSEEHEASRRVKAELLVQMDGVggtsendDPSKMVMVLAAT 359
Cdd:PTZ00361 257 YLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDGF-------DSRGDVKVIMAT 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 360 NFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRi 437
Cdd:PTZ00361 330 NRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRER- 408

                        250       260       270
                 ....*....|....*....|....*....|..
gi 530383329 438 egltpeeirnlskeemHMPTTMEDFEMALKKV 469
Cdd:PTZ00361 409 ----------------RMKVTQADFRKAKEKV 424
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 200-463 8.23e-50

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 175.34  E-value: 8.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 200 ISQNPNVRWDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSST 277
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEqiGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 278 LTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEAsRRVKAELLVQMDGVggtsendDPSKMVM 354
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGADREV-QRILLELLNQMDGF-------DQTTNVK 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 355 VLAATNFPWDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMA 432
Cdd:PTZ00454 287 VIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQA 366

                        250       260       270
                 ....*....|....*....|....*....|.
gi 530383329 433 MRRRIEGLTPEEIRNLSKEemHMPTTMEDFE 463
Cdd:PTZ00454 367 VRKNRYVILPKDFEKGYKT--VVRKTDRDYD 395
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 208-377 9.16e-49

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: 165.20  E-value: 9.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 208 WDDIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGE 285
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 286 SEKLVRLLFEMARFYSPATIFIDEIDSICSRR---GTSEEHEASRRVkAELLVQMDGVggtsendDPSKMVMVLAATNFP 362
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTM-LELLNQLDGF-------DPRGNIKVIMATNRP 152

                        170
                 ....*....|....*..
gi 530383329 363 WDIDEALRR--RLEKRI 377
Cdd:cd19502  153 DILDPALLRpgRFDRKI 169
ftsH CHL00176
cell division protein; Validated
 206-445 1.69e-46

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 171.00  E-value: 1.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 206 VRWDDIADLVEAKKLLKEAVVLpMWMPEFFKGI-RRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRG 284
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 285 ESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGT--SEEHEASRRVKAELLVQMDGVGGTsenddpsKMVMVLAATNFP 362
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDEREQTLNQLLTEMDGFKGN-------KGVIVIAATNRV 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 363 WDIDEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGL 440
Cdd:CHL00176 332 DILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATI 411


                 ....*
gi 530383329 441 TPEEI 445
Cdd:CHL00176 412 TMKEI 416
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 217-379 3.35e-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: 155.35  E-value: 3.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 217 AKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLF 294
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 295 EMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMDGVggtsendDPSKMVMVLAATNFPWDIDEALRR--R 372
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-------EEMNGVVVIAATNRPDIIDPALLRagR 152


                 ....*..
gi 530383329 373 LEKRIYI 379
Cdd:cd19529  153 FDRLIYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
210-437 3.46e-44

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 164.82  E-value: 3.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEY-LREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRGT--SEEHEASRRVKAELLVQMDGVGGtsenddpSKMVMVLAATNFPWDI 365
Cdd:PRK10733 231 SRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFEG-------NEGIIVIAATNRPDVL 303

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383329 366 DEALRR--RLEKRIYIPLPSAKGREELLRISLRELELADDVDLASIAENMEGYSGADITNVCRDASLMAMR--RRI 437
Cdd:PRK10733 304 DPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARgnKRV 379
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 210-380 3.05e-43

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 150.66  E-value: 3.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESE 287
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKaiGIKPP-RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 288 KLVRLLFEMARFYSPATIFIDEIDSICSRRGTSeEHEASRRVKAELLVQMDGVGGTSEnddpskmVMVLAATNFPWDIDE 367
Cdd:cd19519   80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT-HGEVERRIVSQLLTLMDGLKQRAH-------VIVMAATNRPNSIDP 151

                        170
                 ....*....|....*
gi 530383329 368 ALRR--RLEKRIYIP 380
Cdd:cd19519  152 ALRRfgRFDREIDIG 166
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 206-379 1.52e-41

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: 146.22  E-value: 1.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 206 VRWDDIADLVEAKKLLKEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSST 277
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVV-------EFLKnpekftklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 278 LTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGT--SEEHEASRRVKAELLVQMDGVGGTSEnddpskmVMV 355
Cdd:cd19501   73 FVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglGGGHDEREQTLNQLLVEMDGFESNTG-------VIV 145

                        170       180
                 ....*....|....*....|....*.
gi 530383329 356 LAATNFPWDIDEALRR--RLEKRIYI 379
Cdd:cd19501  146 IAATNRPDVLDPALLRpgRFDRQVYV 171
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 218-379 5.91e-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: 5.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 218 KKLLKEAVVLPMWMPE-FFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEM 296
Cdd:cd19528    2 KRELQELVQYPVEHPDkFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 297 ARFYSPATIFIDEIDSICSRRGTS--EEHEASRRVKAELLVQMDGVggtsendDPSKMVMVLAATNFPWDIDEALRR--R 372
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNigDAGGAADRVINQILTEMDGM-------NTKKNVFIIGATNRPDIIDPAILRpgR 154


                 ....*..
gi 530383329 373 LEKRIYI 379
Cdd:cd19528  155 LDQLIYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 214-379 1.10e-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: 141.09  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 214 LVEAKKLLKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVR 291
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 292 LLFEMARFYSPATIFIDEIDSICSRRGtSEEHEASRRVKAELLVQMDGVGGTSEnddpskmVMVLAATNFPWDIDEALRR 371
Cdd:cd19530   80 QVFQRARASAPCVIFFDEVDALVPKRG-DGGSWASERVVNQLLTEMDGLEERSN-------VFVIAATNRPDIIDPAMLR 151

                        170
                 ....*....|
gi 530383329 372 --RLEKRIYI 379
Cdd:cd19530  152 pgRLDKTLYV 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 210-379 2.20e-39

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: 140.02  E-value: 2.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKL 289
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 290 VRLLFEMARFYSPATIFIDEIDSICSRRgtSEEHEASRRVKAELLVQMDGVGGTSENDdpskmVMVLAATNFPWDIDEAL 369
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQ--DDEASPVGRLQVELLAQLDGVLGSGEDG-----VLVVCTTSKPEEIDESL 153

                        170
                 ....*....|
gi 530383329 370 RRRLEKRIYI 379
Cdd:cd19523  154 RRYFSKRLLV 163
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 221-377 5.48e-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: 131.37  E-value: 5.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 221 LKEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMAR 298
Cdd:cd19518   12 LCELLIHPILPPEYFQhlGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEKIRELFDQAI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 299 FYSPATIFIDEIDSICSRRGTSEEhEASRRVKAELLVQMDGVGGTSENDDPskmVMVLAATNFPWDIDEALRR--RLEKR 376
Cdd:cd19518   91 SNAPCIVFIDEIDAITPKRESAQR-EMERRIVSQLLTCMDELNNEKTAGGP---VLVIGATNRPDSLDPALRRagRFDRE 166


                 .
gi 530383329 377 I 377
Cdd:cd19518  167 I 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 217-378 2.29e-35

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: 129.09  E-value: 2.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 217 AKKLLKEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFE 295
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPlRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 296 MARFYSPATIFIDEIDSICSRRGtseeHEAS---RRVKAELLVQMDGVGGTsenddpsKMVMVLAATNFPWDIDEALRR- 371
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRG----HDSTgvtDRVVNQLLTQLDGVEGL-------DGVYVLAATSRPDLIDPALLRp 149


                 ....*...
gi 530383329 372 -RLEKRIY 378
Cdd:cd19526  150 gRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 218-379 4.28e-35

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: 128.40  E-value: 4.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 218 KKLLKEAVVLPMWMPEFF-KGIRRPwKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEM 296
Cdd:cd19527    2 KKEILDTIQLPLEHPELFsSGLRKR-SGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 297 ARFYSPATIFIDEIDSICSRRGTS-EEHEASRRVKAELLVQMDGVGGTSENddpskmVMVLAATNFPWDIDEALRR--RL 373
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMSSSGQD------VFVIGATNRPDLLDPALLRpgRF 154


                 ....*.
gi 530383329 374 EKRIYI 379
Cdd:cd19527  155 DKLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 210-378 2.78e-34

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 126.86  E-value: 2.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 210 DIADLVEAKKLLKEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATEC-----KTTFFNVSSSTLTSKYR 283
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 284 GESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVkAELLVQMDGVGGTSEnddpskmVMVLAATNFPW 363
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIV-STLLALMDGLDNRGQ-------VVVIGATNRPD 152

                        170
                 ....*....|....*..
gi 530383329 364 DIDEALRR--RLEKRIY 378
Cdd:cd19517  153 ALDPALRRpgRFDREFY 169
Kp60-NTD cd21748
N-terminal domain (NTD) found in katanin p60 (Kp60) ATPase-containing subunit A1, and similar ...
 5-72 2.01e-33

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: 120.76  E-value: 2.01e-33
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383329   5 MISENVKLAREYALLGNYDSAMVYYQGVLDQMNKYLYSVKDTYLQQKWQQVWQEINVEAKHVKDIMKT 72
Cdd:cd21748    2 EICENLKLAREYALLGNYDSALVYYQGVLQQINRYLRTIRDPSRKQKWQQVQQEIAEEYELVKDIQSE 69
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 239-381 1.65e-25

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: 101.84  E-value: 1.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 239 RRPWKGVLMVGPPGTGKTLLAKAVATEC---KTTFFNVSSSTLTSKYRGESEK---LVRLLFEMARFYSPATIFIDEIDS 312
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530383329 313 IcsrrgtseeheaSRRVKAELLVQMDGVggtSENDDPSKMVMVLAATNFPW--DIDEALRRRLEKRIYIPL 381
Cdd:cd00009   96 L------------SRGAQNALLRVLETL---NDLRIDRENVRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 243-379 1.82e-18

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: 82.92  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 243 KGVLMVGPPGTGKTLLAKAV-----ATECKTtffnVSSSTLTSKYRGESEKLVRLLFEMA----RFYSPAT----IFIDE 309
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqRRLGANSglhiIIFDE 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383329 310 IDSICSRRGTSEEHEA-SRRVKAELLVQMDGVggtsendDPSKMVMVLAATNFPWDIDEALRR--RLEKRIYI 379
Cdd:cd19504  112 IDAICKQRGSMAGSTGvHDTVVNQLLSKIDGV-------EQLNNILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 243-360 2.95e-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: 78.95  E-value: 2.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEE 322
Cdd:cd19507   32 KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGD 111

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530383329 323 HEASRRVKAELLVQMdgvggtSENDDPskmVMVLAATN 360
Cdd:cd19507  112 SGTSSRVLGTFLTWL------QEKKKP---VFVVATAN 140
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 241-382 3.43e-17

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: 78.57  E-value: 3.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329   241 PWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSS-----------------STLTSKYRGESEKLVRLLFEMARFYSPA 303
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329   304 TIFIDEIDSICsrrgtseeheasrRVKAELLVQMDGVGGTSENDDPSKMVMVLAATNFPWDIDEA-LRRRLEKRIYIPLP 382
Cdd:smart00382  81 VLILDEITSLL-------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
ycf46 CHL00195
Ycf46; Provisional
 197-421 4.99e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 77.37  E-value: 4.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 197 RDIISQ-------NPNVRWDDIADLVEAKKLLKEavvlpmwMPEFFK------GIRRPwKGVLMVGPPGTGKTLLAKAVA 263
Cdd:CHL00195 209 KQIISQteilefySVNEKISDIGGLDNLKDWLKK-------RSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIA 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 264 TECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIFIDEIDSICSRRGTSEEHEASRRVKAELLVQMdgvggt 343
Cdd:CHL00195 281 NDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVLATFITWL------ 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 344 SENDDPskmVMVLA-ATNFPWDIDEALRR-RLEKRIYIPLPSAKGREELLRISLREL--ELADDVDLASIAENMEGYSGA 419
Cdd:CHL00195 355 SEKKSP---VFVVAtANNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGA 431


                 ..
gi 530383329 420 DI 421
Cdd:CHL00195 432 EI 433
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 403-447 2.00e-13

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: 64.48  E-value: 2.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 530383329  403 DVDLASIAENMEGYSGADITNVCRDASLMAMRRRIEGLTPEEIRN 447
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 ...
 243-377 3.06e-11

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: 61.77  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 243 KGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRGES--EKLVRLLFEMARFYSPATIFIDEIDSICSRRGTS 320
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530383329 321 EEHEAS-RRVKAELLVQMdgvggtsENDDPSKMVMVLAATNFPWDIDEALRRRLEKRI 377
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 ...
 245-379 3.74e-11

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: 62.46  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 245 VLMVGPPGTGKTLLAKAVA---------TECKTTFFNVSSSTLTSKYRGESEKLVRLLF----EMARfYSPATIF--IDE 309
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELID-DKDALVFvlIDE 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383329 310 IDSICSRRGT----SEEHEASRRVKAeLLVQMDGVGGTSENddpskmvMVLAATNFPWDIDEALRRRLEKRIYI 379
Cdd:cd19508  134 VESLAAARSAsssgTEPSDAIRVVNA-VLTQIDRIKRYHNN-------VILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 189-339 1.64e-09

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: 57.00  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 189 KDLVEALERDIISQNpnvrwddiadlvEAKKLLkeAVVL-----PMWMPEFFKGIRRPwKGVLMVGPPGTGKTLLAKAVA 263
Cdd:cd19498    3 REIVSELDKYIIGQD------------EAKRAV--AIALrnrwrRMQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLA 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383329 264 TECKTTFFNVSSSTLTS-KYRG-ESEKLVRLLFEmarfyspATIFIDEIDSICSrRGTSEEHEASRR-VKAELLVQMDG 339
Cdd:cd19498   68 KLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAK-RGGSSGPDVSREgVQRDLLPIVEG 138
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 232-379 1.78e-08

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 53.51  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 232 PEFFKGIRRPWK-GVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTltskyRGESEKLVRLLfeMARFYSPATIFIDEI 310
Cdd:cd19510   12 EDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDI 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383329 311 D-SICSRRGTSEEHEA----SRRVKAELLVQMDGVGGTSENddpskmvMVLAATNFPWDIDEALRR--RLEKRIYI 379
Cdd:cd19510   85 DaAFESREHNKKNPSAygglSRVTFSGLLNALDGVASSEER-------IVFMTTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 239-377 5.53e-08

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: 52.14  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 239 RRPWKGVLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLTSKYRgESEKLVRLLFEMARFYSPATI-FIDEIDSICSRR 317
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKR 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 318 GTSEEHEASRRVKAELLVQMdgvggtsenDDPSKMVMVLAATNFPWDIDEALRRRLEKRI 377
Cdd:cd19512   98 STEKISEDLRAALNAFLYRT---------GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 451-489 7.66e-08

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: 49.03  E-value: 7.66e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530383329  451 EEMHMPT-TMEDFEMALKKVSKSVSAADIERYEKWIFEFG 489
Cdd:pfam09336  22 DKLLEPPvTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 241-369 1.04e-07

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: 51.61  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 241 PWKGVLMVGPPGTGKTLLAKAVATEC--------------KTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIF 306
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPCIIW 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383329 307 IDEIDSICSRRGTsEEHEASRRVKAELLVQMdgVGGTSENDDPSKMVmVLAATNFPWDIDEAL 369
Cdd:cd19505   91 IPNIHELNVNRST-QNLEEDPKLLLGLLLNY--LSRDFEKSSTRNIL-VIASTHIPQKVDPAL 149
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 245-313 2.85e-06

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: 48.75  E-value: 2.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383329 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLT-SKYRGESEK--LVRLL----FEMARfYSPATIFIDEIDSI 313
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDVEniLLKLLqaadYDVER-AQRGIVYIDEIDKI 127
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 188-393 3.06e-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: 49.01  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 188 DKDLVEALERDIISQnpnvrwDDIADLVEAkkllkeAVVLpmwmpeffkgiRRPwkgVLMVGPPGTGKTLLAKAVATECK 267
Cdd:COG0714    3 EARLRAEIGKVYVGQ------EELIELVLI------ALLA-----------GGH---LLLEGVPGVGKTTLAKALARALG 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 268 TTFFNVS-SSTL-------TSKYRGESEKLV---RLLFEmarfyspATIFIDEIDsicsRrgtseeheASRRVKAELL-- 334
Cdd:COG0714   57 LPFIRIQfTPDLlpsdilgTYIYDQQTGEFEfrpGPLFA-------NVLLADEIN----R--------APPKTQSALLea 117

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 335 -----VQMDgvGGTSENDDPskmVMVLAATNfPWDID------EALRRRLEKRIYIPLPSakgREELLRI 393
Cdd:COG0714  118 meerqVTIP--GGTYKLPEP---FLVIATQN-PIEQEgtyplpEAQLDRFLLKLYIGYPD---AEEEREI 178
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 244-373 9.80e-06

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: 44.98  E-value: 9.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  244 GVLMVGPPGTGKTLLAK--AVATECKTTFF-----NVSSSTLTSKYR---GESEKLVRLLFEMARfySPATIFIDEIDsi 313
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNidpGGASWVDGPLVRAAR--EGEIAVLDEIN-- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383329  314 csrrgtseehEASRRVKAEL--------LVQMDGVGgtsENDDPSKMVMVLAATNFP----WDIDEALRRRL 373
Cdd:pfam07728  77 ----------RANPDVLNSLlsllderrLLLPDGGE---LVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
243-293 1.14e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.66  E-value: 1.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530383329 243 KGVLMVGPPGTGKTLLAKAVATEC--KTTFFNVSSSTLTSKYRGESEKLVRLL 293
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYSAELKKTEFLMQAL 117
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
245-318 1.31e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 47.46  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLT-SKYRGES-EK-LVRLLfeMARFYSPAT-----IFIDEIDSIcSR 316
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEDvENiLLKLL--QAADYDVEKaqrgiVYIDEIDKI-AR 187


                 ..
gi 530383329 317 RG 318
Cdd:PRK05342 188 KS 189
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 249-310 1.60e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 47.36  E-value: 1.60e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383329 249 GPPGTGKTLLAKAVATECKTTFFNVsSSTLTSKyrgeseKLVRLLFE---MARFYSPATI-FIDEI 310
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFVAL-SAVTSGV------KDIREVIEearERRAYGRRTIlFVDEI 114
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 246-414 2.04e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 47.15  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  246 LMVGPPGTGKTLLAKAVATE-C------KTTFFNVSSSTLTSKYRGESEKLVRLLFEMARfysPATIFIDEIDSICSRRG 318
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADLIGQYIGESEAKTNEIIDSAL---GGVLFLDEAYTLVETGY 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  319 TSEEHEASRRVKaELLVQMDG------VGGTSENDDPSKMVmvlaatnfpwDIDEALRRRLEKRIYIPLPSAkgrEELLR 392
Cdd:TIGR03922 393 GQKDPFGLEAID-TLLARMENdrdrlvVIGAGYRKDLDKFL----------EVNEGLRSRFTRVIEFPSYSP---DELVE 458

                         170       180
                  ....*....|....*....|..
gi 530383329  393 ISLRELELADDVDLASIAENME 414
Cdd:TIGR03922 459 IARRMATERDSVLDDAAADALL 480
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 245-315 3.40e-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: 44.11  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329  245 VLMVGPPGTGKTLLAKAVA-----TECKTTFFNVSS---STLTSKYRGESEKLVR-----LLFEMARFYSPATIFIDEID 311
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgDERALIRIDMSEymeEHSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85


                  ....
gi 530383329  312 SICS 315
Cdd:pfam07724  86 KAHP 89
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 249-411 4.38e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 45.85  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 249 GPPGTGKTLLAKAVATECKTTFFNVsSSTLTSKyrgeseKLVRLLFEMA---RFYSPATI-FIDEIdsicsrrgtseeHe 324
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEAL-SAVTSGV------KDLREVIEEArqrRSAGRRTIlFIDEI------------H- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 325 asRRVKAE---LLVQM-DG----VGGTSENddPSK----------MVMVLAATNfPWDIDEALRRRLE--KRIYIPLpSA 384
Cdd:PRK13342 103 --RFNKAQqdaLLPHVeDGtitlIGATTEN--PSFevnpallsraQVFELKPLS-EEDIEQLLKRALEdkERGLVEL-DD 176

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530383329 385 KGREELLRIS-------LRELELADD----VDLASIAE 411
Cdd:PRK13342 177 EALDALARLAngdarraLNLLELAALgvdsITLELLEE 214
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 245-318 1.47e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 43.88  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 245 VLMVGPPGTGKTLLAKAVAtecktTFFNV-----SSSTLT-SKYRGES-EK-LVRLL----FEMARfyspAT---IFIDE 309
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLA-----RILDVpfaiaDATTLTeAGYVGEDvENiLLKLLqaadYDVEK----AErgiIYIDE 182


                 ....*....
gi 530383329 310 IDSIcSRRG 318
Cdd:COG1219  183 IDKI-ARKS 190
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 243-288 2.63e-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: 43.07  E-value: 2.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530383329  243 KGVLMVGPPGTGKTLLAKAVATEC--KTTFFNVSSSTLtskYRGESEK 288
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEV---YSLEMKK 95
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 245-264 3.15e-04

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: 43.11  E-value: 3.15e-04
                         10        20
                 ....*....|....*....|
gi 530383329 245 VLMVGPPGTGKTLLAKAVAT 264
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 246-374 3.77e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.39  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 246 LMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLtskyRGESE--------------KLVRLLFEmARFYSPaTIFIDEID 311
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGV----RDEAEirghrrtyvgampgRIIQALKK-AGTNNP-VFLLDEID 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530383329 312 SI-CSRRGTSEeheasrrvkAELLVQMDGVGGTSEND-------DPSKmVMVLAATNFPWDIDEALRRRLE 374
Cdd:cd19500  115 KIgSSFRGDPA---------SALLEVLDPEQNSTFSDhyldvpfDLSK-VLFIATANSLDTIPGPLLDRME 175
PRK04195 PRK04195
replication factor C large subunit; Provisional
 209-265 8.67e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.83  E-value: 8.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530383329 209 DDIADLVEAKKLLKEavvlpmWMPEFFKGirRPWKGVLMVGPPGTGKTLLAKAVATE 265
Cdd:PRK04195  14 SDVVGNEKAKEQLRE------WIESWLKG--KPKKALLLYGPPGVGKTSLAHALAND 62
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 245-264 8.73e-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: 40.60  E-value: 8.73e-04
                          10        20
                  ....*....|....*....|
gi 530383329  245 VLMVGPPGTGKTLLAKAVAT 264
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
243-274 1.48e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 1.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530383329 243 KGVLMVGPPGTGKTLLAKAVATEC-----KTTFFNVS 274
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTAP 136
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 239-313 4.71e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.43  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 239 RRPWKGVLMVGPPGTGKTLLAKAVA------------TECKTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYSPATIF 306
Cdd:PRK11034 204 RRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILF 283


                 ....*..
gi 530383329 307 IDEIDSI 313
Cdd:PRK11034 284 IDEIHTI 290
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 245-310 5.54e-03

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: 37.47  E-value: 5.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383329 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSS------TLTSKYRgeSEKLVRLLFEMARFYSPATIFIDEI 310
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINVNLElsrrllELPEKQR--ALRAPRLLDEIAEKSSGDVVLLDNI 88
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 243-277 7.31e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 37.37  E-value: 7.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530383329  243 KGVLMVGPPGTGKTLLAKAV-----ATECKTTFFNVSSST 277
Cdd:pfam12775  32 KPVLLVGPTGTGKTVIIQNLlrkldKEKYLPLFINFSAQT 71
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
245-310 7.41e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.57  E-value: 7.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383329 245 VLMVGPPGTGKTLLAKAVATECKTTFFNVSSSTLtskyrgesEK---LVRLLfemarfyspaT-------IFIDEI 310
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL--------EKpgdLAAIL----------TnleegdvLFIDEI 111
44 PHA02544
clamp loader, small subunit; Provisional
 223-327 9.54e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.05  E-value: 9.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383329 223 EAVVLPMWMPEFFKGIRRpwKG-----VLMVGPPGTGKTLLAKAVATE--CKTTFFNVSSSTLtskyrgeseKLVRllFE 295
Cdd:PHA02544  21 DECILPAADKETFKSIVK--KGripnmLLHSPSPGTGKTTVAKALCNEvgAEVLFVNGSDCRI---------DFVR--NR 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530383329 296 MARFYSPAT-------IFIDEIDsicsRRGTSEEHEASR 327
Cdd:PHA02544  88 LTRFASTVSltgggkvIIIDEFD----RLGLADAQRHLR 122
 
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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