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Conserved domains on  [gi|1220516022|ref|NP_001340829|]
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katanin p60 ATPase-containing subunit A-like 2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 281-445 3.17e-84

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: 259.21  E-value: 3.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 281 IIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLV 360
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 361 RVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRRL 439
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRF 157


                  ....*.
gi 1220516022 440 EKRILV 445
Cdd:cd19509   158 EKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 211-547 8.14e-79

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


:

Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 251.08  E-value: 8.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 211 IIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQL 290
Cdd:COG1222    10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 291 VKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARY 369
Cdd:COG1222    90 IREAVELPLKNPELFRKYgIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELARE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 370 HAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRILVDL 447
Cdd:COG1222   170 KAPSIIFIDEIDAIAARRT--DDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEVPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 448 PSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKifdalenhqsessdlpriQL 527
Cdd:COG1222   247 PDEEAREEILKIHL------RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE------------------GR 302

                         330       340
                  ....*....|....*....|
gi 1220516022 528 DIVTTADFLDVLTHTKPSAK 547
Cdd:COG1222   303 DTVTMEDLEKAIEKVKKKTE 322
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 51-81 5.92e-04

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 37.41  E-value: 5.92e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1220516022   51 RRKNLLILISHYLTQEGYIDTANALEQETKL 81
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
 
Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 281-445 3.17e-84

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: 259.21  E-value: 3.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 281 IIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLV 360
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 361 RVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRRL 439
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRF 157


                  ....*.
gi 1220516022 440 EKRILV 445
Cdd:cd19509   158 EKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 211-547 8.14e-79

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 251.08  E-value: 8.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 211 IIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQL 290
Cdd:COG1222    10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 291 VKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARY 369
Cdd:COG1222    90 IREAVELPLKNPELFRKYgIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELARE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 370 HAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRILVDL 447
Cdd:COG1222   170 KAPSIIFIDEIDAIAARRT--DDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEVPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 448 PSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKifdalenhqsessdlpriQL 527
Cdd:COG1222   247 PDEEAREEILKIHL------RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE------------------GR 302

                         330       340
                  ....*....|....*....|
gi 1220516022 528 DIVTTADFLDVLTHTKPSAK 547
Cdd:COG1222   303 DTVTMEDLEKAIEKVKKKTE 322
cell_div_CdvC NF041006
cell division protein CdvC;
274-560 9.66e-74

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 9.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFtgilsP--W-KGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVS 350
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 351 KWRGDSEKLVRVLFELARYHA-----PSTIFLDELESVMSQRGTASGGEhegsLRMKTELLVQMDGLA-RSEDL-VFVLA 423
Cdd:NF041006  173 KWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGE----VRVRNQFLKEMDGLQdKSENYhVYVIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 424 ASNLPWELDCAMLRRLEKRILVDLPSREARQAMIYHWlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMR 503
Cdd:NF041006  249 ATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY------TSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMR 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220516022 504 PVRKIFdalENHQSEssdlPRiqldIVTTADFLDVLTHTKPSA-KNLAQRYSDWQREF 560
Cdd:NF041006  323 VVKEMF---EKGLGE----PR----PITMEDFKEVLKIRKPSVnQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 267-563 2.66e-64

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: 223.63  E-value: 2.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 267 RDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISA 345
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMgIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 346 STIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGgeHEGSLRMKTELLVQMDGLARSEDLVfVLAAS 425
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFD--TSVTDRIVNQLLTEMDGIQELSNVV-VIAAT 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 426 NLPWELDCAMLR--RLEKRILVDLPSREARQAMI-YHwlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAM 502
Cdd:TIGR01243 598 NRPDILDPALLRpgRFDRLILVPPPDEEARKEIFkIH-------TRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAM 670

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1220516022 503 RPVRKIFDALENHQSESSDLPRIQLDIVTTADFLDVLTHTKPS-AKNLAQRYSDWQREFESV 563
Cdd:TIGR01243 671 AALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSvSKEDMLRYERLAKELKRL 732
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 278-548 4.79e-62

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: 209.38  E-value: 4.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 278 WNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS 356
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 357 EKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGLarsEDLVFVLAASNLPWELDCAML 436
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGR---RVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 437 RRLEKRILVDLPSREARQAMIYHWLPPvsksraLELHTELEYSVLSQETEGYSGSDIKLVCREAAMRpvrkifdALenhq 516
Cdd:COG0464   310 RRFDEIIFFPLPDAEERLEIFRIHLRK------RPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ-------AL---- 372

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1220516022 517 sessdlpRIQLDIVTTADFLDVLTHTKPSAKN 548
Cdd:COG0464   373 -------RLGREPVTTEDLLEALEREDIFLKR 397
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 274-537 1.09e-56

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 195.05  E-value: 1.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFT--GIlSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSK 351
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 352 WRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQR---GTasGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLP 428
Cdd:PRK03992  205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGT--SGDREVQ-RTLMQLLAEMDGFDPRGN-VKIIAATNRI 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 429 WELDCAMLR--RLEKRILVDLPSREARqAMIyhwlppvsksraLELHT-------ELEYSVLSQETEGYSGSDIKLVCRE 499
Cdd:PRK03992  281 DILDPAILRpgRFDRIIEVPLPDEEGR-LEI------------LKIHTrkmnladDVDLEELAELTEGASGADLKAICTE 347

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1220516022 500 AAMRPVRkifdalENHqsessdlpriqlDIVTTADFLD 537
Cdd:PRK03992  348 AGMFAIR------DDR------------TEVTMEDFLK 367
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 315-447 1.94e-47

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: 161.61  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGE 394
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1220516022 395 HEgslRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDL 447
Cdd:pfam00004  81 SR---RVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 311-448 7.25e-15

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: 72.02  E-value: 7.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022  311 PWKGLLLYGPPGTGKTLLAKAVATECKTT---FFNISASTI--------------VSKWRGDSEKLVRVLFELARYHAPS 373
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1220516022  374 TIFLDELESVMSQRGTAsggehegsLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLP 448
Cdd:smart00382  81 VLILDEITSLLDAEQEA--------LLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 475-519 2.98e-09

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: 52.54  E-value: 2.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1220516022 475 ELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFDALENHQSES 519
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 315-380 4.62e-04

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 42.07  E-value: 4.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATEC-----KTTFFniSASTIVSKWRG--DSEKLVRVLFELARYHApstIFLDEL 380
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFT--TAADLVEQLAQarADGRLGRLLRRLARYDL---LIIDEL 160
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 51-81 5.92e-04

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 37.41  E-value: 5.92e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1220516022   51 RRKNLLILISHYLTQEGYIDTANALEQETKL 81
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 54-78 5.27e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.60  E-value: 5.27e-03
                          10        20
                  ....*....|....*....|....*
gi 1220516022  54 NLLILISHYLTQEGYIDTANALEQE 78
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
 
Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 281-445 3.17e-84

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: 259.21  E-value: 3.17e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 281 IIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLV 360
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 361 RVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRRL 439
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRF 157


                  ....*.
gi 1220516022 440 EKRILV 445
Cdd:cd19509   158 EKRIYI 163
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 280-445 1.08e-80

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: 250.29  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKL 359
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 360 VRVLFELARYHAPSTIFLDELESVMSQRGTasGGEHEGSLRMKTELLVQMDGLARSED------LVFVLAASNLPWELDC 433
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGASEnddpskMVMVLAATNFPWDIDE 158

                         170
                  ....*....|..
gi 1220516022 434 AMLRRLEKRILV 445
Cdd:cd19522   159 ALRRRLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 274-445 4.33e-79

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: 4.33e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWR 353
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 354 GDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDC 433
Cdd:cd19521    82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDS 158

                         170
                  ....*....|..
gi 1220516022 434 AMLRRLEKRILV 445
Cdd:cd19521   159 AIRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 211-547 8.14e-79

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 251.08  E-value: 8.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 211 IIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQL 290
Cdd:COG1222    10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 291 VKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARY 369
Cdd:COG1222    90 IREAVELPLKNPELFRKYgIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELARE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 370 HAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRILVDL 447
Cdd:COG1222   170 KAPSIIFIDEIDAIAARRT--DDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEVPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 448 PSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKifdalenhqsessdlpriQL 527
Cdd:COG1222   247 PDEEAREEILKIHL------RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE------------------GR 302

                         330       340
                  ....*....|....*....|
gi 1220516022 528 DIVTTADFLDVLTHTKPSAK 547
Cdd:COG1222   303 DTVTMEDLEKAIEKVKKKTE 322
cell_div_CdvC NF041006
cell division protein CdvC;
274-560 9.66e-74

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 9.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFtgilsP--W-KGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVS 350
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 351 KWRGDSEKLVRVLFELARYHA-----PSTIFLDELESVMSQRGTASGGEhegsLRMKTELLVQMDGLA-RSEDL-VFVLA 423
Cdd:NF041006  173 KWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGE----VRVRNQFLKEMDGLQdKSENYhVYVIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 424 ASNLPWELDCAMLRRLEKRILVDLPSREARQAMIYHWlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMR 503
Cdd:NF041006  249 ATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY------TSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMR 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220516022 504 PVRKIFdalENHQSEssdlPRiqldIVTTADFLDVLTHTKPSA-KNLAQRYSDWQREF 560
Cdd:NF041006  323 VVKEMF---EKGLGE----PR----PITMEDFKEVLKIRKPSVnQEMLKAYEAWHEKF 369
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 260-445 3.10e-68

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: 218.70  E-value: 3.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 260 ELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTT 339
Cdd:cd19525     3 KMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGAT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 340 FFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDL 418
Cdd:cd19525    83 FFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGAtTSSEDR 159

                         170       180
                  ....*....|....*....|....*..
gi 1220516022 419 VFVLAASNLPWELDCAMLRRLEKRILV 445
Cdd:cd19525   160 ILVVGATNRPQEIDEAARRRLVKRLYI 186
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 267-563 2.66e-64

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: 223.63  E-value: 2.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 267 RDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISA 345
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMgIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 346 STIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGgeHEGSLRMKTELLVQMDGLARSEDLVfVLAAS 425
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFD--TSVTDRIVNQLLTEMDGIQELSNVV-VIAAT 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 426 NLPWELDCAMLR--RLEKRILVDLPSREARQAMI-YHwlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAM 502
Cdd:TIGR01243 598 NRPDILDPALLRpgRFDRLILVPPPDEEARKEIFkIH-------TRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAM 670

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1220516022 503 RPVRKIFDALENHQSESSDLPRIQLDIVTTADFLDVLTHTKPS-AKNLAQRYSDWQREFESV 563
Cdd:TIGR01243 671 AALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSvSKEDMLRYERLAKELKRL 732
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 280-445 1.12e-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: 205.85  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKL 359
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 360 VRVLFELARYHAPSTIFLDELESVMSQRgtaSGGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRR 438
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSER---SEGEHEASRRLKTEFLIEFDGVqSNGDDRVLVMGATNRPQELDDAVLRR 157


                  ....*..
gi 1220516022 439 LEKRILV 445
Cdd:cd19524   158 FTKRVYV 164
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 278-548 4.79e-62

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: 209.38  E-value: 4.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 278 WNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS 356
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 357 EKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGLarsEDLVFVLAASNLPWELDCAML 436
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGR---RVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 437 RRLEKRILVDLPSREARQAMIYHWLPPvsksraLELHTELEYSVLSQETEGYSGSDIKLVCREAAMRpvrkifdALenhq 516
Cdd:COG0464   310 RRFDEIIFFPLPDAEERLEIFRIHLRK------RPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ-------AL---- 372

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1220516022 517 sessdlpRIQLDIVTTADFLDVLTHTKPSAKN 548
Cdd:COG0464   373 -------RLGREPVTTEDLLEALEREDIFLKR 397
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 274-537 1.09e-56

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 195.05  E-value: 1.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFT--GIlSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSK 351
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 352 WRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQR---GTasGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLP 428
Cdd:PRK03992  205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGT--SGDREVQ-RTLMQLLAEMDGFDPRGN-VKIIAATNRI 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 429 WELDCAMLR--RLEKRILVDLPSREARqAMIyhwlppvsksraLELHT-------ELEYSVLSQETEGYSGSDIKLVCRE 499
Cdd:PRK03992  281 DILDPAILRpgRFDRIIEVPLPDEEGR-LEI------------LKIHTrkmnladDVDLEELAELTEGASGADLKAICTE 347

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1220516022 500 AAMRPVRkifdalENHqsessdlpriqlDIVTTADFLD 537
Cdd:PRK03992  348 AGMFAIR------DDR------------TEVTMEDFLK 367
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 280-445 6.65e-54

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: 180.31  E-value: 6.65e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLF--TGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSE 357
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 358 KLVRVLFELARYHAPSTIFLDELESVMSQRgtaSGGEHEGSLRMKTELLVQMDGLARS-EDLVFVLAASNLPWELDCAML 436
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR---SSTDHEATAMMKAEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAIL 157


                  ....*....
gi 1220516022 437 RRLEKRILV 445
Cdd:cd19520   158 RRMPKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 255-546 3.60e-51

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: 187.04  E-value: 3.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 255 NSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVA 333
Cdd:TIGR01243 154 ATEVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLgIEPPKGVLLYGPPGTGKTLLAKAVA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 334 TECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGgehEGSLRMKTELLVQMDGLa 413
Cdd:TIGR01243 234 NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGL- 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 414 RSEDLVFVLAASNLPWELDCAMLR--RLEKRILVDLPSREARQAMiyhwLPPVSKSRALELHTELEYsvLSQETEGYSGS 491
Cdd:TIGR01243 310 KGRGRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEI----LKVHTRNMPLAEDVDLDK--LAEVTHGFVGA 383

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1220516022 492 DIKLVCREAAMRPVRKIFDAlENHQSESSDLPRIQLD--IVTTADFLDVLTHTKPSA 546
Cdd:TIGR01243 384 DLAALAKEAAMAALRRFIRE-GKINFEAEEIPAEVLKelKVTMKDFMEALKMVEPSA 439
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 287-445 1.20e-49

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: 168.62  E-value: 1.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 287 AKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFE 365
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLgIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 366 LARYHAPSTIFLDELESVMSQRGTASGGehEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRI 443
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSS--GVTDRVVSQLLTELDGIESLKG-VVVIAATNRPDMIDPALLRpgRLDKLI 157


                  ..
gi 1220516022 444 LV 445
Cdd:cd19511   158 YV 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 280-443 9.23e-48

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 164.00  E-value: 9.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEK 358
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALgLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 359 LVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGLArSEDLVFVLAASNLPWELDCAMLR- 437
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMS-SRGKVVVIAATNRPDAIDPALRRp 156


                  ....*..
gi 1220516022 438 -RLEKRI 443
Cdd:cd19503   157 gRFDREV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 315-447 1.94e-47

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: 161.61  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGE 394
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1220516022 395 HEgslRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDL 447
Cdd:pfam00004  81 SR---RVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 288-445 1.31e-46

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: 160.75  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 288 KQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFEL 366
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLKFgMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 367 ARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRIL 444
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKN-VFIIGATNRPDIIDPAILRpgRLDQLIY 160


                  .
gi 1220516022 445 V 445
Cdd:cd19528   161 I 161
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 276-445 2.55e-46

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 160.09  E-value: 2.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 276 IKWNDIIGLDAAKQLVKEAVVYpIRYPQLFT--GILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWR 353
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 354 GDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDC 433
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTG-VIVIAATNRPDVLDP 157

                         170
                  ....*....|....
gi 1220516022 434 AMLR--RLEKRILV 445
Cdd:cd19501   158 ALLRpgRFDRQVYV 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 274-507 1.08e-45

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 165.71  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKW 352
Cdd:PTZ00454  140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIgIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 353 RGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELD 432
Cdd:PTZ00454  220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTN-VKVIMATNRADTLD 298

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1220516022 433 CAMLR--RLEKRILVDLPSREARQaMIYHWLppVSKsraLELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRK 507
Cdd:PTZ00454  299 PALLRpgRLDRKIEFPLPDRRQKR-LIFQTI--TSK---MNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 278-443 1.22e-45

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: 158.27  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 278 WNDIIGLDAAKQLVKEAVVYPIRYPQLFT--GILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGD 355
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 356 SEKLVRVLFELARYHAPSTIFLDELESVMSQR-GTASGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCA 434
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfDSGTGGDREVQ-RTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPA 158

                         170
                  ....*....|.
gi 1220516022 435 MLR--RLEKRI 443
Cdd:cd19502   159 LLRpgRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 287-445 4.64e-45

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 156.50  E-value: 4.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 287 AKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFE 365
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLgIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 366 LARYHAPSTIFLDELESVMSQRGTasGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCAMLR--RLEKRI 443
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGT--TGDSGVTERVVNQLLTELDGLEEMNGVV-VIAATNRPDIIDPALLRagRFDRLI 157


                  ..
gi 1220516022 444 LV 445
Cdd:cd19529   158 YI 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 287-445 8.18e-43

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 150.51  E-value: 8.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 287 AKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFEL 366
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 367 ARYHAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRIL 444
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRD--SSGESGELRRVLNQLLTELDGVNSRSK-VLVIAATNRPDLLDPALLRpgRFDEVIE 157


                  .
gi 1220516022 445 V 445
Cdd:cd19481   158 F 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 274-506 2.80e-42

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 157.24  E-value: 2.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 274 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKW 352
Cdd:PTZ00361  178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIgIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 353 RGDSEKLVRVLFELARYHAPSTIFLDELESVMSQR-GTASGGEHEGSLRMkTELLVQMDGLARSEDlVFVLAASNLPWEL 431
Cdd:PTZ00361  258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRyDATSGGEKEIQRTM-LELLNQLDGFDSRGD-VKVIMATNRIESL 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 432 DCAMLR--RLEKRILVDLPSREarqamiyhwlppvSKSRALELHT---------ELEYSVLSQETegYSGSDIKLVCREA 500
Cdd:PTZ00361  336 DPALIRpgRIDRKIEFPNPDEK-------------TKRRIFEIHTskmtlaedvDLEEFIMAKDE--LSGADIKAICTEA 400


                  ....*.
gi 1220516022 501 AMRPVR 506
Cdd:PTZ00361  401 GLLALR 406
ftsH CHL00176
cell division protein; Validated
 276-507 1.10e-41

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 159.06  E-value: 1.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 276 IKWNDIIGLDAAKQLVKEaVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRG 354
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFEE-VVSFLKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 355 DSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCA 434
Cdd:CHL00176  259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVI-VIAATNRVDILDAA 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1220516022 435 MLR--RLEKRILVDLPSREARQAMiyhwLPPVSKSRALELHTELEysVLSQETEGYSGSDIKLVCREAAMRPVRK 507
Cdd:CHL00176  338 LLRpgRFDRQITVSLPDREGRLDI----LKVHARNKKLSPDVSLE--LIARRTPGFSGADLANLLNEAAILTARR 406
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
280-506 2.25e-41

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 158.27  E-value: 2.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVY---PIRYPQLFTGIlsPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS 356
Cdd:PRK10733  153 DVAGCDEAKEEVAELVEYlrePSRFQKLGGKI--P-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 357 EKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCAML 436
Cdd:PRK10733  230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGII-VIAATNRPDVLDPALL 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1220516022 437 R--RLEKRILVDLPSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVR 506
Cdd:PRK10733  309 RpgRFDRQVVVGLPDVRGREQILKVHM------RRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 280-445 2.41e-40

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 143.87  E-value: 2.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKL 359
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 360 VRVLFELARYHAPSTIFLDELESVMSQRGTasggEHEGSLRMKTELLVQMDG-LARSEDLVFVLAASNLPWELDCAMLRR 438
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGvLGSGEDGVLVVCTTSKPEEIDESLRRY 156


                  ....*..
gi 1220516022 439 LEKRILV 445
Cdd:cd19523   157 FSKRLLV 163
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 284-445 6.49e-40

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 142.63  E-value: 6.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 284 LDAAKQLVKEAVVYPIRYPQLFT--GILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVR 361
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 362 VLFELARYHAPSTIFLDELESVMSQRGtasGGEHEGSLRMKTELLVQMDGL-ARSEdlVFVLAASNLPWELDCAMLR--R 438
Cdd:cd19530    80 QVFQRARASAPCVIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLeERSN--VFVIAATNRPDIIDPAMLRpgR 154


                  ....*..
gi 1220516022 439 LEKRILV 445
Cdd:cd19530   155 LDKTLYV 161
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
278-500 1.60e-39

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 144.26  E-value: 1.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 278 WNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSE 357
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 358 KLVRVLFELARyHAPSTIFLDELESVMSQRGTASG-GEhegSLRMKTELLVQMDGLARSedlVFVLAASNLPWELDCAML 436
Cdd:COG1223    81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDvGE---VKRVVNALLQELDGLPSG---SVVIAATNHPELLDSALW 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1220516022 437 RRLEKRILVDLPSREARQAMIyhwlppVSKSRALELHTELEYSVLSQETEGYSGSDIKLVCREA 500
Cdd:COG1223   154 RRFDEVIEFPLPDKEERKEIL------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
273-507 9.43e-39

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 149.80  E-value: 9.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 273 NPNIKWNDIIGLDAAKQLVKEAVVYpIRYPQLFT--G--IlsPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTI 348
Cdd:COG0465   136 KPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTrlGakI--P-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 349 VskwrgdsEKLV-----RV--LFELARYHAPSTIFLDELESVMSQRGTASGG---EHEGSLrmkTELLVQMDGLARSEDL 418
Cdd:COG0465   212 V-------EMFVgvgasRVrdLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGghdEREQTL---NQLLVEMDGFEGNEGV 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 419 VfVLAASNLPWELDCAMLR--RLEKRILVDLPSREARQAmIyhwlppvsksraLELHT-------ELEYSVLSQETEGYS 489
Cdd:COG0465   282 I-VIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREA-I------------LKVHArkkplapDVDLEVIARRTPGFS 347

                         250
                  ....*....|....*...
gi 1220516022 490 GSDIKLVCREAAMRPVRK 507
Cdd:COG0465   348 GADLANLVNEAALLAARR 365
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 280-438 9.73e-39

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: 139.49  E-value: 9.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEK 358
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIgIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 359 LVRVLFELARYHAPSTIFLDELESVMSQRGTASGgehEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAmLRR 438
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHG---EVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPA-LRR 155
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 288-445 2.35e-37

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: 135.72  E-value: 2.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 288 KQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELA 367
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 368 RYHAPSTIFLDELESVMSQRGTA--SGGEHEgslRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLR--RLEKRI 443
Cdd:cd19527    82 RDAKPCVIFFDELDSLAPSRGNSgdSGGVMD---RVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLL 158


                  ..
gi 1220516022 444 LV 445
Cdd:cd19527   159 YL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 287-444 4.50e-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: 129.47  E-value: 4.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 287 AKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFE 365
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSpLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 366 LARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGlARSEDLVFVLAASNLPWELDCAMLR--RLEKRI 443
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDG-VEGLDGVYVLAATSRPDLIDPALLRpgRLDKLV 156


                  .
gi 1220516022 444 L 444
Cdd:cd19526   157 Y 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 280-443 7.28e-34

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: 126.37  E-value: 7.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLF--TGILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSE 357
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 358 KLVRVLFELARYHAPSTIFLDELESVMSQRGTASggeHEGSLRMKTELLVQMDGL---ARSEDLVFVLAASNLPWELDCA 434
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQ---REMERRIVSQLLTCMDELnneKTAGGPVLVIGATNRPDSLDPA 156

                         170
                  ....*....|.
gi 1220516022 435 MLR--RLEKRI 443
Cdd:cd19518   157 LRRagRFDREI 167
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 280-438 1.42e-31

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: 119.92  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATEC-----KTTFFNISASTIVSKWR 353
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFkITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 354 GDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGslrMKTELLVQMDGL-ARSEdlVFVLAASNLPWELD 432
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS---IVSTLLALMDGLdNRGQ--VVVIGATNRPDALD 155


                  ....*.
gi 1220516022 433 CAmLRR 438
Cdd:cd19517   156 PA-LRR 160
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 282-447 1.41e-21

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 91.44  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 282 IGLDAAKQLVKEAVvypirypqlftgILSPWKGLLLYGPPGTGKTLLAKAVATEC---KTTFFNISASTIVSKWRGDSEK 358
Cdd:cd00009     1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 359 ---LVRVLFELARYHAPSTIFLDELESVmsqrgtaSGGEHEGSLRMktelLVQMDGLARSEDLVFVLAASNLPWELDCAM 435
Cdd:cd00009    69 ghfLVRLLFELAEKAKPGVLFIDEIDSL-------SRGAQNALLRV----LETLNDLRIDRENVRVIGATNRPLLGDLDR 137

                         170
                  ....*....|....
gi 1220516022 436 --LRRLEKRILVDL 447
Cdd:cd00009   138 alYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 313-440 1.46e-16

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: 77.53  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 313 KGLLLYGPPGTGKTLLAKAV-----ATECKTtffnISASTIVSKWRGDSEKLVRVLF-----ELARYHAPS---TIFLDE 379
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeEQRRLGANSglhIIIFDE 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1220516022 380 LESVMSQRGTASGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLE 440
Cdd:cd19504   112 IDAICKQRGSMAGSTGVHD-TVVNQLLSKIDGVEQLNN-ILVIGMTNRKDLIDEALLRpgRLE 172
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 280-431 6.97e-15

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: 72.40  E-value: 6.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 280 DIIGLDAAKQLV--------KEAVVYPIRYPqlftgilspwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSK 351
Cdd:cd19507     1 DVGGLDNLKDWLkkrkaafsKQASAYGLPTP----------KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 352 WRGDSEKLVRVLFELARYHAPSTIFLDELESVMSqrGTASGGEHEGSLRMKTELLVQMdglARSEDLVFVLAASN----L 427
Cdd:cd19507    71 LVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFS--NADSKGDSGTSSRVLGTFLTWL---QEKKKPVFVVATANnvqsL 145


                  ....
gi 1220516022 428 PWEL 431
Cdd:cd19507   146 PPEL 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 311-448 7.25e-15

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: 72.02  E-value: 7.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022  311 PWKGLLLYGPPGTGKTLLAKAVATECKTT---FFNISASTI--------------VSKWRGDSEKLVRVLFELARYHAPS 373
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1220516022  374 TIFLDELESVMSQRGTAsggehegsLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLP 448
Cdd:smart00382  81 VLILDEITSLLDAEQEA--------LLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLI 147
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 315-438 2.92e-14

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 71.71  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 315 LLLYGPPGTGKTLLAKAVA---------TECKTTFFNISASTIVSKWRGDSEKLVRVLF----ELAR-YHAPSTIFLDEL 380
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDdKDALVFVLIDEV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1220516022 381 ESVMSQRGTA-SGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCAMLRR 438
Cdd:cd19508   135 ESLAAARSASsSGTEPSDAIRVVNAVLTQIDRIKRYHNNV-ILLTSNLLEKIDVAFVDR 192
ycf46 CHL00195
Ycf46; Provisional
 273-500 3.45e-13

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 71.97  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 273 NPNIKWNDIIGLDAAKQ--------LVKEAVVYPIRYPqlftgilspwKGLLLYGPPGTGKTLLAKAVATECKTTFFNIS 344
Cdd:CHL00195  222 SVNEKISDIGGLDNLKDwlkkrstsFSKQASNYGLPTP----------RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLD 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 345 ASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSqrGTASGGEHEGSLRMKTELLVQmdgLARSEDLVFVLAA 424
Cdd:CHL00195  292 VGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFS--NSESKGDSGTTNRVLATFITW---LSEKKSPVFVVAT 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 425 SN----LPWEldcaMLR--RLEKRILVDLPSREARQAMIYHWLppvSKSRALELHTeLEYSVLSQETEGYSGSDIKLVCR 498
Cdd:CHL00195  367 ANnidlLPLE----ILRkgRFDEIFFLDLPSLEEREKIFKIHL---QKFRPKSWKK-YDIKKLSKLSNKFSGAEIEQSII 438


                  ..
gi 1220516022 499 EA 500
Cdd:CHL00195  439 EA 440
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 313-444 6.02e-13

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: 66.78  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 313 KGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS--EKLVRVLFELARYHAPSTIFLDELESVMSQRGTA 390
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1220516022 391 SGGEHEGSlRMKTElLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRIL 444
Cdd:cd19506   107 TEKQLDPK-RLKKD-LPKILKSLKPEDRVLIVGTTSRPFEADLKSFCKVYNKII 158
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 475-519 2.98e-09

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: 52.54  E-value: 2.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1220516022 475 ELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFDALENHQSES 519
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 315-379 1.12e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 54.29  E-value: 1.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTivskwrgDSEKLVRVLFELA---RYHAPSTI-FLDE 379
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSAVT-------SGVKDIREVIEEArerRAYGRRTIlFVDE 113
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 315-379 1.52e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.94  E-value: 1.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTivskwrgDSEKLVRVLFELARYHAPS---TI-FLDE 379
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrTIlFIDE 100
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 311-438 1.74e-07

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 50.81  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 311 PWK-GLLLYGPPGTGKTLLAKAVATECKTTFFNISASTivskwRGDSEKLVRVLfeLARYHAPSTIFLDELESVMSQR-- 387
Cdd:cd19510    21 PYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDIDAAFESReh 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1220516022 388 ----GTASGGEHEGSLrmkTELLVQMDGLARSEDLVFVLaASNLPWELDCAMLRR 438
Cdd:cd19510    94 nkknPSAYGGLSRVTF---SGLLNALDGVASSEERIVFM-TTNHIERLDPALIRP 144
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 310-443 2.96e-07

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: 50.22  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 310 SPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRgDSEKLVRVLFELARYHAPSTI-FLDELESVMSQRG 388
Cdd:cd19512    20 GLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKRS 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1220516022 389 TASGGEhegSLRMKTELLVQMDGlARSEDLVFVLaASNLPWELDCAMLRRLEKRI 443
Cdd:cd19512    99 TEKISE---DLRAALNAFLYRTG-EQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
313-363 8.34e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.43  E-value: 8.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1220516022 313 KGLLLYGPPGTGKTLLAKAVATEC--KTTFFNISASTIVSKWRGDSEKLVRVL 363
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYSAELKKTEFLMQAL 117
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 239-423 1.11e-04

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: 44.84  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 239 DPSERLLKPLSAFIGMNSEMRELAAVVSRD------------IYLHNPNIKWNDIIGLDAAKQ---LVKEAVVYPIRYPQ 303
Cdd:TIGR03922 224 DPSYRLVTTTAETIEARTDPWDPSSAPSRAefvdpaaaerkaKLLAEAEAELAEQIGLERVKRqvaALKSSTAMALARAE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 304 LFTGILSPWKGLLLYGPPGTGKTLLAKAVATE-C------KTTFFNISASTIVSKWRGDSEKLVRVLFELAryhAPSTIF 376
Cdd:TIGR03922 304 RGLPVAQTSNHMLFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADLIGQYIGESEAKTNEIIDSA---LGGVLF 380

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1220516022 377 LDELESVMSQRGTAsgGEHEGSLRMKTeLLVQMDglARSEDLVFVLA 423
Cdd:TIGR03922 381 LDEAYTLVETGYGQ--KDPFGLEAIDT-LLARME--NDRDRLVVIGA 422
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 313-350 2.26e-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: 43.45  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1220516022 313 KGLLLYGPPGTGKTLLAKAVATEC--KTTFFNISASTIVS 350
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYS 90
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 315-344 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: 41.78  E-value: 3.77e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATECKTTFFNIS 344
Cdd:cd19500    40 LCLVGPPGVGKTSLGKSIARALGRKFVRIS 69
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 316-381 4.02e-04

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: 41.41  E-value: 4.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1220516022 316 LLYGPPGTGKTLLAKAVA-----TECKTTFFNISA---STIVSKWRGDSEKLVRV-----LFELARYHAPSTIFLDELE 381
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAellfgDERALIRIDMSEymeEHSVSRLIGAPPGYVGYeeggqLTEAVRRKPYSIVLIDEIE 85
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 315-380 4.62e-04

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 42.07  E-value: 4.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATEC-----KTTFFniSASTIVSKWRG--DSEKLVRVLFELARYHApstIFLDEL 380
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFT--TAADLVEQLAQarADGRLGRLLRRLARYDL---LIIDEL 160
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
315-339 5.23e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.43  E-value: 5.23e-04
                          10        20
                  ....*....|....*....|....*....
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATE----CKTT 339
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEmgvnIRIT 82
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 285-334 5.77e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 42.08  E-value: 5.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1220516022 285 DAAKQLVKEAVV---YPIRypQLFTGILSpwKG-LLLYGPPGTGKTLLAKAVAT 334
Cdd:COG0714     4 ARLRAEIGKVYVgqeELIE--LVLIALLA--GGhLLLEGVPGVGKTTLAKALAR 53
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 51-81 5.92e-04

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 37.41  E-value: 5.92e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1220516022   51 RRKNLLILISHYLTQEGYIDTANALEQETKL 81
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
PRK04195 PRK04195
replication factor C large subunit; Provisional
 279-335 6.36e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.60  E-value: 6.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220516022 279 NDIIGLDAAKQLVKE-AVVYPIRYPQlftgilspwKGLLLYGPPGTGKTLLAKAVATE 335
Cdd:PRK04195   14 SDVVGNEKAKEQLREwIESWLKGKPK---------KALLLYGPPGVGKTSLAHALAND 62
PRK08116 PRK08116
hypothetical protein; Validated
 314-335 7.47e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.54  E-value: 7.47e-04
                          10        20
                  ....*....|....*....|..
gi 1220516022 314 GLLLYGPPGTGKTLLAKAVATE 335
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANE 137
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 309-375 1.20e-03

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: 39.67  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 309 LSPWKGLLLYGPPGTGKTLLAKAVATEC---------------KTTFFNISASTIVSKWRgDSEKLVRVLFELARYHAPS 373
Cdd:cd19505     9 LSPSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllynKPDFGNDDWIDGMLILK-ESLHRLNLQFELAKAMSPC 87


                  ..
gi 1220516022 374 TI 375
Cdd:cd19505    88 II 89
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 314-381 1.38e-03

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: 39.20  E-value: 1.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1220516022 314 GLLLYGPPGTGKTLLAK--AVATECKTTFF-----NISASTIVSKWRGDSEKLVRVLFELARyhA---PSTIFLDELE 381
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNIDPGGASWVDGPLVR--AareGEIAVLDEIN 76
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 315-334 2.05e-03

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: 40.79  E-value: 2.05e-03
                          10        20
                  ....*....|....*....|
gi 1220516022 315 LLLYGPPGTGKTLLAKAVAT 334
Cdd:COG0606   214 LLMIGPPGSGKTMLARRLPG 233
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
313-342 2.37e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 2.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1220516022 313 KGLLLYGPPGTGKTLLAKAVATEC-----KTTFFN 342
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTT 134
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 315-334 2.62e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.44  E-value: 2.62e-03
                          10        20
                  ....*....|....*....|
gi 1220516022 315 LLLYGPPGTGKTLLAKAVAT 334
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
PRK13341 PRK13341
AAA family ATPase;
315-345 2.65e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATECKTTFFNISA 345
Cdd:PRK13341   55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA 85
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 315-339 3.48e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.25  E-value: 3.48e-03
                          10        20
                  ....*....|....*....|....*....
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATE----CKTT 339
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEmgvnIRIT 64
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
315-335 5.01e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 39.45  E-value: 5.01e-03
                          10        20
                  ....*....|....*....|.
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATE 335
Cdd:COG1474    54 VLIYGPTGTGKTAVAKYVLEE 74
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 54-78 5.27e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.60  E-value: 5.27e-03
                          10        20
                  ....*....|....*....|....*
gi 1220516022  54 NLLILISHYLTQEGYIDTANALEQE 78
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
 302-334 7.02e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 38.44  E-value: 7.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1220516022 302 PQLFTGILSPW----KG----LLLYGPPGTGKTLLAKAVAT 334
Cdd:pfam01057  95 PAEVGSVLLAWlskqFGkrntVWFYGPASTGKTNLAQAIAH 135
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 316-394 7.87e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.05  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220516022 316 LLYGPPGTGKTLLAKAVA------------TECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESV 383
Cdd:PRK11034  211 LLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                          90
                  ....*....|.
gi 1220516022 384 MSQrGTASGGE 394
Cdd:PRK11034  291 IGA-GAASGGQ 300
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 313-333 8.08e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.98  E-value: 8.08e-03
                          10        20
                  ....*....|....*....|.
gi 1220516022 313 KGLLLYGPPGTGKTLLAKAVA 333
Cdd:COG1401   222 KNVILAGPPGTGKTYLARRLA 242
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 313-333 9.08e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 38.84  E-value: 9.08e-03
                          10        20
                  ....*....|....*....|...
gi 1220516022 313 KG--LLLYGPPGTGKTLLAKAVA 333
Cdd:COG0466   351 KGpiLCLVGPPGVGKTSLGKSIA 373
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 315-339 9.71e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.52  E-value: 9.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 1220516022 315 LLLYGPPGTGKTLLAKAVATE----CKTT 339
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEmgvnIRIT 85
 
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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