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Conserved domains on  [gi|28571849|ref|NP_651206|]
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spastin, isoform B [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 ...
 484-648 7.98e-98

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: 299.84  E-value: 7.98e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 563
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 564 VRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 643
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD-DRVLVMGATNRPQELDDAVLRRFT 159


                ....*
gi 28571849 644 KRVYV 648
Cdd:cd19524 160 KRVYV 164
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 230-308 2.10e-28

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: 108.52  E-value: 2.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 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 ...
 676-727 6.36e-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: 49.46  E-value: 6.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28571849   676 LRRLAKITDGYSGSDLTALAKDAALEPIRELnveqvkcldisaMRAITEQDF 727
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 ...
 722-754 2.53e-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: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 28571849   722 ITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYG 754
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 ...
 484-648 7.98e-98

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: 299.84  E-value: 7.98e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 563
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 564 VRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 643
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD-DRVLVMGATNRPQELDDAVLRRFT 159


                ....*
gi 28571849 644 KRVYV 648
Cdd:cd19524 160 KRVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 480-737 1.49e-72

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 239.52  E-value: 1.49e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 480 VEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 557
Cdd:COG1222  75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 558 GDGEKLVRALFAVARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDE 636
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAiAARRTDDGTSGEVQRTVNQLLAELDGFESRGD---VLIIAATNRPDLLDP 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 637 AALR--RFTKRVYVSLPDEQTRELLLNRLLQKQgsPL-DTEALRRLAKITDGYSGSDLTALAKDAALEPIRElnveqvkc 713
Cdd:COG1222 231 ALLRpgRFDRVIEVPLPDEEAREEILKIHLRDM--PLaDDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE-------- 300

                       250       260
                ....*....|....*....|....
gi 28571849 714 ldisAMRAITEQDFHSSLKRIRRS 737
Cdd:COG1222 301 ----GRDTVTMEDLEKAIEKVKKK 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 457-757 7.69e-55

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: 201.29  E-value: 7.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   457 SVKGVEQKLVQLILDEIVEggakVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLAR 534
Cdd:TIGR01243 431 ALKMVEPSAIREVLVEVPN----VRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAK 505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   535 AVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA-SRRLKTEFLVEFDGL 613
Cdd:TIGR01243 506 AVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGI 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   614 PGNPDgdrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPL-DTEALRRLAKITDGYSGSD 690
Cdd:TIGR01243 586 QELSN---VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLaEDVDLEELAEMTEGYTGAD 660

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571849   691 LTALAKDAALEPIRELNVE------QVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDIT 757
Cdd:TIGR01243 661 IEAVCREAAMAALRESIGSpakeklEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 474-736 2.88e-52

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 186.58  E-value: 2.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  474 VEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAAS 551
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  552 LTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLlserssseheASRRL--KT-----------EFLVEFDGLpgNPD 618
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI----------AAKRTdsGTsgdrevqrtlmQLLAEMDGF--DPR 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  619 GDrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEaLRRLAKITDGYSGSDLTALAK 696
Cdd:PRK03992 269 GN-VKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD-LEELAELTEGASGADLKAICT 346

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28571849  697 DAALEPIRELNveqvkcldisamRAITEQDFHSSLKRIRR 736
Cdd:PRK03992 347 EAGMFAIRDDR------------TEVTMEDFLKAIEKVMG 374
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 519-650 1.94e-47

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 164.30  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   519 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA 598
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28571849   599 SRRLKTEFLVEFDGLpgNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSL 650
Cdd:pfam00004  81 SRRVVNQLLTELDGF--TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 230-308 2.10e-28

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: 108.52  E-value: 2.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 230 KHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDC-WSGRGDVWDRAQRLHDKMQTNLSMARDRLHFL 308
Cdd:cd02679   2 RGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
229-306 8.15e-17

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 75.42  E-value: 8.15e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28571849    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 ...
 515-652 1.08e-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: 72.02  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849    515 PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLT-----------------SKYVGDGEKLVRALFAVARHMQPS 577
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571849    578 IIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGlpgnpdgdRIVVLAATNRPQELDEAALR-RFTKRVYVSLPD 652
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 ...
 676-727 6.36e-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: 49.46  E-value: 6.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28571849   676 LRRLAKITDGYSGSDLTALAKDAALEPIRELnveqvkcldisaMRAITEQDF 727
Cdd:pfam17862   4 LEELAERTEGFSGADLEALCREAALAALRRG------------LEAVTQEDL 43
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 722-754 2.53e-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: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 28571849   722 ITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYG 754
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 ...
 484-648 7.98e-98

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: 299.84  E-value: 7.98e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 563
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 564 VRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 643
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD-DRVLVMGATNRPQELDDAVLRRFT 159


                ....*
gi 28571849 644 KRVYV 648
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 ...
 485-648 2.50e-88

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: 2.50e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 485 IAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLV 564
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 565 RALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFTK 644
Cdd:cd19509  81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPE-DRVLVLGATNRPWELDEAFLRRFEK 159


                ....
gi 28571849 645 RVYV 648
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; ...
 462-648 6.32e-83

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: 261.85  E-value: 6.32e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 462 EQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECS 541
Cdd:cd19525   1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 542 ATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDR 621
Cdd:cd19525  81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSE-DR 159

                       170       180
                ....*....|....*....|....*..
gi 28571849 622 IVVLAATNRPQELDEAALRRFTKRVYV 648
Cdd:cd19525 160 ILVVGATNRPQEIDEAARRRLVKRLYI 186
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 480-737 1.49e-72

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 239.52  E-value: 1.49e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 480 VEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 557
Cdd:COG1222  75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 558 GDGEKLVRALFAVARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDE 636
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAiAARRTDDGTSGEVQRTVNQLLAELDGFESRGD---VLIIAATNRPDLLDP 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 637 AALR--RFTKRVYVSLPDEQTRELLLNRLLQKQgsPL-DTEALRRLAKITDGYSGSDLTALAKDAALEPIRElnveqvkc 713
Cdd:COG1222 231 ALLRpgRFDRVIEVPLPDEEAREEILKIHLRDM--PLaDDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE-------- 300

                       250       260
                ....*....|....*....|....
gi 28571849 714 ldisAMRAITEQDFHSSLKRIRRS 737
Cdd:COG1222 301 ----GRDTVTMEDLEKAIEKVKKK 320
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 479-648 9.66e-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: 207.41  E-value: 9.66e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 479 KVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVG 558
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 559 DGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLpGNpDGDRIVVLAATNRPQELDEAA 638
Cdd:cd19521  83 ESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGV-GN-DSQGVLVLGATNIPWQLDSAI 160

                       170
                ....*....|
gi 28571849 639 LRRFTKRVYV 648
Cdd:cd19521 161 RRRFEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 470-735 1.32e-62

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 215.16  E-value: 1.32e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 470 LDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNI 547
Cdd:COG0464 144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEV 222

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 548 SAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPgnpdgDRIVVLAA 627
Cdd:COG0464 223 DLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR-----SDVVVIAA 297

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 628 TNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQgsPLDTEA-LRRLAKITDGYSGSDLTALAKDAALEPIREL 706
Cdd:COG0464 298 TNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKR--PLDEDVdLEELAEATEGLSGADIRNVVRRAALQALRLG 375

                       250       260
                ....*....|....*....|....*....
gi 28571849 707 NveqvkcldisamRAITEQDFHSSLKRIR 735
Cdd:COG0464 376 R------------EPVTTEDLLEALERED 392
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 484-648 1.26e-60

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: 1.26e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 563
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 564 VRALFAVARHMQPSIIFIDEVDSL-LSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDR----IVVLAATNRPQELDEAA 638
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSIcSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDpskmVMVLAATNFPWDIDEAL 160

                       170
                ....*....|
gi 28571849 639 LRRFTKRVYV 648
Cdd:cd19522 161 RRRLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 484-648 1.20e-59

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: 198.80  E-value: 1.20e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELF--TGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGE 561
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 562 KLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRR 641
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGN-CRVIVMGATNRPQDLDEAILRR 159


                ....*..
gi 28571849 642 FTKRVYV 648
Cdd:cd19520 160 MPKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 457-757 7.69e-55

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: 201.29  E-value: 7.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   457 SVKGVEQKLVQLILDEIVEggakVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLAR 534
Cdd:TIGR01243 431 ALKMVEPSAIREVLVEVPN----VRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAK 505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   535 AVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA-SRRLKTEFLVEFDGL 613
Cdd:TIGR01243 506 AVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGI 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   614 PGNPDgdrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPL-DTEALRRLAKITDGYSGSD 690
Cdd:TIGR01243 586 QELSN---VVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLaEDVDLEELAEMTEGYTGAD 660

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571849   691 LTALAKDAALEPIRELNVE------QVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDIT 757
Cdd:TIGR01243 661 IEAVCREAAMAALRESIGSpakeklEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKRLT 733
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 474-736 2.88e-52

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 186.58  E-value: 2.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  474 VEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAAS 551
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  552 LTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLlserssseheASRRL--KT-----------EFLVEFDGLpgNPD 618
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI----------AAKRTdsGTsgdrevqrtlmQLLAEMDGF--DPR 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  619 GDrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEaLRRLAKITDGYSGSDLTALAK 696
Cdd:PRK03992 269 GN-VKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD-LEELAELTEGASGADLKAICT 346

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28571849  697 DAALEPIRELNveqvkcldisamRAITEQDFHSSLKRIRR 736
Cdd:PRK03992 347 EAGMFAIRDDR------------TEVTMEDFLKAIEKVMG 374
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 454-737 3.56e-48

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: 182.03  E-value: 3.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   454 PVVSVKGVEQKLVQLILDEIVEGGA-KVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTL 531
Cdd:TIGR01243 148 FVYVTEATEVEIREKPVREEIERKVpKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGKTL 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   532 LARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFD 611
Cdd:TIGR01243 228 LAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMD 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   612 GLPGNpdgDRIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPLDTEA-LRRLAKITDGYSG 688
Cdd:TIGR01243 308 GLKGR---GRVIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILK--VHTRNMPLAEDVdLDKLAEVTHGFVG 382

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28571849   689 SDLTALAKDAALEPIRELNVEQVKCLDISAMRA-------ITEQDFHSSLKRIRRS 737
Cdd:TIGR01243 383 ADLAALAKEAAMAALRRFIREGKINFEAEEIPAevlkelkVTMKDFMEALKMVEPS 438
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 519-650 1.94e-47

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 164.30  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   519 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEA 598
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28571849   599 SRRLKTEFLVEFDGLpgNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSL 650
Cdd:pfam00004  81 SRRVVNQLLTELDGF--TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 484-648 2.71e-47

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: 165.06  E-value: 2.71e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKL 563
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 564 VRALFAVARHMQPSIIFIDEVDsLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDgDRIVVLAATNRPQELDEAALRRFT 643
Cdd:cd19523  81 LQASFLAARCRQPSVLFISDLD-ALLSSQDDEASPVGRLQVELLAQLDGVLGSGE-DGVLVVCTTSKPEEIDESLRRYFS 158


                ....*
gi 28571849 644 KRVYV 648
Cdd:cd19523 159 KRLLV 163
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 475-716 7.47e-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: 174.01  E-value: 7.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   475 EGGAKVEWTDIAGQDVAKQALQEMV-ILPSvrPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASL 552
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVdFLKN--PSKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   553 TSKYVGDGEKLVRALFAVARHMQPSIIFIDEVD---SLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATN 629
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDavgRQRGAGLGGGNDEREQTLNQLLVEMDGFGTN---TGVIVIAATN 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   630 RPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPLDTEA-LRRLAKITDGYSGSDLTALAKDAALEPIREl 706
Cdd:TIGR01241 202 RPDVLDPALLRpgRFDRQVVVDLPDIKGREEILK--VHAKNKKLAPDVdLKAVARRTPGFSGADLANLLNEAALLAARK- 278

                         250
                  ....*....|
gi 28571849   707 NVEQVKCLDI 716
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 ...
 484-648 1.04e-46

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: 1.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFT--GLRaPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGE 561
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 562 KLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPdgdRIVVLAATNRPQELDEAALR- 640
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG---KVVVIAATNRPDAIDPALRRp 156


                ....*....
gi 28571849 641 -RFTKRVYV 648
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 ...
 491-648 1.78e-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: 159.76  E-value: 1.78e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 491 AKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALF 568
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 569 AVARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGnpdGDRIVVLAATNRPQELDEAALR--RFTKR 645
Cdd:cd19511  80 QKARQAAPCIIFFDEIDSlAPRRGQSDSSGVTDRVVSQLLTELDGIES---LKGVVVIAATNRPDMIDPALLRpgRLDKL 156


                ...
gi 28571849 646 VYV 648
Cdd:cd19511 157 IYV 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 491-648 1.99e-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: 157.06  E-value: 1.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 491 AKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAV 570
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 571 ARHMQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDEAALR--RFTKRVY 647
Cdd:cd19481  81 ARRLAPCILFIDEIDAiGRKRDSSGESGELRRVLNQLLTELDGVNSR---SKVLVIAATNRPDLLDPALLRpgRFDEVIE 157


                .
gi 28571849 648 V 648
Cdd:cd19481 158 F 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
482-740 4.74e-44

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 158.89  E-value: 4.74e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 482 WTDIAGQDVAKQALQEMVILPSVRPEL-FTGLrAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDG 560
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLrKFGL-WPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 561 EKLVRALFAVARHmQPSIIFIDEVDS-LLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgdrIVVLAATNRPQELDEAAL 639
Cdd:COG1223  80 ARNLRKLFDFARR-APCVIFFDEFDAiAKDRGDQNDVGEVKRVVNALLQELDGLPSG-----SVVIAATNHPELLDSALW 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 640 RRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDtEALRRLAKITDGYSGSDLTALAKDAALEPIRELNveqvkcldisam 719
Cdd:COG1223 154 RRFDEVIEFPLPDKEERKEILELNLKKFPLPFE-LDLKKLAKKLEGLSGADIEKVLKTALKKAILEDR------------ 220

                       250       260
                ....*....|....*....|.
gi 28571849 720 RAITEQDFHSSLKRIRRSVAP 740
Cdd:COG1223 221 EKVTKEDLEEALKQRKERKKE 241
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 482-648 5.00e-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: 153.65  E-value: 5.00e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 482 WTDIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDG 560
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 561 EKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASR---RLKTEFLVEFDGLpgNPDGDrIVVLAATNRPQELDEA 637
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGF--DPRGN-IKVIMATNRPDILDPA 158

                       170
                ....*....|...
gi 28571849 638 ALR--RFTKRVYV 648
Cdd:cd19502 159 LLRpgRFDRKIEF 171
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 480-648 3.42e-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: 3.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 480 VEWTDIAGQDVAKQALQEMV-ILPsvRPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 557
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVeFLK--NPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 558 GDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEH----EASRRLkTEFLVEFDGLPGNPDgdrIVVLAATNRPQE 633
Cdd:cd19501  79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGgghdEREQTL-NQLLVEMDGFESNTG---VIVIAATNRPDV 154

                       170
                ....*....|....*..
gi 28571849 634 LDEAALR--RFTKRVYV 648
Cdd:cd19501 155 LDPALLRpgRFDRQVYV 171
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
473-748 8.24e-41

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 158.28  E-value: 8.24e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 473 IVEGGAKVEWTDIAGQDVAKQALQEMV-ILPSvrPELFTGL--RAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISA 549
Cdd:COG0465 132 YDEDKPKVTFDDVAGVDEAKEELQEIVdFLKD--PEKFTRLgaKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 550 ASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDsllserssseheA---SR----------RLKT--EFLVEFDGLP 614
Cdd:COG0465 209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEID------------AvgrQRgaglggghdeREQTlnQLLVEMDGFE 276

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 615 GNpdgDRIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNrlLQKQGSPLDTEA-LRRLAKITDGYSGSDL 691
Cdd:COG0465 277 GN---EGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILK--VHARKKPLAPDVdLEVIARRTPGFSGADL 351

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571849 692 TALAKDAALepirelnveqvkcldISAMR---AITEQDFHSSLKRI-----RRSVApqsLNSYEK 748
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 ...
 491-648 1.19e-38

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: 140.71  E-value: 1.19e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 491 AKQALQEMVILPSVRPELFT--GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALF 568
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 569 AVARHMQPSIIFIDEVDSLLSERSSSEHEA-SRRLKTEFLVEFDGLpgnPDGDRIVVLAATNRPQELDEAALR--RFTKR 645
Cdd:cd19529  80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGvTERVVNQLLTELDGL---EEMNGVVVIAATNRPDIIDPALLRagRFDRL 156


                ...
gi 28571849 646 VYV 648
Cdd:cd19529 157 IYI 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
473-704 3.16e-37

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 148.64  E-value: 3.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  473 IVEGGAKVEWTDIAGQDVAKQALQEMVIL---PSVRPELftGLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISA 549
Cdd:PRK10733 142 LTEDQIKTTFADVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISG 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  550 ASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSE---HEASRRLKTEFLVEFDGLPGNpdgDRIVVLA 626
Cdd:PRK10733 219 SDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLgggHDEREQTLNQMLVEMDGFEGN---EGIIVIA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  627 ATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKqgSPLDTEA-LRRLAKITDGYSGSDLTALAKDAALEPI 703
Cdd:PRK10733 296 ATNRPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRR--VPLAPDIdAAIIARGTPGFSGADLANLVNEAALFAA 373


                 .
gi 28571849  704 R 704
Cdd:PRK10733 374 R 374
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 465-705 4.26e-37

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 144.53  E-value: 4.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  465 LVQLILDEI--------VEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELF--TGLRAPaKGLLLFGPPGNGKTLLAR 534
Cdd:PTZ00361 157 VVGILLDEVdplvsvmkVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAK 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  535 AVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASR---RLKTEFLVEFD 611
Cdd:PTZ00361 236 AVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKeiqRTMLELLNQLD 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  612 GLPGNPDgdrIVVLAATNRPQELDEAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEaLRRLAKITDGYSGS 689
Cdd:PTZ00361 316 GFDSRGD---VKVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVD-LEEFIMAKDELSGA 391

                        250
                 ....*....|....*.
gi 28571849  690 DLTALAKDAALEPIRE 705
Cdd:PTZ00361 392 DIKAICTEAGLLALRE 407
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 484-642 4.75e-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: 136.41  E-value: 4.75e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEK 562
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 563 LVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDeAALRRF 642
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQR---AHVIVMAATNRPNSID-PALRRF 156
ftsH CHL00176
cell division protein; Validated
 484-734 5.26e-37

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 147.50  E-value: 5.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  484 DIAGQDVAKQALQEMVILPSvRPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEK 562
Cdd:CHL00176 184 DIAGIEEAKEEFEEVVSFLK-KPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  563 LVRALFAVARHMQPSIIFIDEVDSLLSERSSS---EHEASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDEAAL 639
Cdd:CHL00176 263 RVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKG---VIVIAATNRVDILDAALL 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  640 R--RFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTeALRRLAKITDGYSGSDLTALAKDAALEPIRElnveqvkcldis 717
Cdd:CHL00176 340 RpgRFDRQITVSLPDREGRLDILKVHARNKKLSPDV-SLELIARRTPGFSGADLANLLNEAAILTARR------------ 406

                        250
                 ....*....|....*..
gi 28571849  718 AMRAITEQDFHSSLKRI 734
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 ...
 492-648 1.15e-35

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: 132.23  E-value: 1.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 492 KQALQEMVILPSVRPELFT--GLRAPAkGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFA 569
Cdd:cd19530   5 REELTMSILRPIKRPDIYKalGIDLPT-GVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 570 VARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDEAALR--RFTKRVY 647
Cdd:cd19530  84 RARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEER---SNVFVIAATNRPDIIDPAMLRpgRLDKTLY 160


                .
gi 28571849 648 V 648
Cdd:cd19530 161 V 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 480-704 2.39e-35

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 138.74  E-value: 2.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  480 VEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRA-PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVG 558
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIdPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  559 DGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASR---RLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELD 635
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN---VKVIMATNRADTLD 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571849  636 EAALR--RFTKRVYVSLPDEQTRELLLNRLLQKQ--GSPLDTEA-LRRLAKItdgySGSDLTALAKDAALEPIR 704
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 ...
 492-648 1.23e-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: 1.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 492 KQALQEMVILPSVRPELFT--GLrAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFA 569
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLkfGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 570 VARHMQPSIIFIDEVDSLLSERSSSEHE---ASRRLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDEAALR--RFTK 644
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNTKKN---VFIIGATNRPDIIDPAILRpgRLDQ 157


                ....
gi 28571849 645 RVYV 648
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 ...
 484-641 2.63e-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: 128.68  E-value: 2.63e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELF--TGLRaPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGE 561
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 562 KLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPD-GDRIVVLAATNRPQELDeAALR 640
Cdd:cd19518  80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTaGGPVLVIGATNRPDSLD-PALR 158


                .
gi 28571849 641 R 641
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 ...
 492-648 3.81e-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: 3.81e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 492 KQALQEMVILPSVRPELFT-GLRAPAkGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAV 570
Cdd:cd19527   2 KKEILDTIQLPLEHPELFSsGLRKRS-GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 571 ARHMQPSIIFIDEVDSLLSERSSSEHEAS--RRLKTEFLVEFDGLPGNPDGdrIVVLAATNRPQELDEAALR--RFTKRV 646
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSGDSGGvmDRVVSQLLAELDGMSSSGQD--VFVIGATNRPDLLDPALLRpgRFDKLL 158


                ..
gi 28571849 647 YV 648
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 ...
 491-647 1.25e-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: 123.69  E-value: 1.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 491 AKQALQEMVILPSVRPELF--TGLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALF 568
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFasSPLRLR-SGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 569 AVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGnpdGDRIVVLAATNRPQELDEAALR--RFTKRV 646
Cdd:cd19526  80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEG---LDGVYVLAATSRPDLIDPALLRpgRLDKLV 156


                .
gi 28571849 647 Y 647
Cdd:cd19526 157 Y 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 484-641 3.62e-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: 3.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEMVILPSVRPELFTGLR-APAKGLLLFGPPGNGKTLLARAVATECSA-----TFLNISAASLTSKYV 557
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 558 GDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDeA 637
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNR---GQVVVIGATNRPDALD-P 156


                ....
gi 28571849 638 ALRR 641
Cdd:cd19517 157 ALRR 160
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 230-308 2.10e-28

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: 108.52  E-value: 2.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 230 KHHHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVDC-WSGRGDVWDRAQRLHDKMQTNLSMARDRLHFL 308
Cdd:cd02679   2 RGYYKQAFEEISKALRADEW--GDKEQALAHYRKGLRELEEGIAVPVpSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 486-650 2.84e-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: 99.53  E-value: 2.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 486 AGQDVAKQALQEMVILPsvrpelftglraPAKGLLLFGPPGNGKTLLARAVATEC---SATFLNISAASLTSKYVG---D 559
Cdd:cd00009   1 VGQEEAIEALREALELP------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 560 GEKLVRALFAVARHMQPSIIFIDEVDsllsersssehEASRRLKTEFLVEFDGL-PGNPDGDRIVVLAATNRP--QELDE 636
Cdd:cd00009  69 GHFLVRLLFELAEKAKPGVLFIDEID-----------SLSRGAQNALLRVLETLnDLRIDRENVRVIGATNRPllGDLDR 137

                       170
                ....*....|....
gi 28571849 637 AALRRFTKRVYVSL 650
Cdd:cd00009 138 ALYDRLDIRIVIPL 151
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
229-306 8.15e-17

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 75.42  E-value: 8.15e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28571849    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 ...
 515-652 1.08e-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: 72.02  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849    515 PAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLT-----------------SKYVGDGEKLVRALFAVARHMQPS 577
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileevldqllliivggKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571849    578 IIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGlpgnpdgdRIVVLAATNRPQELDEAALR-RFTKRVYVSLPD 652
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; ...
 476-640 2.15e-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: 2.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 476 GGAKVEWTDIAgqdvaKQALQEMVILPSVRPELftGLRApAKGLLLFGPPGNGKTLLARAVATECSATFLNI-SAASLTS 554
Cdd:cd19504   3 GGLDKEFSDIF-----RRAFASRVFPPEIVEQL--GCKH-VKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 555 KYVGDGEKLVRALFAVARHMQPS--------IIFIDEVDSLLSERSSSEHEAS--RRLKTEFLVEFDGLpgnPDGDRIVV 624
Cdd:cd19504  75 KYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGSTGvhDTVVNQLLSKIDGV---EQLNNILV 151

                       170
                ....*....|....*.
gi 28571849 625 LAATNRPQELDEAALR 640
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 ...
 517-646 2.28e-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: 68.32  E-value: 2.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 517 KGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDG--EKLVRALFAVARHMQPSIIFIDEVDSLLSERSSS 594
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 28571849 595 EHEAS--RRLKTEFLVEFDGLPGNpdgDRIVVLAATNRPQELDEAALRRFTKRV 646
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 ...
 484-607 1.22e-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: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 484 DIAGQDVAKQALQEmvilpsvRPELFT------GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYV 557
Cdd:cd19507   1 DVGGLDNLKDWLKK-------RKAAFSkqasayGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLV 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 28571849 558 GDGEKLVRALFAVARHMQPSIIFIDEVDSL-LSERSSSEHEASRRLKTEFL 607
Cdd:cd19507  73 GESESRLRQMIQTAEAIAPCVLWIDEIEKGfSNADSKGDSGTSSRVLGTFL 123
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 519-720 3.33e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 68.96  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  519 LLLFGPPGNGKTLLARAVATECSATFLNISAASltskyvgDGEKLVRALFAVARHM----QPSIIFIDEVdsllsersss 594
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEI---------- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  595 eHeasrRL-KT--EFLvefdgLPGNPDGDrIVVLAAT--NrPQ-ELDEAALRRftKRVYV--SLPDEQTRELLLNRLLQK 666
Cdd:PRK13342 102 -H----RFnKAqqDAL-----LPHVEDGT-ITLIGATteN-PSfEVNPALLSR--AQVFElkPLSEEDIEQLLKRALEDK 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571849  667 QGS--PLDTEALRRLAKITDGysgsD----LTALakDAALEPIRELNVEQVK-CLDISAMR 720
Cdd:PRK13342 168 ERGlvELDDEALDALARLANG----DarraLNLL--ELAALGVDSITLELLEeALQKRAAR 222
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 519-685 1.51e-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: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 519 LLLFGPPGNGKTLLARAVATECSATFLNISAasltskyVGDGEKLVRALFAVAR----HMQPSIIFIDEVdsllsersss 594
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARerraYGRRTILFVDEI---------- 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 595 eHeasrRL-KTE---FL--VEfdglpgnpdgDRIVVL-AAT--------NrpqeldeAALR-RftKRVYV--SLPDEQTR 656
Cdd:COG2256 115 -H----RFnKAQqdaLLphVE----------DGTITLiGATtenpsfevN-------SALLsR--CRVFVlkPLSEEDLE 170

                       170       180       190
                ....*....|....*....|....*....|....*
gi 28571849 657 ELL------LNRLLQKQGSPLDTEALRRLAKITDG 685
Cdd:COG2256 171 QLLeraladDERGLGGYKLELDDEALEALARLADG 205
ycf46 CHL00195
Ycf46; Provisional
 483-691 1.50e-10

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 64.27  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  483 TDIAGQDVAKQALQEmvilpsvRPELFT------GLRAPaKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKY 556
Cdd:CHL00195 228 SDIGGLDNLKDWLKK-------RSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  557 VGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHE--ASRRLKT--EFLVEfdglPGNPdgdrIVVLAATNRPQ 632
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSgtTNRVLATfiTWLSE----KKSP----VFVVATANNID 371

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571849  633 ELDEAALR--RFTKRVYVSLPDEQTRELL----LNRLLQKQGSPLDTEalrRLAKITDGYSGSDL 691
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 ...
 676-727 6.36e-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: 49.46  E-value: 6.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 28571849   676 LRRLAKITDGYSGSDLTALAKDAALEPIRELnveqvkcldisaMRAITEQDF 727
Cdd:pfam17862   4 LEELAERTEGFSGADLEALCREAALAALRRG------------LEAVTQEDL 43
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 517-641 1.99e-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: 1.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 517 KGLLLFGPPGNGKTLLARAVATECSatfLNISAASLTSkyVGDGEKLVRALFAVARhmQPSIIFIDEVDsllSERSSSEH 596
Cdd:cd19510  24 RGYLLYGPPGTGKSSFIAALAGELD---YDICDLNLSE--VVLTDDRLNHLLNTAP--KQSIILLEDID---AAFESREH 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 28571849 597 EASRRLKTEFL--VEFDGLPGNPDG-----DRIVVLaATNRPQELDEAALRR 641
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 ...
 485-600 3.01e-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: 3.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 485 IAGQDVAKQAL--------QEMVILPSVRPELFtglrapAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTS-K 555
Cdd:cd19498  13 IIGQDEAKRAVaialrnrwRRMQLPEELRDEVT------PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvG 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 28571849 556 YVG-DGEKLVRALFAvarhmqpSIIFIDEVDSLLSERSSSEHEASR 600
Cdd:cd19498  87 YVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGSSGPDVSR 125
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 485-585 5.55e-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: 5.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 485 IAGQDVAKQALQEMVILPSVRpeLFTGLRAPAKGL-------LLFGPPGNGKTLLARAVATECSATFLNISAASLT-SKY 556
Cdd:cd19497  14 VIGQERAKKVLSVAVYNHYKR--IRNNLKQKDDDVeleksniLLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGY 91

                        90       100       110
                ....*....|....*....|....*....|....*
gi 28571849 557 VGDG-----EKLVR-ALFAVARhMQPSIIFIDEVD 585
Cdd:cd19497  92 VGEDvenilLKLLQaADYDVER-AQRGIVYIDEID 125
PRK04195 PRK04195
replication factor C large subunit; Provisional
 480-714 9.12e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 48.76  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  480 VEWT---------DIAGQDVAKQALQEMVilpsvrpELFTGLRaPAKGLLLFGPPGNGKTLLARAVATEcsatF------ 544
Cdd:PRK04195   2 MPWVekyrpktlsDVVGNEKAKEQLREWI-------ESWLKGK-PKKALLLYGPPGVGKTSLAHALAND----Ygwevie 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  545 LNIS---AASLTSKYVGDGEKlVRALFAVARhmqpSIIFIDEVdsllserssseheasrrlkteflvefDGLPGNpdGDR 621
Cdd:PRK04195  70 LNASdqrTADVIERVAGEAAT-SGSLFGARR----KLILLDEV--------------------------DGIHGN--EDR 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  622 ---------I------VVLAATN----RPQELDEAAL----RRFTKRVYVSlpdeqtrelLLNRLLQKQGSPLDTEALRR 678
Cdd:PRK04195 117 ggarailelIkkakqpIILTANDpydpSLRELRNACLmiefKRLSTRSIVP---------VLKRICRKEGIECDDEALKE 187

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 28571849  679 LAKITDGysgsDLTALAKD--AALEPIRELNVEQVKCL 714
Cdd:PRK04195 188 IAERSGG----DLRSAINDlqAIAEGYGKLTLEDVKTL 221
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 518-642 9.83e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 45.75  E-value: 9.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   518 GLLLFGPPGNGKTLLAR--AVATECSATFL-----NISAASLTSKYVGDGEKLVRALFAVARHMQPS-IIFIDEVDSLLS 589
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28571849   590 ersssehEASRRLKT-----EFLVEFDGLPGNPDGDRIVVLAATNRP----QELDEAALRRF 642
Cdd:pfam07728  81 -------DVLNSLLSllderRLLLPDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
PRK13341 PRK13341
AAA family ATPase;
519-584 1.09e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 48.90  E-value: 1.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571849  519 LLLFGPPGNGKTLLARAVATECSATFLNISAasltskyVGDGEKLVRALFAVA-----RHMQPSIIFIDEV 584
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAkerleRHGKRTILFIDEV 118
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
487-585 1.24e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 48.23  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  487 GQDVAKQALqemvilpSV-------RpelftgLRAPAKGL----------LLFGPPGNGKTLLARAVatecsATFLNI-- 547
Cdd:PRK05342  75 GQERAKKVL-------SVavynhykR------LRHGDKKDddvelqksniLLIGPTGSGKTLLAQTL-----ARILDVpf 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 28571849  548 ---SAASLT-SKYVG-DGEK-LVRALFA----VARhMQPSIIFIDEVD 585
Cdd:PRK05342 137 aiaDATTLTeAGYVGeDVENiLLKLLQAadydVEK-AQRGIVYIDEID 183
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 519-681 1.58e-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: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 519 LLLFGPPGNGKTLLARAVATECSATFLNIS------AASLT--SKYVGDGEKLV---RALFAvarhmqpSIIFIDEVDSl 587
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQftpdllPSDILgtYIYDQQTGEFEfrpGPLFA-------NVLLADEINR- 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 588 lserssseheASRrlKT---------EFLVEFDG----LPgnpdgDRIVVLAATNRPQ-----ELDEAALRRFTKRVYVS 649
Cdd:COG0714 106 ----------APP--KTqsalleameERQVTIPGgtykLP-----EPFLVIATQNPIEqegtyPLPEAQLDRFLLKLYIG 168

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 28571849 650 LPDEQT-RELLLNRLLQKQGSP---LDTEALRRLAK 681
Cdd:COG0714 169 YPDAEEeREILRRHTGRHLAEVepvLSPEELLALQE 204
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 519-648 1.73e-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: 46.29  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 519 LLLFGPPGNGKTLLARAVATECS---------ATFLNISAASLTSKYVGDGEKLVRALFAVARHM---QPSIIF--IDEV 584
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlIDEV 134

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571849 585 DS--LLSERSSSEHEASR--RLKTEFLVEFDGLPGNPDgdrIVVLAATNRPQELDEAALRRFTKRVYV 648
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 ...
 513-646 1.15e-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: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 513 RAPAKGLLLFGPPGNGKTLLARAVATECSATFlnisaASLTSkyvGD----GEKLVRALFAVARHMQPS----IIFIDEV 584
Cdd:cd19512  19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDY-----AIMTG---GDvapmGREGVTAIHKVFDWANTSrrglLLFVDEA 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571849 585 DS-LLSERSSSEHEASRRLKTEFLVEfdglPGNPDGDRIVVLaATNRPQELDEAALRRFTKRV 646
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 ...
 722-754 2.53e-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: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 28571849   722 ITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYG 754
Cdd:pfam09336  29 VTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 520-585 2.99e-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: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   520 LLFGPPGNGKTLLARAVatecsATFLNISAASLTSK--------------------YVGDGEKLVraLFAVARHMQPSII 579
Cdd:pfam07724   7 LFLGPTGVGKTELAKAL-----AELLFGDERALIRIdmseymeehsvsrligappgYVGYEEGGQ--LTEAVRRKPYSIV 79


                  ....*.
gi 28571849   580 FIDEVD 585
Cdd:pfam07724  80 LIDEIE 85
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 519-650 3.28e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.95  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 519 LLLFGPPGNGKTLLARAVATE-CSATFLNISAASLtskyvgdgEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSsehE 597
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQaLLSDEPVIFISFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQG---D 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 28571849 598 ASRRLKTEFLVEFDGLPGNpdgdRIVVLAATNRPQELDEAALRRFTKRVYVSL 650
Cdd:cd01120  70 RSSELLEDLAKLLRAARNT----GITVIATIHSDKFDIDRGGSSNDERLLKSL 118
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 511-679 4.17e-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: 43.68  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   511 GLRAP--AKGLLLFGPPGNGKTLLARAVATE-CSATFL------NISAASLTSKYVGDGEKLVRALFAVARHmqpSIIFI 581
Cdd:TIGR03922 305 GLPVAqtSNHMLFAGPPGTGKTTIARVVAKIyCGLGVLrkplvrEVSRADLIGQYIGESEAKTNEIIDSALG---GVLFL 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   582 DEVdsllsersSSEHEASRRLKTEF-LVEFDGLPG--NPDGDRIVVLAATNRPQ-----ELDEAALRRFTKRV-YVSL-P 651
Cdd:TIGR03922 382 DEA--------YTLVETGYGQKDPFgLEAIDTLLArmENDRDRLVVIGAGYRKDldkflEVNEGLRSRFTRVIeFPSYsP 453

                         170       180
                  ....*....|....*....|....*...
gi 28571849   652 DEQTRelLLNRLLQKQGSPLDTEALRRL 679
Cdd:TIGR03922 454 DELVE--IARRMATERDSVLDDAAADAL 479
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
517-567 5.55e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.04  E-value: 5.55e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 28571849 517 KGLLLFGPPGNGKTLLARAVATECSA--TFLNISAASLTSKYVGDGEKLVRAL 567
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELGEdtPFVAISGSEIYSAELKKTEFLMQAL 117
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
456-682 6.26e-04

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 43.25  E-value: 6.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 456 VSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVR-----PELFTGLRAPAKGLLLFGPPGNGKT 530
Cdd:COG5635 115 KAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLeriesLKRLELLEAKKKRLLILGEPGSGKT 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 531 LLARAVATECSATFLN--------ISAASLT---------SKYVGDGEKLVRALFAVARHMQPSIIFID---EVdsllse 590
Cdd:COG5635 195 TLLRYLALELAERYLDaedpipilIELRDLAeeasledllAEALEKRGGEPEDALERLLRNGRLLLLLDgldEV------ 268

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 591 rsssEHEASRRLKTEFLVEF-DGLPGNpdgdRIVVlaaTNRPQELDEAALRRFTkRVYVS-LPDEQTRELLLN--RLLQK 666
Cdd:COG5635 269 ----PDEADRDEVLNQLRRFlERYPKA----RVII---TSRPEGYDSSELEGFE-VLELApLSDEQIEEFLKKwfEATER 336

                       250       260
                ....*....|....*....|.
gi 28571849 667 QGSPL-----DTEALRRLAKI 682
Cdd:COG5635 337 KAERLlealeENPELRELARN 357
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 485-585 7.89e-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: 7.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 485 IAGQDVAKQALQEMVILPSVrpelftGLRAPAKG---LLLFGPPGNGKTLLARAVA-----TECSATFLNISAAS----- 551
Cdd:cd19499  13 VVGQDEAVKAVSDAIRRARA------GLSDPNRPigsFLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEYMekhsv 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 28571849 552 -----LTSKYVGDGE--KLVRALfavaRHMQPSIIFIDEVD 585
Cdd:cd19499  87 srligAPPGYVGYTEggQLTEAV----RRKPYSVVLLDEIE 123
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 520-585 8.61e-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: 8.61e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28571849 520 LLFGPPGNGKTLLARAVatecsATFLN----IS-AASLT-SKYVG-DGE----KLVRAL-FAVARhMQPSIIFIDEVD 585
Cdd:COG1219 113 LLIGPTGSGKTLLAQTL-----ARILDvpfaIAdATTLTeAGYVGeDVEnillKLLQAAdYDVEK-AERGIIYIDEID 184
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 484-538 1.04e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.98  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 28571849   484 DIAGQDVAKQALqemvilpsvrpELftglrAPAKG--LLLFGPPGNGKTLLARAVAT 538
Cdd:pfam01078   4 DVKGQEQAKRAL-----------EI-----AAAGGhnLLMIGPPGSGKTMLAKRLPG 44
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 232-305 1.06e-03

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: 38.44  E-value: 1.06e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571849 232 HHRRAFEYISKALKIDEEneGHKELAIELYRKGIKELEDGIAVD-CWSGRGDVWDRAQRLHDKMQTNLSMARDRL 305
Cdd:cd02656   2 LLQQAKELIKQAVKEDED--GNYEEALELYKEALDYLLQALKAEkEPKLRKLLRKKVKEYLDRAEFLKELLKKQK 74
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
482-736 1.24e-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: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 482 WTDIAGQDVAKQALQEMVILPSVrpelftglrAPAkgLLLFGPPGNGKTLLARAVAT--------------ECSA----- 542
Cdd:COG2812   9 FDDVVGQEHVVRTLKNALASGRL---------AHA--YLFTGPRGVGKTTLARILAKalncengptgepcgECEScraia 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 543 --TFLNIS----AASLTSkyVGDGEKLVRALfavarHMQPS-----IIFIDEVdsllserssseHEASRR-----LKTef 606
Cdd:COG2812  78 agSHPDVIeidaEASNIG--VDDIRELIEKV-----SYAPVegrykVYIIDEA-----------HMLTTEafnalLKT-- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 607 LVEfdglpgnPDGDRIVVLAATN----------RPQELDeaaLRRftkrvyvsLPDEQTRElLLNRLLQKQGSPLDTEAL 676
Cdd:COG2812 138 LEE-------PPPHVVFILATTEpqkllptilsRCQRFD---FRR--------LPPEEIAE-HLAKIAEREGIEIEPEAL 198

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 677 RRLAKITDGySGSDLTALAKDAALEPIRELNvEQVkcldISAMRAITEQDFHSSLKRIRR 736
Cdd:COG2812 199 ALIARAADG-SMRDALSLLDQAIAFGLLDRR-ELL----LDLLEALLAGDVAALLALAEE 252
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
519-584 1.45e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 1.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571849  519 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKyvGDgeklvraLFAVARHMQP-SIIFIDEV 584
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GD-------LAAILTNLEEgDVLFIDEI 111
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 519-584 1.93e-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: 1.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28571849   519 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKyvGDgeklvraLFAVARHMQP-SIIFIDEV 584
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 ...
 512-585 2.11e-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: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 512 LRAPAKG--LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSK---------YVGD--GeKLVRALfAVARHMQPsI 578
Cdd:cd19500  31 LKGSMKGpiLCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmpG-RIIQAL-KKAGTNNP-V 107


                ....*..
gi 28571849 579 IFIDEVD 585
Cdd:cd19500 108 FLLDEID 114
PRK08116 PRK08116
hypothetical protein; Validated
 518-539 2.29e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.77  E-value: 2.29e-03
                         10        20
                 ....*....|....*....|..
gi 28571849  518 GLLLFGPPGNGKTLLARAVATE 539
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 519-584 2.40e-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: 2.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28571849   519 LLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKyvGDgekLVRALFAVARHmqpSIIFIDEV 584
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GD---LAAILTNLEEG---DVLFIDEI 90
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 484-538 2.67e-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: 41.18  E-value: 2.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28571849 484 DIAGQDVAKQALQemvIlpsvrpelftglrAPAKG--LLLFGPPGNGKTLLARAVAT 538
Cdd:COG0606 193 DVKGQEQAKRALE---I-------------AAAGGhnLLMIGPPGSGKTMLARRLPG 233
44 PHA02544
clamp loader, small subunit; Provisional
 499-743 3.65e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 40.36  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  499 VILPSVRPELFTGL----RAPAkgLLLFGP-PGNGKTLLARAVATECSATFLNISAASLTSKYVGDgeKLVRALFAVARH 573
Cdd:PHA02544  23 CILPAADKETFKSIvkkgRIPN--MLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFVRN--RLTRFASTVSLT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  574 MQPSIIFIDEVDsllserSSSEHEASRRLKTeFLVEFDGlpgnpdgdRIVVLAATNRPQELDEAALRRFTKrVYVSLPDE 653
Cdd:PHA02544  99 GGGKVIIIDEFD------RLGLADAQRHLRS-FMEAYSK--------NCSFIITANNKNGIIEPLRSRCRV-IDFGVPTK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849  654 QTRELL-------LNRLLQKQGSPLDTEAL-----------RRLAKITDGYSGS---DLTALA--KDAALEPIrelnVEQ 710
Cdd:PHA02544 163 EEQIEMmkqmivrCKGILEAEGVEVDMKVLaalvkknfpdfRRTINELQRYASTgkiDAGILSevTNSDIDDV----VEA 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 28571849  711 VKCLDISAMRAITEQ------DFHSSL-KRIRRSVAPQSL 743
Cdd:PHA02544 239 LKAKDFKAVRALAPNyandyaSFVGKLyDELYPQVTPPSI 278
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
505-583 5.17e-03

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


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 39.88  E-value: 5.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849 505 RPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSA--TFLNISAASLTSKYV---GDGEKLVRALFAVARHMQPSII 579
Cdd:COG3598   2 RRWLVPGLLPEGGVTLLAGPPGTGKSFLALQLAAAVAAggPWLGRRVPPGKVLYLaaeDDRGELRRRLKALGADLGLPFA 81


                ....
gi 28571849 580 FIDE 583
Cdd:COG3598  82 DLDG 85
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 487-567 6.26e-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: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571849   487 GQDVAKQALQemVILPSVRPELFTGlrapaKGLLLFGPPGNGKTLLARAVATECSAT--FLNISAASLTSKYVGDGEKLV 564
Cdd:pfam06068  28 GQEKAREAAG--VIVEMIKEGKIAG-----RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEALT 100


                  ...
gi 28571849   565 RAL 567
Cdd:pfam06068 101 QAF 103
 
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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