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Conserved domains on  [gi|2006873046|ref|NP_001380737|]
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fidgetin-like protein 1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 383-568 1.36e-134

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: 392.81  E-value: 1.36e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 383 EPRMVELIMNEIMDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 462
Cdd:cd19525     1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 463 ATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRI 542
Cdd:cd19525    81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                         170       180
                  ....*....|....*....|....*.
gi 2006873046 543 LVVGATNRPQEIDEAARRRLVKRLYI 568
Cdd:cd19525   161 LVVGATNRPQEIDEAARRRLVKRLYI 186
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 634-674 1.10e-07

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


The actual alignment was detected with superfamily member pfam09336:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 49.03  E-value: 1.10e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2006873046 634 ISPDQV--RPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 674
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 593-624 8.20e-06

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: 43.30  E-value: 8.20e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2006873046 593 DEETELVVQQSDGFSGADMTQLCREASLGPIR 624
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
 
Name Accession Description Interval E-value
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 383-568 1.36e-134

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: 392.81  E-value: 1.36e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 383 EPRMVELIMNEIMDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 462
Cdd:cd19525     1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 463 ATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRI 542
Cdd:cd19525    81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                         170       180
                  ....*....|....*....|....*.
gi 2006873046 543 LVVGATNRPQEIDEAARRRLVKRLYI 568
Cdd:cd19525   161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 360-657 6.32e-77

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 249.15  E-value: 6.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 360 KPKSSRAGSAEPAHLTDDRLKNVEPRMVELIMNEIMDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFT--GLRgPP 437
Cdd:COG1222    34 QPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 438 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD-GE 516
Cdd:COG1222   113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGT 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 517 HESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDE 594
Cdd:COG1222   193 SGEVQRTVNQLLAELDGF--ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEI-LKIHLRDMPLADDV 269

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006873046 595 ETELVVQQSDGFSGADMTQLCREASLGPIRslhtADIATISPDqvrpiayiDFENAFRTVRPS 657
Cdd:COG1222   270 DLDKLAKLTEGFSGADLKAIVTEAGMFAIR----EGRDTVTME--------DLEKAIEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 379-674 8.29e-65

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: 227.87  E-value: 8.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 379 LKNVEPRMVELIMNEImdhgPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKC 456
Cdd:TIGR01243 432 LKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLFGPPGTGKTLLAKA 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 457 IASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES-SRRIKTEFLVQLDGAT 535
Cdd:TIGR01243 507 VATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQ 586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 536 TSSEdrILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQ 613
Cdd:TIGR01243 587 ELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEI-FKIHTRSMPLAEDVDLEELAEMTEGYTGADIEA 663

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006873046 614 LCREASLGPIR----SLHTADIATISPDQVRP--IAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 674
Cdd:TIGR01243 664 VCREAAMAALResigSPAKEKLEVGEEEFLKDlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
cell_div_CdvC NF041006
cell division protein CdvC;
388-673 1.75e-62

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 212.29  E-value: 1.75e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 388 ELIMNEimdhGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTglRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFS 467
Cdd:NF041006   91 ELVVKE----KPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP--LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIH 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 468 ISASSLTSKWVGEGEKMVRALFAVAR-----CQQPAVIFIDEIDSLLsqrgdGEHESSR----RIKTEFLVQLDGATTSS 538
Cdd:NF041006  165 VDAASIMSKWLGEAEKNVAKIFKKARekskeEGKPAIIFIDEIDALL-----GVYSSEVggevRVRNQFLKEMDGLQDKS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 539 ED-RILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVNLMSKEQcclTDEETEL--VVQQSDGFSGADMTQLC 615
Cdd:NF041006  240 ENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIK---LENDVDLdeLAEMTEGYTASDIRDIV 316

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2006873046 616 REASLGPIRSLHTADIAtispdQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTF 673
Cdd:NF041006  317 QAAHMRVVKEMFEKGLG-----EPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 440-570 7.28e-53

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 178.17  E-value: 7.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES 519
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2006873046 520 SRRIKTEFLVQLDGAtTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPL 570
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 396-655 1.00e-50

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 181.18  E-value: 1.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 396 DHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 473
Cdd:PRK03992  123 IESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV-GiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 474 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGATTSSEDRIlvVGATN 549
Cdd:PRK03992  202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGNVKI--IAATN 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 550 RPQEIDEAARR-----RLVKrlyIPLPEASARKQIV------VNLMSkeqccltDEETELVVQQSDGFSGADMTQLCREA 618
Cdd:PRK03992  279 RIDILDPAILRpgrfdRIIE---VPLPDEEGRLEILkihtrkMNLAD-------DVDLEELAELTEGASGADLKAICTEA 348

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2006873046 619 SLGPIRSLHTAdiatispdqvrpIAYIDFENAFRTVR 655
Cdd:PRK03992  349 GMFAIRDDRTE------------VTMEDFLKAIEKVM 373
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 436-572 1.54e-18

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046  436 PPKGILLFGPPGTGKTLIGKCIASQSGAT---FFSISASSLTS--------------KWVGEGEKMVRALFAVARCQQPA 498
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006873046  499 VIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQldgattsSEDRILVVGATNRPQEIDEAA-RRRLVKRLYIPLPE 572
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALlRRRFDRRIVLLLIL 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 634-674 1.10e-07

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 49.03  E-value: 1.10e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2006873046 634 ISPDQV--RPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 674
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 593-624 8.20e-06

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: 43.30  E-value: 8.20e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2006873046 593 DEETELVVQQSDGFSGADMTQLCREASLGPIR 624
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
 
Name Accession Description Interval E-value
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 383-568 1.36e-134

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: 392.81  E-value: 1.36e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 383 EPRMVELIMNEIMDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 462
Cdd:cd19525     1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 463 ATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRI 542
Cdd:cd19525    81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                         170       180
                  ....*....|....*....|....*.
gi 2006873046 543 LVVGATNRPQEIDEAARRRLVKRLYI 568
Cdd:cd19525   161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 406-568 4.12e-104

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: 313.52  E-value: 4.12e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 406 IAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMV 485
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 486 RALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKR 565
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                  ...
gi 2006873046 566 LYI 568
Cdd:cd19509   161 IYI 163
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 405-568 1.83e-85

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: 265.56  E-value: 1.83e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 484
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 485 VRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVK 564
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 2006873046 565 RLYI 568
Cdd:cd19524   161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 360-657 6.32e-77

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 249.15  E-value: 6.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 360 KPKSSRAGSAEPAHLTDDRLKNVEPRMVELIMNEIMDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFT--GLRgPP 437
Cdd:COG1222    34 QPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 438 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD-GE 516
Cdd:COG1222   113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDdGT 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 517 HESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDE 594
Cdd:COG1222   193 SGEVQRTVNQLLAELDGF--ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEI-LKIHLRDMPLADDV 269

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2006873046 595 ETELVVQQSDGFSGADMTQLCREASLGPIRslhtADIATISPDqvrpiayiDFENAFRTVRPS 657
Cdd:COG1222   270 DLDKLAKLTEGFSGADLKAIVTEAGMFAIR----EGRDTVTME--------DLEKAIEKVKKK 320
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 405-568 4.56e-74

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: 235.55  E-value: 4.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 484
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 485 VRALFAVARCQQPAVIFIDEIDSLLSQRgDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVK 564
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                  ....
gi 2006873046 565 RLYI 568
Cdd:cd19523   160 RLLV 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 399-568 5.46e-70

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: 225.13  E-value: 5.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 399 PPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 478
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 479 GEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSeDRILVVGATNRPQEIDEAA 558
Cdd:cd19521    82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDS-QGVLVLGATNIPWQLDSAI 160

                         170
                  ....*....|
gi 2006873046 559 RRRLVKRLYI 568
Cdd:cd19521   161 RRRFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 405-568 6.72e-68

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: 219.86  E-value: 6.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKM 484
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 485 VRALFAVARCQQPAVIFIDEIDSLLSQRG-DGEHESSRRIKTEFLVQLDGATTSSEDR-----ILVVGATNRPQEIDEAA 558
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRGtSEEHEASRRVKSELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 160

                         170
                  ....*....|
gi 2006873046 559 RRRLVKRLYI 568
Cdd:cd19522   161 RRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 402-664 1.91e-67

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: 226.33  E-value: 1.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 402 HWEDIAGVEFAKATIKEIVVWPMMRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 480
Cdd:COG0464   155 ILDDLGGLEEVKEELRELVALPLKRPELREEYgLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 481 GEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGattsSEDRILVVGATNRPQEIDEAARR 560
Cdd:COG0464   235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEE----LRSDVVVIAATNRPDLLDPALLR 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 561 RLVKRLYIPLPEASARKQIVVNLMSKEQCClTDEETELVVQQSDGFSGADMTQLCREASLgpirslhtadiatispdqvr 640
Cdd:COG0464   311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAAL-------------------- 369

                         250       260
                  ....*....|....*....|....
gi 2006873046 641 piayidfeNAFRTVRPSVSPKDLE 664
Cdd:COG0464   370 --------QALRLGREPVTTEDLL 385
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 405-568 2.81e-66

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: 215.37  E-value: 2.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIF--TGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE 482
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 483 KMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRL 562
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                  ....*.
gi 2006873046 563 VKRLYI 568
Cdd:cd19520   161 PKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 379-674 8.29e-65

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: 227.87  E-value: 8.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 379 LKNVEPRMVELIMNEImdhgPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKC 456
Cdd:TIGR01243 432 LKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLFGPPGTGKTLLAKA 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 457 IASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES-SRRIKTEFLVQLDGAT 535
Cdd:TIGR01243 507 VATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQ 586

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 536 TSSEdrILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQ 613
Cdd:TIGR01243 587 ELSN--VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEI-FKIHTRSMPLAEDVDLEELAEMTEGYTGADIEA 663

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006873046 614 LCREASLGPIR----SLHTADIATISPDQVRP--IAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 674
Cdd:TIGR01243 664 VCREAAMAALResigSPAKEKLEVGEEEFLKDlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
cell_div_CdvC NF041006
cell division protein CdvC;
388-673 1.75e-62

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 212.29  E-value: 1.75e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 388 ELIMNEimdhGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTglRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFS 467
Cdd:NF041006   91 ELVVKE----KPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP--LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIH 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 468 ISASSLTSKWVGEGEKMVRALFAVAR-----CQQPAVIFIDEIDSLLsqrgdGEHESSR----RIKTEFLVQLDGATTSS 538
Cdd:NF041006  165 VDAASIMSKWLGEAEKNVAKIFKKARekskeEGKPAIIFIDEIDALL-----GVYSSEVggevRVRNQFLKEMDGLQDKS 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 539 ED-RILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVVNLMSKEQcclTDEETEL--VVQQSDGFSGADMTQLC 615
Cdd:NF041006  240 ENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKIK---LENDVDLdeLAEMTEGYTASDIRDIV 316

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2006873046 616 REASLGPIRSLHTADIAtispdQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTF 673
Cdd:NF041006  317 QAAHMRVVKEMFEKGLG-----EPRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 412-568 6.32e-53

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 179.40  E-value: 6.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 412 AKATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALF 489
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKrlGIR-PPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 490 AVARCQQPAVIFIDEIDSLLSQRGD-GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKRL 566
Cdd:cd19511    80 QKARQAAPCIIFFDEIDSLAPRRGQsDSSGVTDRVVSQLLTELDGI--ESLKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                  ..
gi 2006873046 567 YI 568
Cdd:cd19511   158 YV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 440-570 7.28e-53

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 178.17  E-value: 7.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHES 519
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2006873046 520 SRRIKTEFLVQLDGAtTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPL 570
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 412-568 1.03e-52

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 178.63  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 412 AKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAV 491
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 492 ARCQQPAVIFIDEIDSLLSQRGD-GEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAARR--RLVKRLYI 568
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSsGESGELRRVLNQLLTELDGVN--SRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 368-657 1.43e-52

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: 193.58  E-value: 1.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 368 SAEPAH---LTDDRLKNVEPRMVElimnEIMDHG-PPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLR-GPPKGILL 442
Cdd:TIGR01243 142 STQPAGfvyVTEATEVEIREKPVR----EEIERKvPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLL 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 443 FGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRR 522
Cdd:TIGR01243 218 YGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKR 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 523 IKTEFLVQLDGatTSSEDRILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDEETELVV 600
Cdd:TIGR01243 298 VVAQLLTLMDG--LKGRGRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEI-LKVHTRNMPLAEDVDLDKLA 374

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006873046 601 QQSDGFSGADMTQLCREASLGPIR--------SLHTADIATISPDQVRpIAYIDFENAFRTVRPS 657
Cdd:TIGR01243 375 EVTHGFVGADLAALAKEAAMAALRrfiregkiNFEAEEIPAEVLKELK-VTMKDFMEALKMVEPS 438
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 405-560 4.64e-52

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: 177.10  E-value: 4.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE 482
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006873046 483 KMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR 560
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM--SSRGKVVVIAATNRPDAIDPALRR 155
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 396-655 1.00e-50

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 181.18  E-value: 1.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 396 DHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 473
Cdd:PRK03992  123 IESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV-GiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 474 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGATTSSEDRIlvVGATN 549
Cdd:PRK03992  202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAEMDGFDPRGNVKI--IAATN 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 550 RPQEIDEAARR-----RLVKrlyIPLPEASARKQIV------VNLMSkeqccltDEETELVVQQSDGFSGADMTQLCREA 618
Cdd:PRK03992  279 RIDILDPAILRpgrfdRIIE---VPLPDEEGRLEILkihtrkMNLAD-------DVDLEELAELTEGASGADLKAICTEA 348

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2006873046 619 SLGPIRSLHTAdiatispdqvrpIAYIDFENAFRTVR 655
Cdd:PRK03992  349 GMFAIRDDRTE------------VTMEDFLKAIEKVM 373
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 399-628 7.17e-49

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 175.37  E-value: 7.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 399 PPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 477
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGiEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 478 VGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGatTSSEDRILVVGATNRPQE 553
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDsgtsGDREVQRTL-MQLLAELDG--FDPRGNVKVIAATNRPDI 273

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006873046 554 IDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQLCREASLGPIRSLHT 628
Cdd:TIGR01242 274 LDPALLRpgRFDRIIEVPLPDFEGRLEI-LKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERD 349
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 412-568 5.06e-48

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: 166.13  E-value: 5.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 412 AKATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALF 489
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKrlGIR-PPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 490 AVARCQQPAVIFIDEIDSLLSQRG-DGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAARR--RLVKRL 566
Cdd:cd19529    80 RKARQVAPCVIFFDEIDSIAPRRGtTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLI 157


                  ..
gi 2006873046 567 YI 568
Cdd:cd19529   158 YI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 405-560 3.23e-45

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: 158.75  E-value: 3.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK 483
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006873046 484 MVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSedRILVVGATNRPQEIDEAARR 560
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPALRR 155
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 403-560 1.59e-44

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: 157.11  E-value: 1.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 403 WEDIAGVEFAKATIKEIVVWPMMRPDIFTGLrG--PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 480
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEEL-GiePPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 481 GEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSR---RIKTEFLVQLDGATTSseDRILVVGATNRPQEIDEA 557
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPR--GNIKVIMATNRPDILDPA 158


                  ...
gi 2006873046 558 ARR 560
Cdd:cd19502   159 LLR 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 395-620 2.90e-43

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 162.84  E-value: 2.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 395 MDHGPPVHWEDIAGVEFAKATIKEIVVWpMMRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 473
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 474 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDG---EHESSRRIKTEFLVQLDGATTSseDRILVVGATNR 550
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGNDEREQTLNQLLVEMDGFGTN--TGVIVIAATNR 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006873046 551 PQEIDEAARR--RLVKRLYIPLPEASARKQIV-VNLMSKEqcclTDEETEL--VVQQSDGFSGADMTQLCREASL 620
Cdd:TIGR01241 203 PDVLDPALLRpgRFDRQVVVDLPDIKGREEILkVHAKNKK----LAPDVDLkaVARRTPGFSGADLANLLNEAAL 273
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 395-654 2.97e-43

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 160.70  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 395 MDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 473
Cdd:PTZ00454  136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 474 TSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSR---RIKTEFLVQLDGATTSSEdrILVVGATNR 550
Cdd:PTZ00454  216 VQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN--VKVIMATNR 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 551 PQEIDEAARR--RLVKRLYIPLPEASARKQIVVNLMSKEQccLTDE-ETELVVQQSDGFSGADMTQLCREASLGPIRSlh 627
Cdd:PTZ00454  294 ADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMN--LSEEvDLEDFVSRPEKISAADIAAICQEAGMQAVRK-- 369

                         250       260
                  ....*....|....*....|....*..
gi 2006873046 628 taDIATISPDqvrpiayiDFENAFRTV 654
Cdd:PTZ00454  370 --NRYVILPK--------DFEKGYKTV 386
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
403-618 5.50e-43

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 155.43  E-value: 5.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 403 WEDIAGVEFAKATIKEIVVWPMMRPDiftgLRG----PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 478
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRREN----LRKfglwPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 479 GEGEKMVRALFAVARcQQPAVIFIDEIDSLLSQRGD----GEhesSRRIKTEFLVQLDGATtsseDRILVVGATNRPQEI 554
Cdd:COG1223    77 GETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDqndvGE---VKRVVNALLQELDGLP----SGSVVIAATNHPELL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 555 DEAARRRLVKRLYIPLPEASARKQIVVNLMSKEQCCLtDEETELVVQQSDGFSGADMTQLCREA 618
Cdd:COG1223   149 DSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 401-568 1.61e-42

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: 151.23  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 401 VHWEDIAGVEFAKATIKEIVVWpMMRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 479
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 480 EGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGE---HESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 556
Cdd:cd19501    80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFESNTG--VIVIAATNRPDVLDP 157

                         170
                  ....*....|....
gi 2006873046 557 AARR--RLVKRLYI 568
Cdd:cd19501   158 ALLRpgRFDRQVYV 171
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 395-624 2.15e-41

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 156.47  E-value: 2.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 395 MDHGPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 472
Cdd:PTZ00361  174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 473 LTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGD----GEHESSRRIkTEFLVQLDGATTSSEdrILVVGAT 548
Cdd:PTZ00361  253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatsgGEKEIQRTM-LELLNQLDGFDSRGD--VKVIMAT 329

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2006873046 549 NRPQEIDEAARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQLCREASLGPIR 624
Cdd:PTZ00361  330 NRIESLDPALIRpgRIDRKIEFPNPDEKTKRRI-FEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALR 406
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 420-568 9.33e-41

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: 146.09  E-value: 9.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 420 VVWPMMRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPA 498
Cdd:cd19530    12 ILRPIKRPDIYKALGiDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2006873046 499 VIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAARR--RLVKRLYI 568
Cdd:cd19530    92 VIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSN--VFVIAATNRPDIIDPAMLRpgRLDKTLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 413-568 1.52e-38

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 139.95  E-value: 1.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 413 KATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFA 490
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLkfGMT-PSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 491 VARCQQPAVIFIDEIDSLLSQRG---DGEHESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAARR--RLVKR 565
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMN--TKKNVFIIGATNRPDIIDPAILRpgRLDQL 158


                  ...
gi 2006873046 566 LYI 568
Cdd:cd19528   159 IYI 161
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
405-650 2.92e-38

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 150.96  E-value: 2.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWpMMRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK 483
Cdd:PRK10733  153 DVAGCDEAKEEVAELVEY-LREPSRFQKLGGKiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 484 MVRALFAVARCQQPAVIFIDEIDSLLSQRG---DGEHESSRRIKTEFLVQLDGatTSSEDRILVVGATNRPQEIDEAARR 560
Cdd:PRK10733  232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglGGGHDEREQTLNQMLVEMDG--FEGNEGIIVIAATNRPDVLDPALLR 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 561 --RLVKRLYIPLPEASARKQIVVNLMSKEQCClTDEETELVVQQSDGFSGADMTQLCREASLGPIRSlhtadiatispdQ 638
Cdd:PRK10733  310 pgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNEAALFAARG------------N 376

                         250
                  ....*....|..
gi 2006873046 639 VRPIAYIDFENA 650
Cdd:PRK10733  377 KRVVSMVEFEKA 388
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 405-560 3.83e-37

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: 136.38  E-value: 3.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGE 482
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 483 KMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSED--RILVVGATNRPQEIDEAARR 560
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAggPVLVIGATNRPDSLDPALRR 159
ftsH CHL00176
cell division protein; Validated
 401-639 2.43e-36

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 145.19  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 401 VHWEDIAGVEFAKATIKEIVVWpMMRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 479
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 480 EGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRG---DGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 556
Cdd:CHL00176  259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGagiGGGNDEREQTLNQLLTEMDGFKGNKG--VIVIAATNRVDILDA 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 557 AARR--RLVKRLYIPLPEASARKQIvVNLMSKEQCCLTDEETELVVQQSDGFSGADMTQLCREASLGPIRslhtADIATI 634
Cdd:CHL00176  337 ALLRpgRFDRQITVSLPDREGRLDI-LKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTAR----RKKATI 411


                  ....*
gi 2006873046 635 SPDQV 639
Cdd:CHL00176  412 TMKEI 416
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 413-568 7.55e-36

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: 132.64  E-value: 7.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 413 KATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVA 492
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 493 RCQQPAVIFIDEIDSLLSQRGDGEHESS--RRIKTEFLVQLDGATTSSEDrILVVGATNRPQEIDEAARR--RLVKRLYI 568
Cdd:cd19527    82 RDAKPCVIFFDELDSLAPSRGNSGDSGGvmDRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 405-560 6.49e-35

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: 130.32  E-value: 6.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 405 DIAGVEFAKATIKEIVVWPMMRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGA-----TFFSISASSLTSKWV 478
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 479 GEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAA 558
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPAL 158


                  ..
gi 2006873046 559 RR 560
Cdd:cd19517   159 RR 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 412-567 3.59e-34

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: 127.54  E-value: 3.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 412 AKATIKEIVVWPMMRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFA 490
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRlRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 491 VARCQQPAVIFIDEIDSLLSQRGdgeHESS---RRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKR 565
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRG---HDSTgvtDRVVNQLLTQLDGV--EGLDGVYVLAATSRPDLIDPALLRpgRLDKL 155


                  ..
gi 2006873046 566 LY 567
Cdd:cd19526   156 VY 157
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
394-620 5.94e-34

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 137.09  E-value: 5.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 394 IMDHGPPVHWEDIAGVEFAKATIKEIVvwPMMR-PDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISAS 471
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIV--DFLKdPEKFTRLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 472 SLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDG------EHESsrrikT--EFLVQLDGATTSSedRIL 543
Cdd:COG0465   210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdEREQ-----TlnQLLVEMDGFEGNE--GVI 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 544 VVGATNRPqEI-DEAARR--RLVKRLYIPLPEASARKQI--V----------VNLmskeqccltdeetELVVQQSDGFSG 608
Cdd:COG0465   283 VIAATNRP-DVlDPALLRpgRFDRQVVVDLPDVKGREAIlkVharkkplapdVDL-------------EVIARRTPGFSG 348

                         250
                  ....*....|..
gi 2006873046 609 ADMTQLCREASL 620
Cdd:COG0465   349 ADLANLVNEAAL 360
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 388-580 1.60e-32

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 132.14  E-value: 1.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 388 ELIMNEImdhgPPVHWEDIAGVEFAKATIKEIVVWPMMRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIAS---QSG 462
Cdd:TIGR03689 170 DLVLEEV----PDVTYADIGGLGSQIEQIRDAVELPFLHPELYReyGLK-PPKGVLLYGPPGCGKTLIAKAVANslaARI 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 463 AT-------FFSISASSLTSKWVGEGEKMVRALFAVARCQ----QPAVIFIDEIDSLLSQRGDG---EHESSrrIKTEFL 528
Cdd:TIGR03689 245 GAegggksyFLNIKGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGSGvssDVETT--VVPQLL 322

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 529 VQLDGatTSSEDRILVVGATNRPQEIDEAARR--RLVKRLYIPLPEASARKQIV 580
Cdd:TIGR03689 323 AEIDG--VESLDNVIVIGASNREDMIDPAILRpgRLDVKIRIERPDAEAAADIF 374
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 434-570 5.23e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 101.45  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 434 RGPPKGILLFGPPGTGKTLIGKCIA---SQSGATFFSISASSLTSKWVGEGEK---MVRALFAVARCQQPAVIFIDEIDS 507
Cdd:cd00009    16 LPPPKNLLLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006873046 508 LlsqrgdgehesSRRIKTEFLVQLDGATTSSE--DRILVVGATNRP--QEIDEAARRRLVKRLYIPL 570
Cdd:cd00009    96 L-----------SRGAQNALLRVLETLNDLRIdrENVRVIGATNRPllGDLDRALYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 438-560 1.62e-21

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: 92.17  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 438 KGILLFGPPGTGKTLIGKCIASQSGATFFSI-SASSLTSKWVGEGEKMVRALFAVARCQQPA--------VIFIDEIDSL 508
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 509 LSQRGDGEHESS--RRIKTEFLVQLDGatTSSEDRILVVGATNRPQEIDEAARR 560
Cdd:cd19504   116 CKQRGSMAGSTGvhDTVVNQLLSKIDG--VEQLNNILVIGMTNRKDLIDEALLR 167
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 436-572 1.54e-18

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046  436 PPKGILLFGPPGTGKTLIGKCIASQSGAT---FFSISASSLTS--------------KWVGEGEKMVRALFAVARCQQPA 498
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2006873046  499 VIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQldgattsSEDRILVVGATNRPQEIDEAA-RRRLVKRLYIPLPE 572
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALlRRRFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 436-559 6.01e-17

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 78.56  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 436 PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLS-QRGD 514
Cdd:cd19507    30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSnADSK 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2006873046 515 GEHESSRRIKTEFLVQLDGATTSsedrILVVGATNR----PQEIDEAAR 559
Cdd:cd19507   110 GDSGTSSRVLGTFLTWLQEKKKP----VFVVATANNvqslPPELLRKGR 154
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 438-555 4.60e-14

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: 70.25  E-value: 4.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 438 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEG--EKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDG 515
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2006873046 516 EHESS--RRIKTEFLVQLDgaTTSSEDRILVVGATNRPQEID 555
Cdd:cd19506   107 TEKQLdpKRLKKDLPKILK--SLKPEDRVLIVGTTSRPFEAD 146
ycf46 CHL00195
Ycf46; Provisional
 404-650 1.74e-13

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 73.13  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 404 EDIAGVEFAKAtikeivvWPMMRPDIFT------GLrgP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 476
Cdd:CHL00195  228 SDIGGLDNLKD-------WLKKRSTSFSkqasnyGL--PtPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 477 WVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQ---RGDGehESSRRIKTEFLVQLDGATTSsedrILVVGATNR--- 550
Cdd:CHL00195  299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNsesKGDS--GTTNRVLATFITWLSEKKSP----VFVVATANNidl 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 551 -PQEIdeaARR-RLVKRLYIPLPEASARKQIV-VNLMSKEQCCLTDEETELVVQQSDGFSGADMTQLCREA---SLGPIR 624
Cdd:CHL00195  373 lPLEI---LRKgRFDEIFFLDLPSLEEREKIFkIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAmyiAFYEKR 449

                         250       260
                  ....*....|....*....|....*.
gi 2006873046 625 SLHTADIaTISPDQVRPIAYIDFENA 650
Cdd:CHL00195  450 EFTTDDI-LLALKQFIPLAQTEKEQI 474
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 434-562 1.99e-11

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 62.54  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 434 RGPPKGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVI-FIDEIDSLLSQR 512
Cdd:cd19512    19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAIHKVFDWANTSRRGLLlFVDEADAFLRKR 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2006873046 513 G-DGEHESSRRIKTEFLVQldgaTTSSEDRILVVGATNRPQEIDEAARRRL 562
Cdd:cd19512    98 StEKISEDLRAALNAFLYR----TGEQSNKFMLVLASNQPEQFDWAINDRI 144
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 437-547 1.16e-10

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 60.86  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 437 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVG-EGEKMVRALFAvarcqqpAVIFIDEIDSLLSQRGD 514
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2006873046 515 GEHESSRR-IKTEFLVQLDGATTSSE------DRILVVGA 547
Cdd:cd19498   119 SGPDVSREgVQRDLLPIVEGSTVSTKygpvktDHILFIAA 158
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 440-509 1.73e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISAssltskwVGEGEKMVRALFAVAR----CQQPAVIFIDEI--------DS 507
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARerraYGRRTILFVDEIhrfnkaqqDA 124


                  ..
gi 2006873046 508 LL 509
Cdd:COG2256   125 LL 126
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 440-509 5.08e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.94  E-value: 5.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSltskwvgEGEKMVRALFAVARCQ----QPAVIFIDEI--------DS 507
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEIhrfnkaqqDA 111


                  ..
gi 2006873046 508 LL 509
Cdd:PRK13342  112 LL 113
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 440-568 1.67e-08

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: 55.15  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQ---------SGATFFSISASSLTSKWVGEGEKMVRALFavARCQQ-----PAVIF--ID 503
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMF--QKIQEliddkDALVFvlID 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006873046 504 EIDSLLSQR----GDGEHESSRRIKTEFLVQLDgaTTSSEDRILVVGATNRPQEIDEAARRRLVKRLYI 568
Cdd:cd19508   133 EVESLAAARsassSGTEPSDAIRVVNAVLTQID--RIKRYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 634-674 1.10e-07

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 49.03  E-value: 1.10e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2006873046 634 ISPDQV--RPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFG 674
Cdd:pfam09336  19 IPSDKLlePPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 436-557 1.15e-07

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 51.99  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 436 PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW--------------VGEGEKMVRALFAVARCQQPAVIF 501
Cdd:cd19505    11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2006873046 502 IDEIDSLLSQRGDGEHESSRRIKTEFLVQL--DGATTSSEDRILVVGATNRPQEIDEA 557
Cdd:cd19505    91 IPNIHELNVNRSTQNLEEDPKLLLGLLLNYlsRDFEKSSTRNILVIASTHIPQKVDPA 148
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 433-514 1.97e-07

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: 51.41  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 433 LRGPPKG-ILLF-GPPGTGKTLIGKCIASQSGATFFSISASSLTSkwvgEGE--------------KMVRALfAVARCQQ 496
Cdd:cd19500    31 LKGSMKGpILCLvGPPGVGKTSLGKSIARALGRKFVRISLGGVRD----EAEirghrrtyvgampgRIIQAL-KKAGTNN 105

                          90
                  ....*....|....*....
gi 2006873046 497 PaVIFIDEIDSL-LSQRGD 514
Cdd:cd19500   106 P-VFLLDEIDKIgSSFRGD 123
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 433-580 5.13e-07

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: 51.71  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 433 LRGPpkgILLFGPPGTGKTLIGKCIASQSGATFFSIS------ASSLTSKWV---GEGEKMVR--ALFAVarcqqpaVIF 501
Cdd:COG0714    30 AGGH---LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILGTYIydqQTGEFEFRpgPLFAN-------VLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 502 IDEIDsllsqRGDgehessrrIKT---------EFLVQLDGATTSSEDRILVVgATNRPQEID------EAARRRLVKRL 566
Cdd:COG0714   100 ADEIN-----RAP--------PKTqsalleameERQVTIPGGTYKLPEPFLVI-ATQNPIEQEgtyplpEAQLDRFLLKL 165

                         170
                  ....*....|....
gi 2006873046 567 YIPLPEASARKQIV 580
Cdd:COG0714   166 YIGYPDAEEEREIL 179
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 434-561 9.78e-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: 48.89  E-value: 9.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 434 RGPP--KGILLFGPPGTGKTLIgkcIASQSGATFFSISASSLTSkwVGEGEKMVRALFAVArcQQPAVIFIDEIDSLLSQ 511
Cdd:cd19510    18 RGIPyrRGYLLYGPPGTGKSSF---IAALAGELDYDICDLNLSE--VVLTDDRLNHLLNTA--PKQSIILLEDIDAAFES 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2006873046 512 RgdgEHESSRRIKTEF---------LVQLDGaTTSSEDRILVVgATNRPQEIDEAARRR 561
Cdd:cd19510    91 R---EHNKKNPSAYGGlsrvtfsglLNALDG-VASSEERIVFM-TTNHIERLDPALIRP 144
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 406-569 6.99e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 49.07  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 406 IAGVEFAKATIKEIVVWPMMRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQ-SGATFFS------ISASSLTSKWV 478
Cdd:TIGR03922 281 LERVKRQVAALKSSTAMALARAERGLPVAQTSNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQYI 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 479 GEGEKMVRALFAVArcqQPAVIFIDEIDSLLsQRGDGEHESsrrIKTEFLVQLDGATTSSEDRILVVGATNRPQ-----E 553
Cdd:TIGR03922 361 GESEAKTNEIIDSA---LGGVLFLDEAYTLV-ETGYGQKDP---FGLEAIDTLLARMENDRDRLVVIGAGYRKDldkflE 433

                         170
                  ....*....|....*.
gi 2006873046 554 IDEAARRRLVKRLYIP 569
Cdd:TIGR03922 434 VNEGLRSRFTRVIEFP 449
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 593-624 8.20e-06

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: 43.30  E-value: 8.20e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2006873046 593 DEETELVVQQSDGFSGADMTQLCREASLGPIR 624
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 440-506 8.33e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 47.59  E-value: 8.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-----EKMVR-ALFAVARCQQpAVIFIDEID 506
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvenilLKLLQaADYDVERAQR-GIVYIDEID 125
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
438-488 2.24e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.27  E-value: 2.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2006873046 438 KGILLFGPPGTGKTLIGKCIASQSGA--TFFSISASSLTSKWVGEGEKMVRAL 488
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELGEdtPFVAISGSEIYSAELKKTEFLMQAL 117
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
440-506 4.41e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 46.31  E-value: 4.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-EKMVRAL-----FAVARCQQpAVIFIDEID 506
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeAGYVGEDvENILLKLlqaadYDVEKAQR-GIVYIDEID 183
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 439-562 1.45e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.28  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 439 GILLFGPPGTGKTLIGKCIASQ-SGATFFSI------SASSLTSKW-VGEGEKMVRALFAVARCQQPAVIFIDEID---- 506
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVqltrdtTEEDLFGRRnIDPGGASWVDGPLVRAAREGEIAVLDEINranp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2006873046 507 -------SLLSQrgdgehessRRIKTEFLVQLDGAttsSEDRILVVGATNRP----QEIDEAARRRL 562
Cdd:pfam07728  81 dvlnsllSLLDE---------RRLLLPDGGELVKA---APDGFRLIATMNPLdrglNELSPALRSRF 135
PRK04195 PRK04195
replication factor C large subunit; Provisional
 400-525 1.48e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.91  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 400 PVHWEDIAGVEFAKATIKEivvWpmmrpdIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISAS-----SL 473
Cdd:PRK04195   10 PKTLSDVVGNEKAKEQLRE---W------IESWLKGkPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 474 TSKWVGEGEKMvRALFAVARcqqpAVIFIDEIDSlLSQRGD--GEHESSRRIKT 525
Cdd:PRK04195   81 IERVAGEAATS-GSLFGARR----KLILLDEVDG-IHGNEDrgGARAILELIKK 128
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
440-508 2.26e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.97  E-value: 2.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSIS----------ASSLTSkwVGEGEkmvralfavarcqqpaVIFIDEIDSL 508
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSgpalekpgdlAAILTN--LEEGD----------------VLFIDEIHRL 114
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 440-567 2.76e-04

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.95  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQ---SGATFFSISASsltskwvgegEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGE 516
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQallSDEPVIFISFL----------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2006873046 517 hesSRRIKTEFLVQLDGATTSSedrILVVGATNRPQEIDEAARRRLVKRLY 567
Cdd:cd01120    71 ---SSELLEDLAKLLRAARNTG---ITVIATIHSDKFDIDRGGSSNDERLL 115
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 440-506 6.27e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 42.73  E-value: 6.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006873046 440 ILLFGPPGTGKTLIGKCIasqsgATF----FSIS-ASSLT-SKWVGEG-EKMVRAL-----FAVARCQQpAVIFIDEID 506
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTL-----ARIldvpFAIAdATTLTeAGYVGEDvENILLKLlqaadYDVEKAER-GIIYIDEID 184
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 440-563 6.43e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 40.69  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIA----SQSG-ATFFSISASSLTSKWVGE----------GEKMvRALFAVARCQQPAVIFIDE 504
Cdd:cd00267    28 VALVGPNGSGKSTLLRAIAgllkPTSGeILIDGKDIAKLPLEELRRrigyvpqlsgGQRQ-RVALARALLLNPDLLLLDE 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2006873046 505 IDSLLSQRgdgehesSRRIKTEFLVQLdgattsSEDRILVVGATNRPQEIDEAARRRLV 563
Cdd:cd00267   107 PTSGLDPA-------SRERLLELLREL------AEEGRTVIIVTHDPELAELAADRVIV 152
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 440-508 1.10e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.52  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLtskwvgegEKMVRALFAVARCQQPAVIFIDEIDSL 508
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL--------EKPGDLAAILTNLEEGDVLFIDEIHRL 93
PRK13341 PRK13341
AAA family ATPase;
441-536 1.48e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.96  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 441 LLFGPPGTGKTLIGKCIASQSGATFFSISAssltskwVGEGEKMVRALFAVARCQ-----QPAVIFIDEI--------DS 507
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERlerhgKRTILFIDEVhrfnkaqqDA 128

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2006873046 508 LLS--QRGDgehessrrikteflVQLDGATT 536
Cdd:PRK13341  129 LLPwvENGT--------------ITLIGATT 145
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 437-506 2.18e-03

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: 39.49  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 437 PKGILLF-GPPGTGKTLIGKCIASQSG---ATFFSISASSLT-----SKWVGEGEKMVRA-----LFAVARCQQPAVIFI 502
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELLFgdeRALIRIDMSEYMeehsvSRLIGAPPGYVGYeeggqLTEAVRRKPYSIVLI 81


                  ....
gi 2006873046 503 DEID 506
Cdd:pfam07724  82 DEIE 85
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 434-505 2.47e-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: 39.02  E-value: 2.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2006873046 434 RG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKwvgegekmvRALFAVARCQQPA-VIFIDEI 505
Cdd:pfam05496  29 RGeALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP---------GDLAAILTNLEPGdVLFIDEI 93
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 433-458 3.15e-03

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 40.77  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|....*..
gi 2006873046 433 LRGPpkgILLF-GPPGTGKTLIGKCIA 458
Cdd:COG0466   350 LKGP---ILCLvGPPGVGKTSLGKSIA 373
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 438-488 3.22e-03

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 40.37  E-value: 3.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2006873046 438 KGILLFGPPGTGKTLIGKCIASQSGAT--FFSISASSLTSKWVGEGEKMVRAL 488
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEALTQAF 103
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 440-505 4.37e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.68  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQSGATFFSIS----------ASSLTSkwVGEGEkmvralfavarcqqpaVIFIDEI 505
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSgpaiekpgdlAAILTN--LEEGD----------------VLFIDEI 114
AAA_22 pfam13401
AAA domain;
440-508 7.34e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2006873046 440 ILLFGPPGTGKTLIGKCIASQ---SGATFFSISASSLTS-----KWVGEG----------EKMVRALF--AVARCQQPAV 499
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpeVRDSVVFVDLPSGTSpkdllRALLRAlglplsgrlsKEELLAALqqLLLALAVAVV 87


                  ....*....
gi 2006873046 500 IFIDEIDSL 508
Cdd:pfam13401  88 LIIDEAQHL 96
 
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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