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Conserved domains on  [gi|1533911146|ref|NP_001354550|]
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katanin p60 ATPase-containing subunit A-like 2 isoform 13 [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 ...
 256-420 2.44e-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: 258.82  E-value: 2.44e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 256 IIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLV 335
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 336 RVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRRL 414
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRF 157


                  ....*.
gi 1533911146 415 EKRILV 420
Cdd:cd19509   158 EKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 186-522 1.01e-78

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


:

Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 250.31  E-value: 1.01e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 186 IIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQL 265
Cdd:COG1222    10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 266 VKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARY 344
Cdd:COG1222    90 IREAVELPLKNPELFRKYgIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELARE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 345 HAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRILVDL 422
Cdd:COG1222   170 KAPSIIFIDEIDAIAARRT--DDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEVPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 423 PSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKifdalenhqsessdlpriQL 502
Cdd:COG1222   247 PDEEAREEILKIHL------RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE------------------GR 302

                         330       340
                  ....*....|....*....|
gi 1533911146 503 DIVTTADFLDVLTHTKPSAK 522
Cdd:COG1222   303 DTVTMEDLEKAIEKVKKKTE 322
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 25-55 5.49e-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: 5.49e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1533911146   25 RRKNLLILISHYLTQEGYIDTANALEQETKL 55
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 ...
 256-420 2.44e-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: 258.82  E-value: 2.44e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 256 IIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLV 335
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 336 RVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRRL 414
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRF 157


                  ....*.
gi 1533911146 415 EKRILV 420
Cdd:cd19509   158 EKRIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 186-522 1.01e-78

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 250.31  E-value: 1.01e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 186 IIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQL 265
Cdd:COG1222    10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 266 VKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARY 344
Cdd:COG1222    90 IREAVELPLKNPELFRKYgIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELARE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 345 HAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRILVDL 422
Cdd:COG1222   170 KAPSIIFIDEIDAIAARRT--DDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEVPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 423 PSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKifdalenhqsessdlpriQL 502
Cdd:COG1222   247 PDEEAREEILKIHL------RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE------------------GR 302

                         330       340
                  ....*....|....*....|
gi 1533911146 503 DIVTTADFLDVLTHTKPSAK 522
Cdd:COG1222   303 DTVTMEDLEKAIEKVKKKTE 322
cell_div_CdvC NF041006
cell division protein CdvC;
249-535 6.56e-74

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 6.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFtgilsP--W-KGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVS 325
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 326 KWRGDSEKLVRVLFELARYHA-----PSTIFLDELESVMSQRGTASGGEhegsLRMKTELLVQMDGLA-RSEDL-VFVLA 398
Cdd:NF041006  173 KWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGE----VRVRNQFLKEMDGLQdKSENYhVYVIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 399 ASNLPWELDCAMLRRLEKRILVDLPSREARQAMIYHWlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMR 478
Cdd:NF041006  249 ATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY------TSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMR 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911146 479 PVRKIFdalENHQSEssdlPRiqldIVTTADFLDVLTHTKPSA-KNLAQRYSDWQREF 535
Cdd:NF041006  323 VVKEMF---EKGLGE----PR----PITMEDFKEVLKIRKPSVnQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 242-538 2.17e-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: 223.25  E-value: 2.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 242 RDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISA 320
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMgIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 321 STIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGgeHEGSLRMKTELLVQMDGLARSEDLVfVLAAS 400
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFD--TSVTDRIVNQLLTEMDGIQELSNVV-VIAAT 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 401 NLPWELDCAMLR--RLEKRILVDLPSREARQAMI-YHwlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAM 477
Cdd:TIGR01243 598 NRPDILDPALLRpgRFDRLILVPPPDEEARKEIFkIH-------TRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAM 670

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533911146 478 RPVRKIFDALENHQSESSDLPRIQLDIVTTADFLDVLTHTKPS-AKNLAQRYSDWQREFESV 538
Cdd:TIGR01243 671 AALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSvSKEDMLRYERLAKELKRL 732
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 253-523 1.16e-61

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: 207.84  E-value: 1.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 253 WNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS 331
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 332 EKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGLarsEDLVFVLAASNLPWELDCAML 411
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGR---RVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 412 RRLEKRILVDLPSREARQAMIYHWLPPvsksraLELHTELEYSVLSQETEGYSGSDIKLVCREAAMRpvrkifdALenhq 491
Cdd:COG0464   310 RRFDEIIFFPLPDAEERLEIFRIHLRK------RPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ-------AL---- 372

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1533911146 492 sessdlpRIQLDIVTTADFLDVLTHTKPSAKN 523
Cdd:COG0464   373 -------RLGREPVTTEDLLEALEREDIFLKR 397
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 249-512 8.74e-57

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 194.67  E-value: 8.74e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFT--GIlSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSK 326
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 327 WRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQR---GTasGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLP 403
Cdd:PRK03992  205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGT--SGDREVQ-RTLMQLLAEMDGFDPRGN-VKIIAATNRI 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 404 WELDCAMLR--RLEKRILVDLPSREARqAMIyhwlppvsksraLELHT-------ELEYSVLSQETEGYSGSDIKLVCRE 474
Cdd:PRK03992  281 DILDPAILRpgRFDRIIEVPLPDEEGR-LEI------------LKIHTrkmnladDVDLEELAELTEGASGADLKAICTE 347

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1533911146 475 AAMRPVRkifdalENHqsessdlpriqlDIVTTADFLD 512
Cdd:PRK03992  348 AGMFAIR------DDR------------TEVTMEDFLK 367
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 290-422 1.91e-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: 161.22  E-value: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGE 369
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533911146 370 HEgslRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDL 422
Cdd:pfam00004  81 SR---RVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 286-423 9.08e-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: 71.64  E-value: 9.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146  286 PWKGLLLYGPPGTGKTLLAKAVATECKTT---FFNISASTI--------------VSKWRGDSEKLVRVLFELARYHAPS 348
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533911146  349 TIFLDELESVMSQRGTAsggehegsLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLP 423
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 ...
 450-494 3.21e-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: 3.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1533911146 450 ELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFDALENHQSES 494
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 290-355 5.04e-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: 41.69  E-value: 5.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATEC-----KTTFFniSASTIVSKWRG--DSEKLVRVLFELARYHApstIFLDEL 355
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFT--TAADLVEQLAQarADGRLGRLLRRLARYDL---LIIDEL 160
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 25-55 5.49e-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: 5.49e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1533911146   25 RRKNLLILISHYLTQEGYIDTANALEQETKL 55
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 28-52 5.51e-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: 5.51e-03
                          10        20
                  ....*....|....*....|....*
gi 1533911146  28 NLLILISHYLTQEGYIDTANALEQE 52
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 ...
 256-420 2.44e-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: 258.82  E-value: 2.44e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 256 IIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLV 335
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 336 RVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRRL 414
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRF 157


                  ....*.
gi 1533911146 415 EKRILV 420
Cdd:cd19509   158 EKRIYI 163
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 255-420 5.71e-81

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: 5.71e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKL 334
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 335 VRVLFELARYHAPSTIFLDELESVMSQRGTasGGEHEGSLRMKTELLVQMDGLARSED------LVFVLAASNLPWELDC 408
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGASEnddpskMVMVLAATNFPWDIDE 158

                         170
                  ....*....|..
gi 1533911146 409 AMLRRLEKRILV 420
Cdd:cd19522   159 ALRRRLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 249-420 2.73e-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: 245.93  E-value: 2.73e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWR 328
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 329 GDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDC 408
Cdd:cd19521    82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDS 158

                         170
                  ....*....|..
gi 1533911146 409 AMLRRLEKRILV 420
Cdd:cd19521   159 AIRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 186-522 1.01e-78

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 250.31  E-value: 1.01e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 186 IIDFQGLLTDAIKGATSELALNTFDHNPDPSERLLKPLSAFIGMNSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQL 265
Cdd:COG1222    10 NIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 266 VKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARY 344
Cdd:COG1222    90 IREAVELPLKNPELFRKYgIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELARE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 345 HAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRILVDL 422
Cdd:COG1222   170 KAPSIIFIDEIDAIAARRT--DDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEVPL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 423 PSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKifdalenhqsessdlpriQL 502
Cdd:COG1222   247 PDEEAREEILKIHL------RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE------------------GR 302

                         330       340
                  ....*....|....*....|
gi 1533911146 503 DIVTTADFLDVLTHTKPSAK 522
Cdd:COG1222   303 DTVTMEDLEKAIEKVKKKTE 322
cell_div_CdvC NF041006
cell division protein CdvC;
249-535 6.56e-74

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 6.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFtgilsP--W-KGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVS 325
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 326 KWRGDSEKLVRVLFELARYHA-----PSTIFLDELESVMSQRGTASGGEhegsLRMKTELLVQMDGLA-RSEDL-VFVLA 398
Cdd:NF041006  173 KWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGE----VRVRNQFLKEMDGLQdKSENYhVYVIG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 399 ASNLPWELDCAMLRRLEKRILVDLPSREARQAMIYHWlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMR 478
Cdd:NF041006  249 ATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY------TSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMR 322

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911146 479 PVRKIFdalENHQSEssdlPRiqldIVTTADFLDVLTHTKPSA-KNLAQRYSDWQREF 535
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; ...
 235-420 1.75e-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: 1.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 235 ELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTT 314
Cdd:cd19525     3 KMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGAT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 315 FFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTasgGEHEGSLRMKTELLVQMDGL-ARSEDL 393
Cdd:cd19525    83 FFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGAtTSSEDR 159

                         170       180
                  ....*....|....*....|....*..
gi 1533911146 394 VFVLAASNLPWELDCAMLRRLEKRILV 420
Cdd:cd19525   160 ILVVGATNRPQEIDEAARRRLVKRLYI 186
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 242-538 2.17e-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: 223.25  E-value: 2.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 242 RDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISA 320
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMgIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 321 STIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGgeHEGSLRMKTELLVQMDGLARSEDLVfVLAAS 400
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFD--TSVTDRIVNQLLTEMDGIQELSNVV-VIAAT 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 401 NLPWELDCAMLR--RLEKRILVDLPSREARQAMI-YHwlppvskSRALELHTELEYSVLSQETEGYSGSDIKLVCREAAM 477
Cdd:TIGR01243 598 NRPDILDPALLRpgRFDRLILVPPPDEEARKEIFkIH-------TRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAM 670

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533911146 478 RPVRKIFDALENHQSESSDLPRIQLDIVTTADFLDVLTHTKPS-AKNLAQRYSDWQREFESV 538
Cdd:TIGR01243 671 AALRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSvSKEDMLRYERLAKELKRL 732
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 255-420 8.23e-64

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: 205.47  E-value: 8.23e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKL 334
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 335 VRVLFELARYHAPSTIFLDELESVMSQRgtaSGGEHEGSLRMKTELLVQMDGL-ARSEDLVFVLAASNLPWELDCAMLRR 413
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSER---SEGEHEASRRLKTEFLIEFDGVqSNGDDRVLVMGATNRPQELDDAVLRR 157


                  ....*..
gi 1533911146 414 LEKRILV 420
Cdd:cd19524   158 FTKRVYV 164
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 253-523 1.16e-61

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: 207.84  E-value: 1.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 253 WNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS 331
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 332 EKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGLarsEDLVFVLAASNLPWELDCAML 411
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGR---RVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 412 RRLEKRILVDLPSREARQAMIYHWLPPvsksraLELHTELEYSVLSQETEGYSGSDIKLVCREAAMRpvrkifdALenhq 491
Cdd:COG0464   310 RRFDEIIFFPLPDAEERLEIFRIHLRK------RPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ-------AL---- 372

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1533911146 492 sessdlpRIQLDIVTTADFLDVLTHTKPSAKN 523
Cdd:COG0464   373 -------RLGREPVTTEDLLEALEREDIFLKR 397
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 249-512 8.74e-57

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 194.67  E-value: 8.74e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFT--GIlSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSK 326
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGI-EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 327 WRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQR---GTasGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLP 403
Cdd:PRK03992  205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGT--SGDREVQ-RTLMQLLAEMDGFDPRGN-VKIIAATNRI 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 404 WELDCAMLR--RLEKRILVDLPSREARqAMIyhwlppvsksraLELHT-------ELEYSVLSQETEGYSGSDIKLVCRE 474
Cdd:PRK03992  281 DILDPAILRpgRFDRIIEVPLPDEEGR-LEI------------LKIHTrkmnladDVDLEELAELTEGASGADLKAICTE 347

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1533911146 475 AAMRPVRkifdalENHqsessdlpriqlDIVTTADFLD 512
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; ...
 255-420 5.68e-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: 179.93  E-value: 5.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLF--TGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSE 332
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 333 KLVRVLFELARYHAPSTIFLDELESVMSQRgtaSGGEHEGSLRMKTELLVQMDGLARS-EDLVFVLAASNLPWELDCAML 411
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR---SSTDHEATAMMKAEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAIL 157


                  ....*....
gi 1533911146 412 RRLEKRILV 420
Cdd:cd19520   158 RRMPKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 230-521 3.09e-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: 186.65  E-value: 3.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 230 NSEMRELAAVVSRDIYLHNPNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVA 308
Cdd:TIGR01243 154 ATEVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLgIEPPKGVLLYGPPGTGKTLLAKAVA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 309 TECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGgehEGSLRMKTELLVQMDGLa 388
Cdd:TIGR01243 234 NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGL- 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 389 RSEDLVFVLAASNLPWELDCAMLR--RLEKRILVDLPSREARQAMiyhwLPPVSKSRALELHTELEYsvLSQETEGYSGS 466
Cdd:TIGR01243 310 KGRGRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEI----LKVHTRNMPLAEDVDLDK--LAEVTHGFVGA 383

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1533911146 467 DIKLVCREAAMRPVRKIFDAlENHQSESSDLPRIQLD--IVTTADFLDVLTHTKPSA 521
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 ...
 262-420 7.86e-50

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: 7.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 262 AKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFE 340
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLgIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 341 LARYHAPSTIFLDELESVMSQRGTASGGehEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRI 418
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSS--GVTDRVVSQLLTELDGIESLKG-VVVIAATNRPDMIDPALLRpgRLDKLI 157


                  ..
gi 1533911146 419 LV 420
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 ...
 255-418 8.99e-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: 163.23  E-value: 8.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEK 333
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALgLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 334 LVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGLArSEDLVFVLAASNLPWELDCAMLR- 412
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMS-SRGKVVVIAATNRPDAIDPALRRp 156


                  ....*..
gi 1533911146 413 -RLEKRI 418
Cdd:cd19503   157 gRFDREV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 290-422 1.91e-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: 161.22  E-value: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGE 369
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533911146 370 HEgslRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDL 422
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 ...
 263-420 8.86e-47

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: 8.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 263 KQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFEL 341
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLKFgMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 342 ARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRIL 419
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKN-VFIIGATNRPDIIDPAILRpgRLDQLIY 160


                  .
gi 1533911146 420 V 420
Cdd:cd19528   161 I 161
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 251-420 1.73e-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: 1.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 251 IKWNDIIGLDAAKQLVKEAVVYpIRYPQLFT--GILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWR 328
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 329 GDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDC 408
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTG-VIVIAATNRPDVLDP 157

                         170
                  ....*....|....
gi 1533911146 409 AMLR--RLEKRILV 420
Cdd:cd19501   158 ALLRpgRFDRQVYV 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 249-482 6.96e-46

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 165.71  E-value: 6.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKW 327
Cdd:PTZ00454  140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIgIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 328 RGDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELD 407
Cdd:PTZ00454  220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTN-VKVIMATNRADTLD 298

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533911146 408 CAMLR--RLEKRILVDLPSREARQaMIYHWLppVSKsraLELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVRK 482
Cdd:PTZ00454  299 PALLRpgRLDRKIEFPLPDRRQKR-LIFQTI--TSK---MNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 253-418 1.19e-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: 157.88  E-value: 1.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 253 WNDIIGLDAAKQLVKEAVVYPIRYPQLFT--GILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGD 330
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 331 SEKLVRVLFELARYHAPSTIFLDELESVMSQR-GTASGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCA 409
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfDSGTGGDREVQ-RTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPA 158

                         170
                  ....*....|.
gi 1533911146 410 MLR--RLEKRI 418
Cdd:cd19502   159 LLRpgRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 262-420 4.07e-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: 156.12  E-value: 4.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 262 AKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFE 340
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLgIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 341 LARYHAPSTIFLDELESVMSQRGTasGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCAMLR--RLEKRI 418
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGT--TGDSGVTERVVNQLLTELDGLEEMNGVV-VIAATNRPDIIDPALLRagRFDRLI 157


                  ..
gi 1533911146 419 LV 420
Cdd:cd19529   158 YI 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 262-420 8.58e-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: 149.74  E-value: 8.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 262 AKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFEL 341
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 342 ARYHAPSTIFLDELESVMSQRGtaSGGEHEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLEKRIL 419
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRD--SSGESGELRRVLNQLLTELDGVNSRSK-VLVIAATNRPDLLDPALLRpgRFDEVIE 157


                  .
gi 1533911146 420 V 420
Cdd:cd19481   158 F 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 249-481 1.65e-42

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 157.63  E-value: 1.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 249 PNIKWNDIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKW 327
Cdd:PTZ00361  178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIgIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 328 RGDSEKLVRVLFELARYHAPSTIFLDELESVMSQR-GTASGGEHEGSLRMkTELLVQMDGLARSEDlVFVLAASNLPWEL 406
Cdd:PTZ00361  258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRyDATSGGEKEIQRTM-LELLNQLDGFDSRGD-VKVIMATNRIESL 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 407 DCAMLR--RLEKRILVDLPSREarqamiyhwlppvSKSRALELHT---------ELEYSVLSQETegYSGSDIKLVCREA 475
Cdd:PTZ00361  336 DPALIRpgRIDRKIEFPNPDEK-------------TKRRIFEIHTskmtlaedvDLEEFIMAKDE--LSGADIKAICTEA 400


                  ....*.
gi 1533911146 476 AMRPVR 481
Cdd:PTZ00361  401 GLLALR 406
ftsH CHL00176
cell division protein; Validated
 251-482 9.55e-42

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 158.67  E-value: 9.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 251 IKWNDIIGLDAAKQLVKEaVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRG 329
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFEE-VVSFLKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 330 DSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCA 409
Cdd:CHL00176  259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVI-VIAATNRVDILDAA 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533911146 410 MLR--RLEKRILVDLPSREARQAMiyhwLPPVSKSRALELHTELEysVLSQETEGYSGSDIKLVCREAAMRPVRK 482
Cdd:CHL00176  338 LLRpgRFDRQITVSLPDREGRLDI----LKVHARNKKLSPDVSLE--LIARRTPGFSGADLANLLNEAAILTARR 406
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
255-481 1.53e-41

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 158.27  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVY---PIRYPQLFTGIlsPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS 331
Cdd:PRK10733  153 DVAGCDEAKEEVAELVEYlrePSRFQKLGGKI--P-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 332 EKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCAML 411
Cdd:PRK10733  230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGII-VIAATNRPDVLDPALL 308

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533911146 412 R--RLEKRILVDLPSREARQAMIYHWLppvsksRALELHTELEYSVLSQETEGYSGSDIKLVCREAAMRPVR 481
Cdd:PRK10733  309 RpgRFDRQVVVGLPDVRGREQILKVHM------RRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 255-420 2.32e-40

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 143.49  E-value: 2.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKL 334
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 335 VRVLFELARYHAPSTIFLDELESVMSQRGTasggEHEGSLRMKTELLVQMDG-LARSEDLVFVLAASNLPWELDCAMLRR 413
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGvLGSGEDGVLVVCTTSKPEEIDESLRRY 156


                  ....*..
gi 1533911146 414 LEKRILV 420
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 ...
 259-420 4.53e-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: 4.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 259 LDAAKQLVKEAVVYPIRYPQLFT--GILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVR 336
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 337 VLFELARYHAPSTIFLDELESVMSQRGtasGGEHEGSLRMKTELLVQMDGL-ARSEdlVFVLAASNLPWELDCAMLR--R 413
Cdd:cd19530    80 QVFQRARASAPCVIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLeERSN--VFVIAATNRPDIIDPAMLRpgR 154


                  ....*..
gi 1533911146 414 LEKRILV 420
Cdd:cd19530   155 LDKTLYV 161
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
253-475 1.36e-39

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 144.26  E-value: 1.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 253 WNDIIGLDAAKQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSE 332
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 333 KLVRVLFELARyHAPSTIFLDELESVMSQRGTASG-GEhegSLRMKTELLVQMDGLARSedlVFVLAASNLPWELDCAML 411
Cdd:COG1223    81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDvGE---VKRVVNALLQELDGLPSG---SVVIAATNHPELLDSALW 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1533911146 412 RRLEKRILVDLPSREARQAMIyhwlppVSKSRALELHTELEYSVLSQETEGYSGSDIKLVCREA 475
Cdd:COG1223   154 RRFDEVIEFPLPDKEERKEIL------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 255-413 8.20e-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: 8.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEK 333
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIgIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 334 LVRVLFELARYHAPSTIFLDELESVMSQRGTASGgehEGSLRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAmLRR 413
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHG---EVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPA-LRR 155
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
248-482 1.07e-38

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 149.42  E-value: 1.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 248 NPNIKWNDIIGLDAAKQLVKEAVVYpIRYPQLFT--G--IlsPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTI 323
Cdd:COG0465   136 KPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTrlGakI--P-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 324 VskwrgdsEKLV-----RV--LFELARYHAPSTIFLDELESVMSQRGTASGG---EHEGSLrmkTELLVQMDGLARSEDL 393
Cdd:COG0465   212 V-------EMFVgvgasRVrdLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGghdEREQTL---NQLLVEMDGFEGNEGV 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 394 VfVLAASNLPWELDCAMLR--RLEKRILVDLPSREARQAmIyhwlppvsksraLELHT-------ELEYSVLSQETEGYS 464
Cdd:COG0465   282 I-VIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREA-I------------LKVHArkkplapDVDLEVIARRTPGFS 347

                         250
                  ....*....|....*...
gi 1533911146 465 GSDIKLVCREAAMRPVRK 482
Cdd:COG0465   348 GADLANLVNEAALLAARR 365
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 263-420 2.64e-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: 135.33  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 263 KQLVKEAVVYPIRYPQLFTGILSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFELA 342
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 343 RYHAPSTIFLDELESVMSQRGTA--SGGEHEgslRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLR--RLEKRI 418
Cdd:cd19527    82 RDAKPCVIFFDELDSLAPSRGNSgdSGGVMD---RVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLL 158


                  ..
gi 1533911146 419 LV 420
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 ...
 262-419 3.49e-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: 3.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 262 AKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSEKLVRVLFE 340
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSpLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 341 LARYHAPSTIFLDELESVMSQRGTASGGEHEgslRMKTELLVQMDGlARSEDLVFVLAASNLPWELDCAMLR--RLEKRI 418
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDG-VEGLDGVYVLAATSRPDLIDPALLRpgRLDKLV 156


                  .
gi 1533911146 419 L 419
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 ...
 255-418 5.80e-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: 5.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLF--TGILSPwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDSE 332
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 333 KLVRVLFELARYHAPSTIFLDELESVMSQRGTASggeHEGSLRMKTELLVQMDGL---ARSEDLVFVLAASNLPWELDCA 409
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQ---REMERRIVSQLLTCMDELnneKTAGGPVLVIGATNRPDSLDPA 156

                         170
                  ....*....|.
gi 1533911146 410 MLR--RLEKRI 418
Cdd:cd19518   157 LRRagRFDREI 167
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 255-413 1.32e-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: 1.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLVKEAVVYPIRYPQLFTGI-LSPWKGLLLYGPPGTGKTLLAKAVATEC-----KTTFFNISASTIVSKWR 328
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFkITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 329 GDSEKLVRVLFELARYHAPSTIFLDELESVMSQRGTASGGEHEGslrMKTELLVQMDGL-ARSEdlVFVLAASNLPWELD 407
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS---IVSTLLALMDGLdNRGQ--VVVIGATNRPDALD 155


                  ....*.
gi 1533911146 408 CAmLRR 413
Cdd:cd19517   156 PA-LRR 160
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 257-422 1.62e-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: 91.05  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 257 IGLDAAKQLVKEAVvypirypqlftgILSPWKGLLLYGPPGTGKTLLAKAVATEC---KTTFFNISASTIVSKWRGDSEK 333
Cdd:cd00009     1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 334 ---LVRVLFELARYHAPSTIFLDELESVmsqrgtaSGGEHEGSLRMktelLVQMDGLARSEDLVFVLAASNLPWELDCAM 410
Cdd:cd00009    69 ghfLVRLLFELAEKAKPGVLFIDEIDSL-------SRGAQNALLRV----LETLNDLRIDRENVRVIGATNRPLLGDLDR 137

                         170
                  ....*....|....
gi 1533911146 411 --LRRLEKRILVDL 422
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; ...
 288-415 1.38e-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: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 288 KGLLLYGPPGTGKTLLAKAV-----ATECKTtffnISASTIVSKWRGDSEKLVRVLF-----ELARYHAPS---TIFLDE 354
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeEQRRLGANSglhIIIFDE 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533911146 355 LESVMSQRGTASGGEHEGSlRMKTELLVQMDGLARSEDlVFVLAASNLPWELDCAMLR--RLE 415
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 ...
 255-406 6.59e-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: 6.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 255 DIIGLDAAKQLV--------KEAVVYPIRYPqlftgilspwKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSK 326
Cdd:cd19507     1 DVGGLDNLKDWLkkrkaafsKQASAYGLPTP----------KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 327 WRGDSEKLVRVLFELARYHAPSTIFLDELESVMSqrGTASGGEHEGSLRMKTELLVQMdglARSEDLVFVLAASN----L 402
Cdd:cd19507    71 LVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFS--NADSKGDSGTSSRVLGTFLTWL---QEKKKPVFVVATANnvqsL 145


                  ....
gi 1533911146 403 PWEL 406
Cdd:cd19507   146 PPEL 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 286-423 9.08e-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: 71.64  E-value: 9.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146  286 PWKGLLLYGPPGTGKTLLAKAVATECKTT---FFNISASTI--------------VSKWRGDSEKLVRVLFELARYHAPS 348
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1533911146  349 TIFLDELESVMSQRGTAsggehegsLRMKTELLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRILVDLP 423
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 ...
 290-413 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 1533911146 290 LLLYGPPGTGKTLLAKAVA---------TECKTTFFNISASTIVSKWRGDSEKLVRVLF----ELAR-YHAPSTIFLDEL 355
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDdKDALVFVLIDEV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911146 356 ESVMSQRGTA-SGGEHEGSLRMKTELLVQMDGLARSEDLVfVLAASNLPWELDCAMLRR 413
Cdd:cd19508   135 ESLAAARSASsSGTEPSDAIRVVNAVLTQIDRIKRYHNNV-ILLTSNLLEKIDVAFVDR 192
ycf46 CHL00195
Ycf46; Provisional
 248-475 2.99e-13

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 71.97  E-value: 2.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 248 NPNIKWNDIIGLDAAKQ--------LVKEAVVYPIRYPqlftgilspwKGLLLYGPPGTGKTLLAKAVATECKTTFFNIS 319
Cdd:CHL00195  222 SVNEKISDIGGLDNLKDwlkkrstsFSKQASNYGLPTP----------RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLD 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 320 ASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESVMSqrGTASGGEHEGSLRMKTELLVQmdgLARSEDLVFVLAA 399
Cdd:CHL00195  292 VGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFS--NSESKGDSGTTNRVLATFITW---LSEKKSPVFVVAT 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 400 SN----LPWEldcaMLR--RLEKRILVDLPSREARQAMIYHWLppvSKSRALELHTeLEYSVLSQETEGYSGSDIKLVCR 473
Cdd:CHL00195  367 ANnidlLPLE----ILRkgRFDEIFFLDLPSLEEREKIFKIHL---QKFRPKSWKK-YDIKKLSKLSNKFSGAEIEQSII 438


                  ..
gi 1533911146 474 EA 475
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 ...
 288-419 5.59e-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: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 288 KGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRGDS--EKLVRVLFELARYHAPSTIFLDELESVMSQRGTA 365
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1533911146 366 SGGEHEGSlRMKTElLVQMDGLARSEDLVFVLAASNLPWELDCAMLRRLEKRIL 419
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 ...
 450-494 3.21e-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: 3.21e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1533911146 450 ELEYSVLSQETEGYSGSDIKLVCREAAMRPVRKIFDALENHQSES 494
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 290-354 1.24e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.91  E-value: 1.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTivskwrgDSEKLVRVLFELA---RYHAPSTI-FLDE 354
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSAVT-------SGVKDIREVIEEArerRAYGRRTIlFVDE 113
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 290-354 1.68e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.55  E-value: 1.68e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATECKTTFFNISASTivskwrgDSEKLVRVLFELARYHAPS---TI-FLDE 354
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrTIlFIDE 100
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 286-413 2.07e-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: 50.43  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 286 PWK-GLLLYGPPGTGKTLLAKAVATECKTTFFNISASTivskwRGDSEKLVRVLfeLARYHAPSTIFLDELESVMSQR-- 362
Cdd:cd19510    21 PYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHL--LNTAPKQSIILLEDIDAAFESReh 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1533911146 363 ----GTASGGEHEGSLrmkTELLVQMDGLARSEDLVFVLaASNLPWELDCAMLRR 413
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 ...
 285-418 2.97e-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: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 285 SPWKGLLLYGPPGTGKTLLAKAVATECKTTFFNISASTIVSKWRgDSEKLVRVLFELARYHAPSTI-FLDELESVMSQRG 363
Cdd:cd19512    20 GLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKRS 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1533911146 364 TASGGEhegSLRMKTELLVQMDGlARSEDLVFVLaASNLPWELDCAMLRRLEKRI 418
Cdd:cd19512    99 TEKISE---DLRAALNAFLYRTG-EQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
288-338 8.51e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.43  E-value: 8.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533911146 288 KGLLLYGPPGTGKTLLAKAVATEC--KTTFFNISASTIVSKWRGDSEKLVRVL 338
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYSAELKKTEFLMQAL 117
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 214-398 1.32e-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: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 214 DPSERLLKPLSAFIGMNSEMRELAAVVSRD------------IYLHNPNIKWNDIIGLDAAKQ---LVKEAVVYPIRYPQ 278
Cdd:TIGR03922 224 DPSYRLVTTTAETIEARTDPWDPSSAPSRAefvdpaaaerkaKLLAEAEAELAEQIGLERVKRqvaALKSSTAMALARAE 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 279 LFTGILSPWKGLLLYGPPGTGKTLLAKAVATE-C------KTTFFNISASTIVSKWRGDSEKLVRVLFELAryhAPSTIF 351
Cdd:TIGR03922 304 RGLPVAQTSNHMLFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADLIGQYIGESEAKTNEIIDSA---LGGVLF 380

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1533911146 352 LDELESVMSQRGTAsgGEHEGSLRMKTeLLVQMDglARSEDLVFVLA 398
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 ...
 288-325 2.22e-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: 2.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1533911146 288 KGLLLYGPPGTGKTLLAKAVATEC--KTTFFNISASTIVS 325
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYS 90
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 290-319 3.74e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.39  E-value: 3.74e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATECKTTFFNIS 319
Cdd:cd19500    40 LCLVGPPGVGKTSLGKSIARALGRKFVRIS 69
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 291-356 4.06e-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: 4.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533911146 291 LLYGPPGTGKTLLAKAVA-----TECKTTFFNISA---STIVSKWRGDSEKLVRV-----LFELARYHAPSTIFLDELE 356
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAellfgDERALIRIDMSEymeEHSVSRLIGAPPGYVGYeeggqLTEAVRRKPYSIVLIDEIE 85
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 290-355 5.04e-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: 41.69  E-value: 5.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATEC-----KTTFFniSASTIVSKWRG--DSEKLVRVLFELARYHApstIFLDEL 355
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFT--TAADLVEQLAQarADGRLGRLLRRLARYDL---LIIDEL 160
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
290-314 5.28e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.43  E-value: 5.28e-04
                          10        20
                  ....*....|....*....|....*....
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATE----CKTT 314
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEmgvnIRIT 82
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 25-55 5.49e-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: 5.49e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1533911146   25 RRKNLLILISHYLTQEGYIDTANALEQETKL 55
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
PRK08116 PRK08116
hypothetical protein; Validated
 289-310 5.84e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.93  E-value: 5.84e-04
                          10        20
                  ....*....|....*....|..
gi 1533911146 289 GLLLYGPPGTGKTLLAKAVATE 310
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANE 137
PRK04195 PRK04195
replication factor C large subunit; Provisional
 254-310 6.51e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.22  E-value: 6.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911146 254 NDIIGLDAAKQLVKE-AVVYPIRYPQlftgilspwKGLLLYGPPGTGKTLLAKAVATE 310
Cdd:PRK04195   14 SDVVGNEKAKEQLREwIESWLKGKPK---------KALLLYGPPGVGKTSLAHALAND 62
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 260-309 6.54e-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: 41.69  E-value: 6.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1533911146 260 DAAKQLVKEAVV---YPIRypQLFTGILSpwKG-LLLYGPPGTGKTLLAKAVAT 309
Cdd:COG0714     4 ARLRAEIGKVYVgqeELIE--LVLIALLA--GGhLLLEGVPGVGKTTLAKALAR 53
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 284-350 1.11e-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: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 284 LSPWKGLLLYGPPGTGKTLLAKAVATEC---------------KTTFFNISASTIVSKWRgDSEKLVRVLFELARYHAPS 348
Cdd:cd19505     9 LSPSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllynKPDFGNDDWIDGMLILK-ESLHRLNLQFELAKAMSPC 87


                  ..
gi 1533911146 349 TI 350
Cdd:cd19505    88 II 89
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 289-356 1.40e-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: 1.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1533911146 289 GLLLYGPPGTGKTLLAK--AVATECKTTFF-----NISASTIVSKWRGDSEKLVRVLFELARyhA---PSTIFLDELE 356
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNIDPGGASWVDGPLVR--AareGEIAVLDEIN 76
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 290-309 2.07e-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: 2.07e-03
                          10        20
                  ....*....|....*....|
gi 1533911146 290 LLLYGPPGTGKTLLAKAVAT 309
Cdd:COG0606   214 LLMIGPPGSGKTMLARRLPG 233
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
288-317 2.36e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1533911146 288 KGLLLYGPPGTGKTLLAKAVATEC-----KTTFFN 317
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTT 134
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 290-309 2.52e-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: 2.52e-03
                          10        20
                  ....*....|....*....|
gi 1533911146 290 LLLYGPPGTGKTLLAKAVAT 309
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
PRK13341 PRK13341
AAA family ATPase;
290-320 2.63e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.42  E-value: 2.63e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATECKTTFFNISA 320
Cdd:PRK13341   55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA 85
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 290-314 3.73e-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: 3.73e-03
                          10        20
                  ....*....|....*....|....*....
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATE----CKTT 314
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEmgvnIRIT 64
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
290-310 5.19e-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: 5.19e-03
                          10        20
                  ....*....|....*....|.
gi 1533911146 290 LLLYGPPGTGKTLLAKAVATE 310
Cdd:COG1474    54 VLIYGPTGTGKTAVAKYVLEE 74
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 28-52 5.51e-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: 5.51e-03
                          10        20
                  ....*....|....*....|....*
gi 1533911146  28 NLLILISHYLTQEGYIDTANALEQE 52
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
 277-309 6.62e-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: 6.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1533911146 277 PQLFTGILSPW----KG----LLLYGPPGTGKTLLAKAVAT 309
Cdd:pfam01057  95 PAEVGSVLLAWlskqFGkrntVWFYGPASTGKTNLAQAIAH 135
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 288-308 8.59e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.60  E-value: 8.59e-03
                          10        20
                  ....*....|....*....|.
gi 1533911146 288 KGLLLYGPPGTGKTLLAKAVA 308
Cdd:COG1401   222 KNVILAGPPGTGKTYLARRLA 242
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 291-369 8.64e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.05  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533911146 291 LLYGPPGTGKTLLAKAVA------------TECKTTFFNISASTIVSKWRGDSEKLVRVLFELARYHAPSTIFLDELESV 358
Cdd:PRK11034  211 LLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                          90
                  ....*....|.
gi 1533911146 359 MSQrGTASGGE 369
Cdd:PRK11034  291 IGA-GAASGGQ 300
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 288-308 8.99e-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: 8.99e-03
                          10        20
                  ....*....|....*....|...
gi 1533911146 288 KG--LLLYGPPGTGKTLLAKAVA 308
Cdd:COG0466   351 KGpiLCLVGPPGVGKTSLGKSIA 373
 
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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