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Conserved domains on  [gi|665394908|ref|NP_001287494|]
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spastin, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
422-586 6.59e-99

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: 301.00  E-value: 6.59e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 501
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 502 VRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 581
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD-DRVLVMGATNRPQELDDAVLRRFT 159

                 ....*
gi 665394908 582 KRVYV 586
Cdd:cd19524  160 KRVYV 164
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
230-308 6.55e-29

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


:

Pssm-ID: 239142  Cd Length: 79  Bit Score: 110.06  E-value: 6.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 230 KHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDC-WSGRGDVWDRAQRLHDKMQTNLSMARDRLHFL 308
Cdd:cd02679    2 RGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
614-665 6.44e-08

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: 49.07  E-value: 6.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665394908  614 LRRLAKITDGYSGSDLTALAKDAALEPIRELnveqvkcldisaMRAITEQDF 665
Cdd:pfam17862   4 LEELAERTEGFSGADLEALCREAALAALRRG------------LEAVTQEDL 43
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
660-692 2.31e-04

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: 39.79  E-value: 2.31e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665394908  660 ITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYG 692
Cdd:pfam09336  29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
422-586 6.59e-99

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: 301.00  E-value: 6.59e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 501
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 502 VRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 581
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD-DRVLVMGATNRPQELDDAVLRRFT 159

                 ....*
gi 665394908 582 KRVYV 586
Cdd:cd19524  160 KRVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
418-675 5.16e-73

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 239.14  E-value: 5.16e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 418 VEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 495
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 496 GDGEKLVRALFAVARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDE 574
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAiAARRTDDGTSGEVQRTVNQLLAELDGFESRGD---VLIIAATNRPDLLDP 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 575 AALR--RFTKRVYVSLPDEQTRELLLNRLLQKQgsPL-DTEALRRLAKITDGYSGSDLTALAKDAALEPIRElnveqvkc 651
Cdd:COG1222  231 ALLRpgRFDRVIEVPLPDEEAREEILKIHLRDM--PLaDDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE-------- 300
                        250       260
                 ....*....|....*....|....
gi 665394908 652 ldisAMRAITEQDFHSSLKRIRRS 675
Cdd:COG1222  301 ----GRDTVTMEDLEKAIEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
395-695 6.59e-56

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: 203.21  E-value: 6.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  395 SVKGVEQKLVQLILDEIVEggakVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLAR 472
Cdd:TIGR01243 431 ALKMVEPSAIREVLVEVPN----VRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAK 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  473 AVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA-SRRLKTEFLVEFDGL 551
Cdd:TIGR01243 506 AVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGI 585
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  552 PGNPDgdrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPL-DTEALRRLAKITDGYSGSD 628
Cdd:TIGR01243 586 QELSN---VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLaEDVDLEELAEMTEGYTGAD 660
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665394908  629 LTALAKDAALEPIRELNVE------QVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDIT 695
Cdd:TIGR01243 661 IEAVCREAAMAALRESIGSpakeklEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
412-674 7.17e-53

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 187.35  E-value: 7.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 412 VEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAAS 489
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 490 LTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLlserssseheASRRL--KT-----------EFLVEFDGLpgNPD 556
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI----------AAKRTdsGTsgdrevqrtlmQLLAEMDGF--DPR 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 557 GDrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEaLRRLAKITDGYSGSDLTALAK 634
Cdd:PRK03992 269 GN-VKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD-LEELAELTEGASGADLKAICT 346
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 665394908 635 DAALEPIRELNveqvkcldisamRAITEQDFHSSLKRIRR 674
Cdd:PRK03992 347 EAGMFAIRDDR------------TEVTMEDFLKAIEKVMG 374
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
457-588 2.12e-47

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 163.53  E-value: 2.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  457 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA 536
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665394908  537 SRRLKTEFLVEFDGLpgNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSL 588
Cdd:pfam00004  81 SRRVVNQLLTELDGF--TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
230-308 6.55e-29

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 110.06  E-value: 6.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 230 KHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDC-WSGRGDVWDRAQRLHDKMQTNLSMARDRLHFL 308
Cdd:cd02679    2 RGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
229-306 3.23e-17

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 76.58  E-value: 3.23e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665394908   229 QKHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDCWS-GRGDVWDRAQRLHDKMQTNLSMARDRLH 306
Cdd:smart00745   1 TRDYLSKAKELISKALKADEA--GNYEEALELYKKAIEYLLEGIKVESDSkRREALKAKAAEYLDRAEEIKKSLLERLA 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
453-590 1.38e-14

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 71.64  E-value: 1.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908   453 PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLT-----------------SKYVGDGEKLVRALFAVARHMQPS 515
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665394908   516 IIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGlpgnpdgdRIVVLAATNRPQELDEAALR-RFTKRVYVSLPD 590
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK--------NLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
614-665 6.44e-08

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: 49.07  E-value: 6.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665394908  614 LRRLAKITDGYSGSDLTALAKDAALEPIRELnveqvkcldisaMRAITEQDF 665
Cdd:pfam17862   4 LEELAERTEGFSGADLEALCREAALAALRRG------------LEAVTQEDL 43
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
660-692 2.31e-04

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: 39.79  E-value: 2.31e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665394908  660 ITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYG 692
Cdd:pfam09336  29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
235-268 9.42e-03

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 35.21  E-value: 9.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665394908  235 RAFEYISKAlkIDEENEGHKELAIELYRKGIKEL 268
Cdd:pfam04212   3 KALELVKKA--VEEDNAGNYEEALELYKEALDYL 34
 
Name Accession Description Interval E-value
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
422-586 6.59e-99

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: 301.00  E-value: 6.59e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 501
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 502 VRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 581
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD-DRVLVMGATNRPQELDDAVLRRFT 159

                 ....*
gi 665394908 582 KRVYV 586
Cdd:cd19524  160 KRVYV 164
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
423-586 6.83e-89

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: 275.00  E-value: 6.83e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 423 IAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLV 502
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 503 RALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFTK 582
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPE-DRVLVLGATNRPWELDEAFLRRFEK 159

                 ....
gi 665394908 583 RVYV 586
Cdd:cd19509  160 RIYI 163
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
400-586 7.29e-84

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: 262.62  E-value: 7.29e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 400 EQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECS 479
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 480 ATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDR 559
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSE-DR 159
                        170       180
                 ....*....|....*....|....*..
gi 665394908 560 IVVLAATNRPQELDEAALRRFTKRVYV 586
Cdd:cd19525  160 ILVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
418-675 5.16e-73

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 239.14  E-value: 5.16e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 418 VEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 495
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 496 GDGEKLVRALFAVARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDE 574
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAiAARRTDDGTSGEVQRTVNQLLAELDGFESRGD---VLIIAATNRPDLLDP 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 575 AALR--RFTKRVYVSLPDEQTRELLLNRLLQKQgsPL-DTEALRRLAKITDGYSGSDLTALAKDAALEPIRElnveqvkc 651
Cdd:COG1222  231 ALLRpgRFDRVIEVPLPDEEAREEILKIHLRDM--PLaDDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE-------- 300
                        250       260
                 ....*....|....*....|....
gi 665394908 652 ldisAMRAITEQDFHSSLKRIRRS 675
Cdd:COG1222  301 ----GRDTVTMEDLEKAIEKVKKK 320
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
417-586 2.31e-63

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: 208.18  E-value: 2.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 417 KVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVG 496
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 497 DGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLpGNpDGDRIVVLAATNRPQELDEAA 576
Cdd:cd19521   83 ESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGV-GN-DSQGVLVLGATNIPWQLDSAI 160
                        170
                 ....*....|
gi 665394908 577 LRRFTKRVYV 586
Cdd:cd19521  161 RRRFEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
408-673 8.88e-63

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: 214.39  E-value: 8.88e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 408 LDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNI 485
Cdd:COG0464  144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEV 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 486 SAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPgnpdgDRIVVLAA 565
Cdd:COG0464  223 DLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR-----SDVVVIAA 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 566 TNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQgsPLDTEA-LRRLAKITDGYSGSDLTALAKDAALEPIREL 644
Cdd:COG0464  298 TNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKR--PLDEDVdLEELAEATEGLSGADIRNVVRRAALQALRLG 375
                        250       260
                 ....*....|....*....|....*....
gi 665394908 645 NveqvkcldisamRAITEQDFHSSLKRIR 673
Cdd:COG0464  376 R------------EPVTTEDLLEALERED 392
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
422-586 5.83e-61

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: 201.75  E-value: 5.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 501
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 502 VRALFAVARHMQPSIIFIDEVDSL-LSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDR----IVVLAATNRPQELDEAA 576
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSIcSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDpskmVMVLAATNFPWDIDEAL 160
                        170
                 ....*....|
gi 665394908 577 LRRFTKRVYV 586
Cdd:cd19522  161 RRRLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
422-586 3.41e-60

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: 199.57  E-value: 3.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELF--TGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGE 499
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 500 KLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRR 579
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGN-CRVIVMGATNRPQDLDEAILRR 159

                 ....*..
gi 665394908 580 FTKRVYV 586
Cdd:cd19520  160 MPKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
395-695 6.59e-56

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: 203.21  E-value: 6.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  395 SVKGVEQKLVQLILDEIVEggakVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLAR 472
Cdd:TIGR01243 431 ALKMVEPSAIREVLVEVPN----VRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAK 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  473 AVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA-SRRLKTEFLVEFDGL 551
Cdd:TIGR01243 506 AVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGI 585
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  552 PGNPDgdrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPL-DTEALRRLAKITDGYSGSD 628
Cdd:TIGR01243 586 QELSN---VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLaEDVDLEELAEMTEGYTGAD 660
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665394908  629 LTALAKDAALEPIRELNVE------QVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDIT 695
Cdd:TIGR01243 661 IEAVCREAAMAALRESIGSpakeklEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
412-674 7.17e-53

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 187.35  E-value: 7.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 412 VEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAAS 489
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 490 LTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLlserssseheASRRL--KT-----------EFLVEFDGLpgNPD 556
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI----------AAKRTdsGTsgdrevqrtlmQLLAEMDGF--DPR 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 557 GDrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEaLRRLAKITDGYSGSDLTALAK 634
Cdd:PRK03992 269 GN-VKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD-LEELAELTEGASGADLKAICT 346
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 665394908 635 DAALEPIRELNveqvkcldisamRAITEQDFHSSLKRIRR 674
Cdd:PRK03992 347 EAGMFAIRDDR------------TEVTMEDFLKAIEKVMG 374
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
392-675 4.56e-49

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: 183.95  E-value: 4.56e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  392 PVVSVKGVEQKLVQLILDEIVEGGA-KVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTL 469
Cdd:TIGR01243 148 FVYVTEATEVEIREKPVREEIERKVpKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGKTL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  470 LARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFD 549
Cdd:TIGR01243 228 LAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMD 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  550 GLPGNpdgDRIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPLDTEA-LRRLAKITDGYSG 626
Cdd:TIGR01243 308 GLKGR---GRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILK--VHTRNMPLAEDVdLDKLAEVTHGFVG 382
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665394908  627 SDLTALAKDAALEPIRELNVEQVKCLDISAMRA-------ITEQDFHSSLKRIRRS 675
Cdd:TIGR01243 383 ADLAALAKEAAMAALRRFIREGKINFEAEEIPAevlkelkVTMKDFMEALKMVEPS 438
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
422-586 9.74e-48

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: 165.83  E-value: 9.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 501
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 502 VRALFAVARHMQPSIIFIDEVDsLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 581
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLD-ALLSSQDDEASPVGRLQVELLAQLDGVLGSGE-DGVLVVCTTSKPEEIDESLRRYFS 158

                 ....*
gi 665394908 582 KRVYV 586
Cdd:cd19523  159 KRLLV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
457-588 2.12e-47

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 163.53  E-value: 2.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  457 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA 536
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665394908  537 SRRLKTEFLVEFDGLpgNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSL 588
Cdd:pfam00004  81 SRRVVNQLLTELDGF--TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
413-654 2.84e-47

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: 174.40  E-value: 2.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  413 EGGAKVEWTDIAGQDVAKQALQEMV-ILPSvrPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASL 490
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVdFLKN--PSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  491 TSKYVGDGEKLVRALFAVARHMQPSIIFIDEVD---SLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATN 567
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDavgRQRGAGLGGGNDEREQTLNQLLVEMDGFGTN---TGVIVIAATN 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  568 RPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPLDTEA-LRRLAKITDGYSGSDLTALAKDAALEPIREl 644
Cdd:TIGR01241 202 RPDVLDPALLRpgRFDRQVVVDLPDIKGREEILK--VHAKNKKLAPDVdLKAVARRTPGFSGADLANLLNEAALLAARK- 278
                         250
                  ....*....|
gi 665394908  645 NVEQVKCLDI 654
Cdd:TIGR01241 279 NKTEITMNDI 288
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
422-586 6.19e-47

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 163.62  E-value: 6.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFT--GLRaPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGE 499
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 500 KLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPdgdRIVVLAATNRPQELDEAALR- 578
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG---KVVVIAATNRPDAIDPALRRp 156

                 ....*....
gi 665394908 579 -RFTKRVYV 586
Cdd:cd19503  157 gRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
429-586 1.01e-45

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: 160.14  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 429 AKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALF 506
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 507 AVARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGnpdGDRIVVLAATNRPQELDEAALR--RFTKR 583
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSlAPRRGQSDSSGVTDRVVSQLLTELDGIES---LKGVVVIAATNRPDMIDPALLRpgRLDKL 156

                 ...
gi 665394908 584 VYV 586
Cdd:cd19511  157 IYV 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
429-586 2.15e-44

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: 156.29  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 429 AKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAV 508
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 509 ARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDEAALR--RFTKRVY 585
Cdd:cd19481   81 ARRLAPCILFIDEIDAiGRKRDSSGESGELRRVLNQLLTELDGVNSR---SKVLVIAATNRPDLLDPALLRpgRFDEVIE 157

                 .
gi 665394908 586 V 586
Cdd:cd19481  158 F 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
420-678 3.17e-44

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 158.89  E-value: 3.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 420 WTDIAGQDVAKQALQEMVILPSVRPEL-FTGLrAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDG 498
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLrKFGL-WPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 499 EKLVRALFAVARHmQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgdrIVVLAATNRPQELDEAAL 577
Cdd:COG1223   80 ARNLRKLFDFARR-APCVIFFDEFDAiAKDRGDQNDVGEVKRVVNALLQELDGLPSG-----SVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 578 RRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDtEALRRLAKITDGYSGSDLTALAKDAALEPIRELNveqvkcldisam 657
Cdd:COG1223  154 RRFDEVIEFPLPDKEERKEILELNLKKFPLPFE-LDLKKLAKKLEGLSGADIEKVLKTALKKAILEDR------------ 220
                        250       260
                 ....*....|....*....|.
gi 665394908 658 RAITEQDFHSSLKRIRRSVAP 678
Cdd:COG1223  221 EKVTKEDLEEALKQRKERKKE 241
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
420-586 2.28e-43

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: 154.03  E-value: 2.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 420 WTDIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDG 498
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 499 EKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASR---RLKTEFLVEFDGLpgNPDGDrIVVLAATNRPQELDEA 575
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGF--DPRGN-IKVIMATNRPDILDPA 158
                        170
                 ....*....|...
gi 665394908 576 ALR--RFTKRVYV 586
Cdd:cd19502  159 LLRpgRFDRKIEF 171
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
418-586 2.79e-41

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 148.15  E-value: 2.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 418 VEWTDIAGQDVAKQALQEMV-ILPsvRPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 495
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVeFLK--NPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 496 GDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEH----EASRRLkTEFLVEFDGLPGNPDgdrIVVLAATNRPQE 571
Cdd:cd19501   79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGgghdEREQTL-NQLLVEMDGFESNTG---VIVIAATNRPDV 154
                        170
                 ....*....|....*..
gi 665394908 572 LDEAALR--RFTKRVYV 586
Cdd:cd19501  155 LDPALLRpgRFDRQVYV 171
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
411-686 4.80e-41

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 158.28  E-value: 4.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 411 IVEGGAKVEWTDIAGQDVAKQALQEMV-ILPSvrPELFTGL--RAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISA 487
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQEIVdFLKD--PEKFTRLgaKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 488 ASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDsllserssseheA---SR----------RLKT--EFLVEFDGLP 552
Cdd:COG0465  209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEID------------AvgrQRgaglggghdeREQTlnQLLVEMDGFE 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 553 GNpdgDRIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPLDTEA-LRRLAKITDGYSGSDL 629
Cdd:COG0465  277 GN---EGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILK--VHARKKPLAPDVdLEVIARRTPGFSGADL 351
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665394908 630 TALAKDAALepirelnveqvkcldISAMR---AITEQDFHSSLKRI-----RRSVApqsLNSYEK 686
Cdd:COG0465  352 ANLVNEAAL---------------LAARRnkkAVTMEDFEEAIDRViagpeRKSRV---ISEKEK 398
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
429-586 5.89e-39

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: 141.09  E-value: 5.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 429 AKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALF 506
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 507 AVARHMQPSIIFIDEVDSLLSERSSSEHEA-SRRLKTEFLVEFDGLpgnPDGDRIVVLAATNRPQELDEAALR--RFTKR 583
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGvTERVVNQLLTELDGL---EEMNGVVVIAATNRPDIIDPALLRagRFDRL 156

                 ...
gi 665394908 584 VYV 586
Cdd:cd19529  157 IYI 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
403-643 1.07e-37

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 146.07  E-value: 1.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 403 LVQLILDEI--------VEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELF--TGLRAPaKGLLLFGPPGNGKTLLAR 472
Cdd:PTZ00361 157 VVGILLDEVdplvsvmkVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAK 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 473 AVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASR---RLKTEFLVEFD 549
Cdd:PTZ00361 236 AVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKeiqRTMLELLNQLD 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 550 GLPGNPDgdrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEaLRRLAKITDGYSGS 627
Cdd:PTZ00361 316 GFDSRGD---VKVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVD-LEEFIMAKDELSGA 391
                        250
                 ....*....|....*.
gi 665394908 628 DLTALAKDAALEPIRE 643
Cdd:PTZ00361 392 DIKAICTEAGLLALRE 407
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
411-638 1.18e-37

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 149.41  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 411 IVEGGAKVEWTDIAGQDVAKQALQEMVIL---PSVRPELftGLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISA 487
Cdd:PRK10733 142 LTEDQIKTTFADVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISG 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 488 ASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSE---HEASRRLKTEFLVEFDGLPGNpdgDRIVVLA 564
Cdd:PRK10733 219 SDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLgggHDEREQTLNQMLVEMDGFEGN---EGIIVIA 295
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665394908 565 ATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKqgSPLDTEA-LRRLAKITDGYSGSDLTALAKDAAL 638
Cdd:PRK10733 296 ATNRPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRR--VPLAPDIdAAIIARGTPGFSGADLANLVNEAAL 370
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
422-580 2.73e-37

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: 136.80  E-value: 2.73e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEK 500
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 501 LVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDeAALRRF 580
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQR---AHVIVMAATNRPNSID-PALRRF 156
ftsH CHL00176
cell division protein; Validated
422-672 3.87e-37

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 147.50  E-value: 3.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSvRPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEK 500
Cdd:CHL00176 184 DIAGIEEAKEEFEEVVSFLK-KPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAA 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 501 LVRALFAVARHMQPSIIFIDEVDSLLSERSS---SEHEASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDEAAL 577
Cdd:CHL00176 263 RVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigGGNDEREQTLNQLLTEMDGFKGNKG---VIVIAATNRVDILDAALL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 578 R--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTeALRRLAKITDGYSGSDLTALAKDAALEPIRElnveqvkcldis 655
Cdd:CHL00176 340 RpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDV-SLELIARRTPGFSGADLANLLNEAAILTARR------------ 406
                        250
                 ....*....|....*..
gi 665394908 656 AMRAITEQDFHSSLKRI 672
Cdd:CHL00176 407 KKATITMKEIDTAIDRV 423
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
430-586 8.12e-36

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: 132.61  E-value: 8.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 430 KQALQEMVILPSVRPELFT--GLRAPAkGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFA 507
Cdd:cd19530    5 REELTMSILRPIKRPDIYKalGIDLPT-GVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 508 VARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDEAALR--RFTKRVY 585
Cdd:cd19530   84 RARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEER---SNVFVIAATNRPDIIDPAMLRpgRLDKTLY 160

                 .
gi 665394908 586 V 586
Cdd:cd19530  161 V 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
418-642 8.97e-36

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 139.51  E-value: 8.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 418 VEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVG 496
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIdPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 497 DGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASR---RLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELD 573
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN---VKVIMATNRADTLD 298
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665394908 574 EAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQ--GSPLDTEA-LRRLAKItdgySGSDLTALAKDAALEPIR 642
Cdd:PTZ00454 299 PALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMnlSEEVDLEDfVSRPEKI----SAADIAAICQEAGMQAVR 368
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
430-586 1.06e-34

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: 129.55  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 430 KQALQEMVILPSVRPELFT--GLrAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFA 507
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLkfGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 508 VARHMQPSIIFIDEVDSLLSERSSSEHE---ASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDEAALR--RFTK 582
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNTKKN---VFIIGATNRPDIIDPAILRpgRLDQ 157

                 ....
gi 665394908 583 RVYV 586
Cdd:cd19528  158 LIYI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
422-579 1.94e-34

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 129.06  E-value: 1.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELF--TGLRaPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGE 499
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 500 KLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPD-GDRIVVLAATNRPQELDeAALR 578
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTaGGPVLVIGATNRPDSLD-PALR 158

                 .
gi 665394908 579 R 579
Cdd:cd19518  159 R 159
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
430-586 3.02e-33

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: 125.32  E-value: 3.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 430 KQALQEMVILPSVRPELFT-GLRAPAkGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAV 508
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSsGLRKRS-GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 509 ARHMQPSIIFIDEVDSLLSERSSSEHEAS--RRLKTEFLVEFDGLPGNPDGdrIVVLAATNRPQELDEAALR--RFTKRV 584
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSGDSGGvmDRVVSQLLAELDGMSSSGQD--VFVIGATNRPDLLDPALLRpgRFDKLL 158

                 ..
gi 665394908 585 YV 586
Cdd:cd19527  159 YL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
429-585 1.22e-32

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: 123.31  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 429 AKQALQEMVILPSVRPELF--TGLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALF 506
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFasSPLRLR-SGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 507 AVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGnpdGDRIVVLAATNRPQELDEAALR--RFTKRV 584
Cdd:cd19526   80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEG---LDGVYVLAATSRPDLIDPALLRpgRLDKLV 156

                 .
gi 665394908 585 Y 585
Cdd:cd19526  157 Y 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
422-579 2.94e-31

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 119.92  E-value: 2.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTLLARAVATECSA-----TFLNISAASLTSKYV 495
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 496 GDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDeA 575
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNR---GQVVVIGATNRPDALD-P 156

                 ....
gi 665394908 576 ALRR 579
Cdd:cd19517  157 ALRR 160
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
230-308 6.55e-29

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 110.06  E-value: 6.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 230 KHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDC-WSGRGDVWDRAQRLHDKMQTNLSMARDRLHFL 308
Cdd:cd02679    2 RGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
424-588 4.65e-24

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: 98.76  E-value: 4.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 424 AGQDVAKQALQEMVILPsvrpelftglraPAKGLLLFGPPGNGKTLLARAVATEC---SATFLNISAASLTSKYVG---D 497
Cdd:cd00009    1 VGQEEAIEALREALELP------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 498 GEKLVRALFAVARHMQPSIIFIDEVDsllsersssehEASRRLKTEFLVEFDGL-PGNPDGDRIVVLAATNRP--QELDE 574
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEID-----------SLSRGAQNALLRVLETLnDLRIDRENVRVIGATNRPllGDLDR 137
                        170
                 ....*....|....
gi 665394908 575 AALRRFTKRVYVSL 588
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
229-306 3.23e-17

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 76.58  E-value: 3.23e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665394908   229 QKHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDCWS-GRGDVWDRAQRLHDKMQTNLSMARDRLH 306
Cdd:smart00745   1 TRDYLSKAKELISKALKADEA--GNYEEALELYKKAIEYLLEGIKVESDSkRREALKAKAAEYLDRAEEIKKSLLERLA 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
453-590 1.38e-14

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 71.64  E-value: 1.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908   453 PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLT-----------------SKYVGDGEKLVRALFAVARHMQPS 515
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665394908   516 IIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGlpgnpdgdRIVVLAATNRPQELDEAALR-RFTKRVYVSLPD 590
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK--------NLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
414-578 1.92e-14

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: 71.75  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 414 GGAKVEWTDIAgqdvaKQALQEMVILPSVRPELftGLRApAKGLLLFGPPGNGKTLLARAVATECSATFLNI-SAASLTS 492
Cdd:cd19504    3 GGLDKEFSDIF-----RRAFASRVFPPEIVEQL--GCKH-VKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 493 KYVGDGEKLVRALFAVARHMQPS--------IIFIDEVDSLLSERSSSEHEAS--RRLKTEFLVEFDGLpgnPDGDRIVV 562
Cdd:cd19504   75 KYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGSTGvhDTVVNQLLSKIDGV---EQLNNILV 151
                        170
                 ....*....|....*.
gi 665394908 563 LAATNRPQELDEAALR 578
Cdd:cd19504  152 IGMTNRKDLIDEALLR 167
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
455-584 1.55e-13

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 68.71  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 455 KGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDG--EKLVRALFAVARHMQPSIIFIDEVDSLLSERSSS 532
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665394908 533 EHEAS--RRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDEAALRRFTKRV 584
Cdd:cd19506  107 TEKQLdpKRLKKDLPKILKSLKPE---DRVLIVGTTSRPFEADLKSFCKVYNKI 157
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
422-545 1.15e-12

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: 66.24  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 422 DIAGQDVAKQALQEmvilpsvRPELFT------GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 495
Cdd:cd19507    1 DVGGLDNLKDWLKK-------RKAAFSkqasayGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLV 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665394908 496 GDGEKLVRALFAVARHMQPSIIFIDEVDSL-LSERSSSEHEASRRLKTEFL 545
Cdd:cd19507   73 GESESRLRQMIQTAEAIAPCVLWIDEIEKGfSNADSKGDSGTSSRVLGTFL 123
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
457-658 3.31e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 68.96  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 457 LLLFGPPGNGKTLLARAVATECSATFLNISAASltskyvgDGEKLVRALFAVARHM----QPSIIFIDEVdsllsersss 532
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEI---------- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 533 eHeasrRL-KT--EFLvefdgLPGNPDGDrIVVLAAT--NrPQ-ELDEAALRRftKRVYV--SLPDEQTRELLLNRLLQK 604
Cdd:PRK13342 102 -H----RFnKAqqDAL-----LPHVEDGT-ITLIGATteN-PSfEVNPALLSR--AQVFElkPLSEEDIEQLLKRALEDK 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665394908 605 QGS--PLDTEALRRLAKITDGysgsD----LTALakDAALEPIRELNVEQVK-CLDISAMR 658
Cdd:PRK13342 168 ERGlvELDDEALDALARLANG----DarraLNLL--ELAALGVDSITLELLEeALQKRAAR 222
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
457-623 1.33e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 67.00  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 457 LLLFGPPGNGKTLLARAVATECSATFLNISAasltskyVGDGEKLVRALFAVAR----HMQPSIIFIDEVdsllsersss 532
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARerraYGRRTILFVDEI---------- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 533 eHeasrRL-KTE---FL--VEfdglpgnpdgDRIVVL-AAT--------NrpqeldeAALR-RftKRVYV--SLPDEQTR 594
Cdd:COG2256  115 -H----RFnKAQqdaLLphVE----------DGTITLiGATtenpsfevN-------SALLsR--CRVFVlkPLSEEDLE 170
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665394908 595 ELL------LNRLLQKQGSPLDTEALRRLAKITDG 623
Cdd:COG2256  171 QLLeraladDERGLGGYKLELDDEALEALARLADG 205
ycf46 CHL00195
Ycf46; Provisional
421-629 1.40e-10

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 64.27  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 421 TDIAGQDVAKQALQEmvilpsvRPELFT------GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKY 494
Cdd:CHL00195 228 SDIGGLDNLKDWLKK-------RSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 495 VGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHE--ASRRLKT--EFLVEfdglPGNPdgdrIVVLAATNRPQ 570
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSgtTNRVLATfiTWLSE----KKSP----VFVVATANNID 371
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665394908 571 ELDEAALR--RFTKRVYVSLPDEQTRELL----LNRLLQKQGSPLDTEalrRLAKITDGYSGSDL 629
Cdd:CHL00195 372 LLPLEILRkgRFDEIFFLDLPSLEEREKIfkihLQKFRPKSWKKYDIK---KLSKLSNKFSGAEI 433
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
614-665 6.44e-08

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: 49.07  E-value: 6.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665394908  614 LRRLAKITDGYSGSDLTALAKDAALEPIRELnveqvkcldisaMRAITEQDF 665
Cdd:pfam17862   4 LEELAERTEGFSGADLEALCREAALAALRRG------------LEAVTQEDL 43
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
455-579 1.84e-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: 51.20  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 455 KGLLLFGPPGNGKTLLARAVATECSatfLNISAASLTSkyVGDGEKLVRALFAVARhmQPSIIFIDEVDsllSERSSSEH 534
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGELD---YDICDLNLSE--VVLTDDRLNHLLNTAP--KQSIILLEDID---AAFESREH 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 665394908 535 EASRRLKTEFL--VEFDGLPGNPDG-----DRIVVLaATNRPQELDEAALRR 579
Cdd:cd19510   94 NKKNPSAYGGLsrVTFSGLLNALDGvasseERIVFM-TTNHIERLDPALIRP 144
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
423-538 2.64e-07

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: 51.23  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 423 IAGQDVAKQAL--------QEMVILPSVRPELFtglrapAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTS-K 493
Cdd:cd19498   13 IIGQDEAKRAVaialrnrwRRMQLPEELRDEVT------PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvG 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 665394908 494 YVG-DGEKLVRALFAvarhmqpSIIFIDEVDSLLSERSSSEHEASR 538
Cdd:cd19498   87 YVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGSSGPDVSR 125
PRK04195 PRK04195
replication factor C large subunit; Provisional
418-652 5.14e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.53  E-value: 5.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 418 VEWT---------DIAGQDVAKQALQEMVilpsvrpELFTGLRaPAKGLLLFGPPGNGKTLLARAVATEcsatF------ 482
Cdd:PRK04195   2 MPWVekyrpktlsDVVGNEKAKEQLREWI-------ESWLKGK-PKKALLLYGPPGVGKTSLAHALAND----Ygwevie 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 483 LNIS---AASLTSKYVGDGEKlVRALFAVARhmqpSIIFIDEVdsllserssseheasrrlkteflvefDGLPGNpdGDR 559
Cdd:PRK04195  70 LNASdqrTADVIERVAGEAAT-SGSLFGARR----KLILLDEV--------------------------DGIHGN--EDR 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 560 ---------I------VVLAAtNRPQELDEAALRRFT-----KRVyvslpdeQTREL--LLNRLLQKQGSPLDTEALRRL 617
Cdd:PRK04195 117 ggarailelIkkakqpIILTA-NDPYDPSLRELRNAClmiefKRL-------STRSIvpVLKRICRKEGIECDDEALKEI 188
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 665394908 618 AKITDGysgsDLTALAKD--AALEPIRELNVEQVKCL 652
Cdd:PRK04195 189 AERSGG----DLRSAINDlqAIAEGYGKLTLEDVKTL 221
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
423-523 5.18e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 48.37  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 423 IAGQDVAKQALQEMVILPSVRpeLFTGLRAPAKGL-------LLFGPPGNGKTLLARAVATECSATFLNISAASLT-SKY 494
Cdd:cd19497   14 VIGQERAKKVLSVAVYNHYKR--IRNNLKQKDDDVeleksniLLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 665394908 495 VGDG-----EKLVR-ALFAVARhMQPSIIFIDEVD 523
Cdd:cd19497   92 VGEDvenilLKLLQaADYDVER-AQRGIVYIDEID 125
PRK13341 PRK13341
AAA family ATPase;
457-522 8.55e-06

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 49.28  E-value: 8.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665394908 457 LLLFGPPGNGKTLLARAVATECSATFLNISAasltskyVGDGEKLVRALFAVA-----RHMQPSIIFIDEV 522
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAkerleRHGKRTILFIDEV 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
456-580 1.04e-05

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: 45.75  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  456 GLLLFGPPGNGKTLLAR--AVATECSATFL-----NISAASLTSKYVGDGEKLVRALFAVARHMQPS-IIFIDEVDSLLS 527
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEINRANP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665394908  528 ersssehEASRRLKT-----EFLVEFDGLPGNPDGDRIVVLAATNRP----QELDEAALRRF 580
Cdd:pfam07728  81 -------DVLNSLLSllderRLLLPDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
425-523 1.11e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 48.23  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 425 GQDVAKQALqemvilpSV-------RpelftgLRAPAKGL----------LLFGPPGNGKTLLARAVatecsATFLNI-- 485
Cdd:PRK05342  75 GQERAKKVL-------SVavynhykR------LRHGDKKDddvelqksniLLIGPTGSGKTLLAQTL-----ARILDVpf 136
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 665394908 486 ---SAASLT-SKYVG-DGEK-LVRALFA----VARhMQPSIIFIDEVD 523
Cdd:PRK05342 137 aiaDATTLTeAGYVGeDVENiLLKLLQAadydVEK-AQRGIVYIDEID 183
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
457-619 1.38e-05

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: 47.47  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 457 LLLFGPPGNGKTLLARAVATECSATFLNIS------AASLT--SKYVGDGEKLV---RALFAvarhmqpSIIFIDEVDSl 525
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILgtYIYDQQTGEFEfrpGPLFA-------NVLLADEINR- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 526 lserssseheASRrlKT---------EFLVEFDG----LPgnpdgDRIVVLAATNRPQ-----ELDEAALRRFTKRVYVS 587
Cdd:COG0714  106 ----------APP--KTqsalleameERQVTIPGgtykLP-----EPFLVIATQNPIEqegtyPLPEAQLDRFLLKLYIG 168
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 665394908 588 LPDEQT-RELLLNRLLQKQGSP---LDTEALRRLAK 619
Cdd:COG0714  169 YPDAEEeREILRRHTGRHLAEVepvLSPEELLALQE 204
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
457-586 2.17e-05

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: 45.90  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 457 LLLFGPPGNGKTLLARAVATECS---------ATFLNISAASLTSKYVGDGEKLVRALFAVARHM---QPSIIF--IDEV 522
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlIDEV 134
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665394908 523 DS--LLSERSSSEHEASR--RLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDEAALRRFTKRVYV 586
Cdd:cd19508  135 ESlaAARSASSSGTEPSDaiRVVNAVLTQIDRIKRYHN---NVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
451-584 1.00e-04

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: 42.90  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 451 RAPAKGLLLFGPPGNGKTLLARAVATECSATFlnisaASLTSkyvGD----GEKLVRALFAVARHMQPS----IIFIDEV 522
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDY-----AIMTG---GDvapmGREGVTAIHKVFDWANTSrrglLLFVDEA 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665394908 523 DS-LLSERSSSEHEASRRLKTEFLVEfdglPGNPDGDRIVVLaATNRPQELDEAALRRFTKRV 584
Cdd:cd19512   91 DAfLRKRSTEKISEDLRAALNAFLYR----TGEQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
660-692 2.31e-04

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: 39.79  E-value: 2.31e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665394908  660 ITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYG 692
Cdd:pfam09336  29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
458-523 2.77e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 42.18  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  458 LLFGPPGNGKTLLARAVatecsATFLNISAASLTSK--------------------YVGDGEKLVraLFAVARHMQPSII 517
Cdd:pfam07724   7 LFLGPTGVGKTELAKAL-----AELLFGDERALIRIdmseymeehsvsrligappgYVGYEEGGQ--LTEAVRRKPYSIV 79

                  ....*.
gi 665394908  518 FIDEVD 523
Cdd:pfam07724  80 LIDEIE 85
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
449-617 3.15e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 44.07  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  449 GLRAP--AKGLLLFGPPGNGKTLLARAVATE-CSATFL------NISAASLTSKYVGDGEKLVRALFAVARHmqpSIIFI 519
Cdd:TIGR03922 305 GLPVAqtSNHMLFAGPPGTGKTTIARVVAKIyCGLGVLrkplvrEVSRADLIGQYIGESEAKTNEIIDSALG---GVLFL 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  520 DEVdsllsersSSEHEASRRLKTEF-LVEFDGLPG--NPDGDRIVVLAATNRPQ-----ELDEAALRRFTKRV-YVSL-P 589
Cdd:TIGR03922 382 DEA--------YTLVETGYGQKDPFgLEAIDTLLArmENDRDRLVVIGAGYRKDldkflEVNEGLRSRFTRVIeFPSYsP 453
                         170       180
                  ....*....|....*....|....*...
gi 665394908  590 DEQTRelLLNRLLQKQGSPLDTEALRRL 617
Cdd:TIGR03922 454 DELVE--IARRMATERDSVLDDAAADAL 479
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
457-588 4.23e-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: 40.56  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 457 LLLFGPPGNGKTLLARAVATE-CSATFLNISAASLtskyvgdgEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSsehE 535
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQaLLSDEPVIFISFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQG---D 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665394908 536 ASRRLKTEFLVEFDGLPGNpdgdRIVVLAATNRPQELDEAALRRFTKRVYVSL 588
Cdd:cd01120   70 RSSELLEDLAKLLRAARNT----GITVIATIHSDKFDIDRGGSSNDERLLKSL 118
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
455-505 4.57e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.42  E-value: 4.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665394908 455 KGLLLFGPPGNGKTLLARAVATECSAT--FLNISAASLTSKYVGDGEKLVRAL 505
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEFLMQAL 117
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
232-305 5.99e-04

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 38.83  E-value: 5.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665394908 232 HHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVD-CWSGRGDVWDRAQRLHDKMQTNLSMARDRL 305
Cdd:cd02656    2 LLQQAKELIKQAVKEDED--GNYEEALELYKEALDYLLQALKAEkEPKLRKLLRKKVKEYLDRAEFLKELLKKQK 74
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
423-523 7.64e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_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: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 41.01  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 423 IAGQDVAKQALQEMVILPSVrpelftGLRAPAKG---LLLFGPPGNGKTLLARAVA-----TECSATFLNISAAS----- 489
Cdd:cd19499   13 VVGQDEAVKAVSDAIRRARA------GLSDPNRPigsFLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEYMekhsv 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 665394908 490 -----LTSKYVGDGE--KLVRALfavaRHMQPSIIFIDEVD 523
Cdd:cd19499   87 srligAPPGYVGYTEggQLTEAV----RRKPYSVVLLDEIE 123
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
458-523 7.73e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 42.34  E-value: 7.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665394908 458 LLFGPPGNGKTLLARAVatecsATFLN----IS-AASLT-SKYVG-DGE----KLVRAL-FAVARhMQPSIIFIDEVD 523
Cdd:COG1219  113 LLIGPTGSGKTLLAQTL-----ARILDvpfaIAdATTLTeAGYVGeDVEnillKLLQAAdYDVEK-AERGIIYIDEID 184
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
422-476 9.04e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.98  E-value: 9.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665394908  422 DIAGQDVAKQALqemvilpsvrpELftglrAPAKG--LLLFGPPGNGKTLLARAVAT 476
Cdd:pfam01078   4 DVKGQEQAKRAL-----------EI-----AAAGGhnLLMIGPPGSGKTMLAKRLPG 44
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
420-674 1.21e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 41.72  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 420 WTDIAGQDVAKQALQEMVILPSVrpelftglrAPAkgLLLFGPPGNGKTLLARAVAT--------------ECSA----- 480
Cdd:COG2812    9 FDDVVGQEHVVRTLKNALASGRL---------AHA--YLFTGPRGVGKTTLARILAKalncengptgepcgECEScraia 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 481 --TFLNIS----AASLTSkyVGDGEKLVRALfavarHMQPS-----IIFIDEVdsllserssseHEASRR-----LKTef 544
Cdd:COG2812   78 agSHPDVIeidaEASNIG--VDDIRELIEKV-----SYAPVegrykVYIIDEA-----------HMLTTEafnalLKT-- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 545 LVEfdglpgnPDGDRIVVLAATN----------RPQELDeaaLRRftkrvyvsLPDEQTRElLLNRLLQKQGSPLDTEAL 614
Cdd:COG2812  138 LEE-------PPPHVVFILATTEpqkllptilsRCQRFD---FRR--------LPPEEIAE-HLAKIAEREGIEIEPEAL 198
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 615 RRLAKITDGySGSDLTALAKDAALEPIRELNvEQVkcldISAMRAITEQDFHSSLKRIRR 674
Cdd:COG2812  199 ALIARAADG-SMRDALSLLDQAIAFGLLDRR-ELL----LDLLEALLAGDVAALLALAEE 252
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
457-522 1.33e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.27  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665394908 457 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKyvGDgeklvraLFAVARHMQP-SIIFIDEV 522
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GD-------LAAILTNLEEgDVLFIDEI 111
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
394-620 1.46e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 42.10  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 394 VSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVR-----PELFTGLRAPAKGLLLFGPPGNGKT 468
Cdd:COG5635  115 KAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLeriesLKRLELLEAKKKRLLILGEPGSGKT 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 469 LLARAVATECSATFLN--------ISAASLT---------SKYVGDGEKLVRALFAVARHMQPSIIFID---EVdsllse 528
Cdd:COG5635  195 TLLRYLALELAERYLDaedpipilIELRDLAeeasledllAEALEKRGGEPEDALERLLRNGRLLLLLDgldEV------ 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 529 rsssEHEASRRLKTEFLVEF-DGLPGNpdgdRIVVlaaTNRPQELDEAALRRFTkRVYVS-LPDEQTRELLLN--RLLQK 604
Cdd:COG5635  269 ----PDEADRDEVLNQLRRFlERYPKA----RVII---TSRPEGYDSSELEGFE-VLELApLSDEQIEEFLKKwfEATER 336
                        250       260
                 ....*....|....*....|.
gi 665394908 605 QGSPL-----DTEALRRLAKI 620
Cdd:COG5635  337 KAERLlealeENPELRELARN 357
PRK08116 PRK08116
hypothetical protein; Validated
456-477 1.73e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.77  E-value: 1.73e-03
                         10        20
                 ....*....|....*....|..
gi 665394908 456 GLLLFGPPGNGKTLLARAVATE 477
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
457-522 1.75e-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: 39.41  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665394908  457 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKyvGDgeklvraLFAVARHMQP-SIIFIDEV 522
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP--GD-------LAAILTNLEPgDVLFIDEI 93
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
450-523 2.00e-03

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: 39.85  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 450 LRAPAKG--LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSK---------YVGD--GeKLVRALfAVARHMQPsI 516
Cdd:cd19500   31 LKGSMKGpiLCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmpG-RIIQAL-KKAGTNNP-V 107

                 ....*..
gi 665394908 517 IFIDEVD 523
Cdd:cd19500  108 FLLDEID 114
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
457-522 2.03e-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: 40.75  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665394908  457 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKyvGDgekLVRALFAVARHmqpSIIFIDEV 522
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GD---LAAILTNLEEG---DVLFIDEI 90
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
422-476 2.57e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 40.79  E-value: 2.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665394908 422 DIAGQDVAKQALQemvIlpsvrpelftglrAPAKG--LLLFGPPGNGKTLLARAVAT 476
Cdd:COG0606  193 DVKGQEQAKRALE---I-------------AAAGGhnLLMIGPPGSGKTMLARRLPG 233
44 PHA02544
clamp loader, small subunit; Provisional
437-681 3.35e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.97  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 437 VILPSVRPELFTGL----RAPAkgLLLFGP-PGNGKTLLARAVATECSATFLNISAASLTSKYVGDgeKLVRALFAVARH 511
Cdd:PHA02544  23 CILPAADKETFKSIvkkgRIPN--MLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFVRN--RLTRFASTVSLT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 512 MQPSIIFIDEVDsllserSSSEHEASRRLKTeFLVEFDGlpgnpdgdRIVVLAATNRPQELDEAALRRFTKrVYVSLPDE 591
Cdd:PHA02544  99 GGGKVIIIDEFD------RLGLADAQRHLRS-FMEAYSK--------NCSFIITANNKNGIIEPLRSRCRV-IDFGVPTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 592 QTRELL-------LNRLLQKQGSPLDTEAL-----------RRLAKITDGYSGS---DLTALA--KDAALEPIrelnVEQ 648
Cdd:PHA02544 163 EEQIEMmkqmivrCKGILEAEGVEVDMKVLaalvkknfpdfRRTINELQRYASTgkiDAGILSevTNSDIDDV----VEA 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 665394908 649 VKCLDISAMRAITEQ------DFHSSL-KRIRRSVAPQSL 681
Cdd:PHA02544 239 LKAKDFKAVRALAPNyandyaSFVGKLyDELYPQVTPPSI 278
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
443-521 5.32e-03

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 39.50  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908 443 RPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSA--TFLNISAASLTSKYV---GDGEKLVRALFAVARHMQPSII 517
Cdd:COG3598    2 RRWLVPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAggPWLGRRVPPGKVLYLaaeDDRGELRRRLKALGADLGLPFA 81

                 ....
gi 665394908 518 FIDE 521
Cdd:COG3598   82 DLDG 85
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
425-505 5.54e-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: 39.60  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665394908  425 GQDVAKQALQemVILPSVRPELFTGlrapaKGLLLFGPPGNGKTLLARAVATECSAT--FLNISAASLTSKYVGDGEKLV 502
Cdd:pfam06068  28 GQEKAREAAG--VIVEMIKEGKIAG-----RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEALT 100

                  ...
gi 665394908  503 RAL 505
Cdd:pfam06068 101 QAF 103
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
235-268 9.42e-03

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 35.21  E-value: 9.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665394908  235 RAFEYISKAlkIDEENEGHKELAIELYRKGIKEL 268
Cdd:pfam04212   3 KALELVKKA--VEEDNAGNYEEALELYKEALDYL 34
 
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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