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Conserved domains on  [gi|685333866|ref|XP_009104519|]
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ATP-dependent zinc metalloprotease FTSH 12, chloroplastic [Brassica rapa]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 1000290)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB super family cl33892
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
358-963 1.37e-104

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


The actual alignment was detected with superfamily member COG0465:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 338.55  E-value: 1.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  358 PKLPYTYFLQKLDSSEVAAVVFTEDlkRLYVTMKEGFPLEYIVDIPLDPYLFETISNSGVEVDLLQKRQIHYFMKVFIAL 437
Cdd:COG0465    20 KEISYSEFLQLVEAGKVKSVTIQGD--RITGTLKDGTKTRFTTYRVNDPELVDLLEEKGVEVTAKPPEESSWLLSLLISL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  438 LPGILIL----WFIRESA-----MLLLITSK-RFLYKKYNQL-FDmayaenfilpvgDV---SETKSMYKEVVlggdvwD 503
Cdd:COG0465    98 LPILLLIglwiFFMRRMQgggggAMSFGKSKaKLYDEDKPKVtFD------------DVagvDEAKEELQEIV------D 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  504 LLDelmiymgNPMQYYE---KdVPfvRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFtdSEK---SGAAKINEMF 577
Cdd:COG0465   160 FLK-------DPEKFTRlgaK-IP--KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF--VEMfvgVGASRVRDLF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  578 SVARRNAPAFVFVDEIDAIaGRHarkdpR----------RRATFEALIAQLDGekektgidrFSLRQAVIFICATNRPDE 647
Cdd:COG0465   228 EQAKKNAPCIIFIDEIDAV-GRQ-----RgaglggghdeREQTLNQLLVEMDG---------FEGNEGVIVIAATNRPDV 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  648 LDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQ 727
Cdd:COG0465   293 LDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTM 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  728 QDIVDVLDKQL--LEGMGVLLTEEEqqkceqsvsyekKRLLAVHEAGHIVLAHLFPRFD-WHAFSqLLPGGKETAVSVFY 804
Cdd:COG0465   373 EDFEEAIDRVIagPERKSRVISEKE------------KKITAYHEAGHALVAALLPGADpVHKVT-IIPRGRALGYTMQL 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  805 PREdmvDQGYTTFGYMKMQMVVAHGGRCAERVVFGdDVSDGGKDDLEKITKIAREMVispqnTKLGLTqlvKKIGMVDLP 884
Cdd:COG0465   440 PEE---DRYLYTKEELLDRIAVLLGGRAAEELVFG-EVTTGASNDLERATKIARAMV-----TEYGMS---EKLGPVAYG 507
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  885 DNPDGELIKYRWDHPHvmpaDMSIEVSELFTRELTRYIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEIMK 963
Cdd:COG0465   508 ESEGEVFLGRDIGQSR----NYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
358-963 1.37e-104

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 338.55  E-value: 1.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  358 PKLPYTYFLQKLDSSEVAAVVFTEDlkRLYVTMKEGFPLEYIVDIPLDPYLFETISNSGVEVDLLQKRQIHYFMKVFIAL 437
Cdd:COG0465    20 KEISYSEFLQLVEAGKVKSVTIQGD--RITGTLKDGTKTRFTTYRVNDPELVDLLEEKGVEVTAKPPEESSWLLSLLISL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  438 LPGILIL----WFIRESA-----MLLLITSK-RFLYKKYNQL-FDmayaenfilpvgDV---SETKSMYKEVVlggdvwD 503
Cdd:COG0465    98 LPILLLIglwiFFMRRMQgggggAMSFGKSKaKLYDEDKPKVtFD------------DVagvDEAKEELQEIV------D 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  504 LLDelmiymgNPMQYYE---KdVPfvRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFtdSEK---SGAAKINEMF 577
Cdd:COG0465   160 FLK-------DPEKFTRlgaK-IP--KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF--VEMfvgVGASRVRDLF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  578 SVARRNAPAFVFVDEIDAIaGRHarkdpR----------RRATFEALIAQLDGekektgidrFSLRQAVIFICATNRPDE 647
Cdd:COG0465   228 EQAKKNAPCIIFIDEIDAV-GRQ-----RgaglggghdeREQTLNQLLVEMDG---------FEGNEGVIVIAATNRPDV 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  648 LDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQ 727
Cdd:COG0465   293 LDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTM 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  728 QDIVDVLDKQL--LEGMGVLLTEEEqqkceqsvsyekKRLLAVHEAGHIVLAHLFPRFD-WHAFSqLLPGGKETAVSVFY 804
Cdd:COG0465   373 EDFEEAIDRVIagPERKSRVISEKE------------KKITAYHEAGHALVAALLPGADpVHKVT-IIPRGRALGYTMQL 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  805 PREdmvDQGYTTFGYMKMQMVVAHGGRCAERVVFGdDVSDGGKDDLEKITKIAREMVispqnTKLGLTqlvKKIGMVDLP 884
Cdd:COG0465   440 PEE---DRYLYTKEELLDRIAVLLGGRAAEELVFG-EVTTGASNDLERATKIARAMV-----TEYGMS---EKLGPVAYG 507
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  885 DNPDGELIKYRWDHPHvmpaDMSIEVSELFTRELTRYIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEIMK 963
Cdd:COG0465   508 ESEGEVFLGRDIGQSR----NYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
ftsH CHL00176
cell division protein; Validated
527-968 4.56e-76

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 262.68  E-value: 4.56e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKS-GAAKINEMFSVARRNAPAFVFVDEIDAI-----AGRH 600
Cdd:CHL00176  217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGvGAARVRDLFKKAKENSPCIVFIDEIDAVgrqrgAGIG 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  601 ARKDPRRRaTFEALIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHS 680
Cdd:CHL00176  297 GGNDEREQ-TLNQLLTEMDGFKGNKG---------VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  681 AGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIVDVLDKQLLEGMGVLLTEEEQqkceqsvsy 760
Cdd:CHL00176  367 RNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKN--------- 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  761 ekKRLLAVHEAGHIVLAHLFPRFDWHAFSQLLPGGKETAVSVFYPREdmvDQGYTTFGYMKMQMVVAHGGRCAERVVFGD 840
Cdd:CHL00176  438 --KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEE---DQSLVSRSQILARIVGALGGRAAEEVVFGS 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  841 -DVSDGGKDDLEKITKIAREMVispqnTKLGLTqlvkKIGMVDLPDNPDGEL-----IKYRWDHPHVMPADMSIEVSELf 914
Cdd:CHL00176  513 tEVTTGASNDLQQVTNLARQMV-----TRFGMS----SIGPISLESNNSTDPflgrfMQRNSEYSEEIADKIDMEVRSI- 582
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 685333866  915 treltryIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEIMKSLSPL 968
Cdd:CHL00176  583 -------LHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTIL 629
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
527-761 4.99e-40

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: 159.30  E-value: 4.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKSgaakINEMFSVARRNAPAFVFVDEIDAIAgrha 601
Cdd:TIGR01243  488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILskwvgESEKA----IREIFRKARQAAPAIIFFDEIDAIA---- 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   602 rkdPRRRATFEA---------LIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQR 672
Cdd:TIGR01243  560 ---PARGARFDTsvtdrivnqLLTEMDGIQELSN---------VVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEAR 627
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   673 VQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIvDVLDKQLLEGMGVLLT--EEE 750
Cdd:TIGR01243  628 KEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL-EVGEEEFLKDLKVEMRhfLEA 706
                          250
                   ....*....|.
gi 685333866   751 QQKCEQSVSYE 761
Cdd:TIGR01243  707 LKKVKPSVSKE 717
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
505-664 1.89e-37

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: 138.13  E-value: 1.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  505 LDELMIYMGNPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKS-GAAKINEMFSVARRN 583
Cdd:cd19501    16 LKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGvGASRVRDLFEQAKKN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  584 APAFVFVDEIDAIAGRHARK----DPRRRATFEALIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRID 659
Cdd:cd19501    96 APCIVFIDEIDAVGRKRGAGlgggHDEREQTLNQLLVEMDGFESNTG---------VIVIAATNRPDVLDPALLRPGRFD 166

                  ....*
gi 685333866  660 RRLYI 664
Cdd:cd19501   167 RQVYV 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
529-666 1.09e-35

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: 131.56  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDS-EKSGAAKINEMFSVARRNAPAFVFVDEIDAIAG-RHARKDPR 606
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKyVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGsRGSGGDSE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   607 RRATFEALIAQLDGEKEKTGidrfslrqAVIFICATNRPDELDLEFVrsGRIDRRLYIGL 666
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSNS--------KVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
527-668 4.75e-13

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: 67.78  E-value: 4.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866    527 RGVLLSGPPGTGKTLFARTLAKE---SGLPFVFASGAEFTD---------------SEKSGAAKINEMFSVARRNAPAFV 588
Cdd:smart00382    3 EVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEevldqllliivggkkASGSGELRLRLALALARKLKPDVL 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866    589 FVDEIDAIAGRHARKDPRRRATFEALIaqldgekektgidRFSLRQAVIFICATNRPDELDLEFVRSgRIDRRLYIGLPD 668
Cdd:smart00382   83 ILDEITSLLDAEQEALLLLLEELRLLL-------------LLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
358-963 1.37e-104

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 338.55  E-value: 1.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  358 PKLPYTYFLQKLDSSEVAAVVFTEDlkRLYVTMKEGFPLEYIVDIPLDPYLFETISNSGVEVDLLQKRQIHYFMKVFIAL 437
Cdd:COG0465    20 KEISYSEFLQLVEAGKVKSVTIQGD--RITGTLKDGTKTRFTTYRVNDPELVDLLEEKGVEVTAKPPEESSWLLSLLISL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  438 LPGILIL----WFIRESA-----MLLLITSK-RFLYKKYNQL-FDmayaenfilpvgDV---SETKSMYKEVVlggdvwD 503
Cdd:COG0465    98 LPILLLIglwiFFMRRMQgggggAMSFGKSKaKLYDEDKPKVtFD------------DVagvDEAKEELQEIV------D 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  504 LLDelmiymgNPMQYYE---KdVPfvRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFtdSEK---SGAAKINEMF 577
Cdd:COG0465   160 FLK-------DPEKFTRlgaK-IP--KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF--VEMfvgVGASRVRDLF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  578 SVARRNAPAFVFVDEIDAIaGRHarkdpR----------RRATFEALIAQLDGekektgidrFSLRQAVIFICATNRPDE 647
Cdd:COG0465   228 EQAKKNAPCIIFIDEIDAV-GRQ-----RgaglggghdeREQTLNQLLVEMDG---------FEGNEGVIVIAATNRPDV 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  648 LDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQ 727
Cdd:COG0465   293 LDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTM 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  728 QDIVDVLDKQL--LEGMGVLLTEEEqqkceqsvsyekKRLLAVHEAGHIVLAHLFPRFD-WHAFSqLLPGGKETAVSVFY 804
Cdd:COG0465   373 EDFEEAIDRVIagPERKSRVISEKE------------KKITAYHEAGHALVAALLPGADpVHKVT-IIPRGRALGYTMQL 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  805 PREdmvDQGYTTFGYMKMQMVVAHGGRCAERVVFGdDVSDGGKDDLEKITKIAREMVispqnTKLGLTqlvKKIGMVDLP 884
Cdd:COG0465   440 PEE---DRYLYTKEELLDRIAVLLGGRAAEELVFG-EVTTGASNDLERATKIARAMV-----TEYGMS---EKLGPVAYG 507
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  885 DNPDGELIKYRWDHPHvmpaDMSIEVSELFTRELTRYIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEIMK 963
Cdd:COG0465   508 ESEGEVFLGRDIGQSR----NYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILA 582
ftsH CHL00176
cell division protein; Validated
527-968 4.56e-76

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 262.68  E-value: 4.56e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKS-GAAKINEMFSVARRNAPAFVFVDEIDAI-----AGRH 600
Cdd:CHL00176  217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGvGAARVRDLFKKAKENSPCIVFIDEIDAVgrqrgAGIG 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  601 ARKDPRRRaTFEALIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHS 680
Cdd:CHL00176  297 GGNDEREQ-TLNQLLTEMDGFKGNKG---------VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  681 AGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIVDVLDKQLLEGMGVLLTEEEQqkceqsvsy 760
Cdd:CHL00176  367 RNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKN--------- 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  761 ekKRLLAVHEAGHIVLAHLFPRFDWHAFSQLLPGGKETAVSVFYPREdmvDQGYTTFGYMKMQMVVAHGGRCAERVVFGD 840
Cdd:CHL00176  438 --KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEE---DQSLVSRSQILARIVGALGGRAAEEVVFGS 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  841 -DVSDGGKDDLEKITKIAREMVispqnTKLGLTqlvkKIGMVDLPDNPDGEL-----IKYRWDHPHVMPADMSIEVSELf 914
Cdd:CHL00176  513 tEVTTGASNDLQQVTNLARQMV-----TRFGMS----SIGPISLESNNSTDPflgrfMQRNSEYSEEIADKIDMEVRSI- 582
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 685333866  915 treltryIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEIMKSLSPL 968
Cdd:CHL00176  583 -------LHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTIL 629
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
359-962 1.48e-67

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 239.17  E-value: 1.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  359 KLPYTYFLQKLDSSEVAAVVFTEdlKRLYVTMKEGFplEYIVDIPL-DPYLFETISNSGVEVDLLQKRQIHYFMKVFIAL 437
Cdd:PRK10733   31 KVDYSTFLQEVNQDQVREARING--REINVTKKDSN--RYTTYIPVnDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISW 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  438 LPGILIL----WFIRE-------SAMLLLITSKRFLYKkynqlfdmayaenfilpvgdvSETKSMYKEVVLGGDVWDLLD 506
Cdd:PRK10733  107 FPMLLLIgvwiFFMRQmqggggkGAMSFGKSKARMLTE---------------------DQIKTTFADVAGCDEAKEEVA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  507 ELMIYMGNPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDS-EKSGAAKINEMFSVARRNAP 585
Cdd:PRK10733  166 ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMfVGVGASRVRDMFEQAKKAAP 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  586 AFVFVDEIDAI-----AGRHARKDPRRRaTFEALIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDR 660
Cdd:PRK10733  246 CIIFIDEIDAVgrqrgAGLGGGHDEREQ-TLNQMLVEMDG---------FEGNEGIIVIAATNRPDVLDPALLRPGRFDR 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  661 RLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIVDVLDKQLL- 739
Cdd:PRK10733  316 QVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMg 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  740 -EGMGVLLTEEEQqkceQSVSYekkrllavHEAGHIVLAHLFPRFDWHAFSQLLPGGKETAVSVFYPREDMVDQGYTTfg 818
Cdd:PRK10733  396 aERRSMVMTEAQK----ESTAY--------HEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQK-- 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  819 yMKMQMVVAHGGRCAERVVFG-DDVSDGGKDDLEKITKIAREMVispqnTKLGLTQlvkKIGMVdLPDNPDGELIKYRwd 897
Cdd:PRK10733  462 -LESQISTLYGGRLAEEIIYGpEHVSTGASNDIKVATNLARNMV-----TQWGFSE---KLGPL-LYAEEEGEVFLGR-- 529
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685333866  898 hpHVMPAD-MSIEVSELFTRELTRYIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEIM 962
Cdd:PRK10733  530 --SVAKAKhMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLM 593
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
514-736 6.19e-60

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 208.32  E-value: 6.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  514 NPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDS---EksGAAKINEMFSVARRNAPAFVFV 590
Cdd:COG1222   100 NPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyigE--GARNVREVFELAREKAPSIIFI 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  591 DEIDAIAGRhaRKDPRR----RATFEALIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGL 666
Cdd:COG1222   178 DEIDAIAAR--RTDDGTsgevQRTVNQLLAELDG---------FESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPL 246
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  667 PDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIVDVLDK 736
Cdd:COG1222   247 PDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEK 316
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
491-736 1.05e-54

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: 195.51  E-value: 1.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  491 MYKEVVLGGDVWDLLDELMIYMG-NPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTD----- 564
Cdd:COG0464   155 ILDDLGGLEEVKEELRELVALPLkRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSkyvge 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  565 SEKsgaaKINEMFSVARRNAPAFVFVDEIDAIAG-RHARKDPRRRATFEALIAQLDGekektgidrfsLRQAVIFICATN 643
Cdd:COG0464   235 TEK----NLREVFDKARGLAPCVLFIDEADALAGkRGEVGDGVGRRVVNTLLTEMEE-----------LRSDVVVIAATN 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  644 RPDELDLEFVRsgRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRS 723
Cdd:COG0464   300 RPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377
                         250
                  ....*....|...
gi 685333866  724 SIYQQDIVDVLDK 736
Cdd:COG0464   378 PVTTEDLLEALER 390
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
527-760 4.45e-47

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 173.48  E-value: 4.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTdsEK---SGAAKINEMFSVARRNAPAFVFVDEIDAIAGRhaRK 603
Cdd:PRK03992  166 KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV--QKfigEGARLVRELFELAREKAPSIIFIDEIDAIAAK--RT 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  604 DP--------RRraTFEALIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQI 675
Cdd:PRK03992  242 DSgtsgdrevQR--TLMQLLAEMDG---------FDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEI 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  676 FGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIVDVLDKqllegmgVLLTEEEQQKCE 755
Cdd:PRK03992  311 LKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEK-------VMGKEEKDSMEE 383

                  ....*
gi 685333866  756 QSVSY 760
Cdd:PRK03992  384 PGVMF 388
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
527-761 4.99e-40

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: 159.30  E-value: 4.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKSgaakINEMFSVARRNAPAFVFVDEIDAIAgrha 601
Cdd:TIGR01243  488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILskwvgESEKA----IREIFRKARQAAPAIIFFDEIDAIA---- 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   602 rkdPRRRATFEA---------LIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQR 672
Cdd:TIGR01243  560 ---PARGARFDTsvtdrivnqLLTEMDGIQELSN---------VVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEAR 627
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   673 VQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIvDVLDKQLLEGMGVLLT--EEE 750
Cdd:TIGR01243  628 KEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL-EVGEEEFLKDLKVEMRhfLEA 706
                          250
                   ....*....|.
gi 685333866   751 QQKCEQSVSYE 761
Cdd:TIGR01243  707 LKKVKPSVSKE 717
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
505-664 1.89e-37

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: 138.13  E-value: 1.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  505 LDELMIYMGNPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKS-GAAKINEMFSVARRN 583
Cdd:cd19501    16 LKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGvGASRVRDLFEQAKKN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  584 APAFVFVDEIDAIAGRHARK----DPRRRATFEALIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRID 659
Cdd:cd19501    96 APCIVFIDEIDAVGRKRGAGlgggHDEREQTLNQLLVEMDGFESNTG---------VIVIAATNRPDVLDPALLRPGRFD 166

                  ....*
gi 685333866  660 RRLYI 664
Cdd:cd19501   167 RQVYV 171
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
504-664 2.18e-37

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: 137.80  E-value: 2.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  504 LLDELMIYMGNPMQYYEKDV---PFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSE-KSGAAKINEMFSV 579
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRyglGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYvGESEKNLRKIFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  580 ARRNAPAFVFVDEIDAIAGRHAR--KDPRRRATFEALIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGR 657
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSsgESGELRRVLNQLLTELDGVNSRSK---------VLVIAATNRPDLLDPALLRPGR 151

                  ....*..
gi 685333866  658 IDRRLYI 664
Cdd:cd19481   152 FDEVIEF 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
527-730 2.85e-37

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 144.91  E-value: 2.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSE-KSGAAKINEMFSVARRNAPAFVFVDEIDAIAGRhaRKDP 605
Cdd:PTZ00454  180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYlGEGPRMVRDVFRLARENAPSIIFIDEVDSIATK--RFDA 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  606 RRRATFEA------LIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVH 679
Cdd:PTZ00454  258 QTGADREVqrilleLLNQMDG---------FDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTI 328
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 685333866  680 SAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDI 730
Cdd:PTZ00454  329 TSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDF 379
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
527-738 1.00e-36

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 144.53  E-value: 1.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAK-INEMFSVARRNAPAFVFVDEIDAIAGRH----- 600
Cdd:PTZ00361  218 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKlVRELFRVAEENAPSIVFIDEIDAIGTKRydats 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  601 -ARKDPRRraTFEALIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVH 679
Cdd:PTZ00361  298 gGEKEIQR--TMLELLNQLDG---------FDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIH 366
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  680 SAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDIVDVLDKQL 738
Cdd:PTZ00361  367 TSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVL 425
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
529-666 1.09e-35

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: 131.56  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDS-EKSGAAKINEMFSVARRNAPAFVFVDEIDAIAG-RHARKDPR 606
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKyVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGsRGSGGDSE 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   607 RRATFEALIAQLDGEKEKTGidrfslrqAVIFICATNRPDELDLEFVrsGRIDRRLYIGL 666
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSNS--------KVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
493-736 2.66e-35

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 134.63  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  493 KEVVLGGDVWDLLDELMIYMGNPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDS---EksG 569
Cdd:COG1223     2 DDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSylgE--T 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  570 AAKINEMFSVARRnAPAFVFVDEIDAIAGR----HARKDPRRraTFEALIAQLDGEKEKtgidrfslrqaVIFICATNRP 645
Cdd:COG1223    80 ARNLRKLFDFARR-APCVIFFDEFDAIAKDrgdqNDVGEVKR--VVNALLQELDGLPSG-----------SVVIAATNHP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  646 DELDlEFVRSgRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSI 725
Cdd:COG1223   146 ELLD-SALWR-RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKV 223
                         250
                  ....*....|.
gi 685333866  726 YQQDIVDVLDK 736
Cdd:COG1223   224 TKEDLEEALKQ 234
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
527-720 8.67e-34

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: 139.66  E-value: 8.67e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAE-----FTDSEKsgaaKINEMFSVARRNAPAFVFVDEIDAIAGRha 601
Cdd:TIGR01243  213 KGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEimskyYGESEE----RLREIFKEAEENAPSIIFIDEIDAIAPK-- 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   602 rkdpRRRATFEA---LIAQL----DGEKEktgidrfslRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQ 674
Cdd:TIGR01243  287 ----REEVTGEVekrVVAQLltlmDGLKG---------RGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKE 353
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 685333866   675 IFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRK 720
Cdd:TIGR01243  354 ILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
497-660 5.42e-31

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: 119.82  E-value: 5.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  497 LGG--DVWDLLDELMIYMGNPMQYYEK---DVPfvRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTdSEKSGA- 570
Cdd:cd19518     2 IGGmdSTLKELCELLIHPILPPEYFQHlgvEPP--RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGEs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  571 -AKINEMFSVARRNAPAFVFVDEIDAIAGRH--ARKDPRRRatfeaLIAQLdgekeKTGIDRFSLR----QAVIFICATN 643
Cdd:cd19518    79 eEKIRELFDQAISNAPCIVFIDEIDAITPKResAQREMERR-----IVSQL-----LTCMDELNNEktagGPVLVIGATN 148
                         170
                  ....*....|....*..
gi 685333866  644 RPDELDLEFVRSGRIDR 660
Cdd:cd19518   149 RPDSLDPALRRAGRFDR 165
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
497-664 9.06e-31

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: 118.93  E-value: 9.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  497 LGG--DVWDLLDELMIY-MGNPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKs 568
Cdd:cd19503     2 IGGldEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVskylgESEK- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  569 gaaKINEMFSVARRNAPAFVFVDEIDAIAGR--HARKDPRRRatfeaLIAQLdgekeKTGIDRFSLRQAVIFICATNRPD 646
Cdd:cd19503    81 ---NLREIFEEARSHAPSIIFIDEIDALAPKreEDQREVERR-----VVAQL-----LTLMDGMSSRGKVVVIAATNRPD 147
                         170
                  ....*....|....*...
gi 685333866  647 ELDLEFVRSGRIDRRLYI 664
Cdd:cd19503   148 AIDPALRRPGRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
527-664 9.55e-31

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: 118.54  E-value: 9.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAE-----FTDSEKSgaakINEMFSVARRNAPAFVFVDEIDAIAGRha 601
Cdd:cd19511    28 KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPElfskyVGESERA----VREIFQKARQAAPCIIFFDEIDSLAPR-- 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685333866  602 RKDPRRRATFEALIAQLDGEkektgIDRFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYI 664
Cdd:cd19511   102 RGQSDSSGVTDRVVSQLLTE-----LDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
527-662 2.07e-28

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: 112.43  E-value: 2.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSE-KSGAAKINEMFSVARRNAPAFVFVDEIDAIAGRHARK-- 603
Cdd:cd19502    38 KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYiGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSgt 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685333866  604 --DPRRRATFEALIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDRRL 662
Cdd:cd19502   118 ggDREVQRTMLELLNQLDG---------FDPRGNIKVIMATNRPDILDPALLRPGRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
527-664 2.01e-27

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: 109.12  E-value: 2.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKSgaakINEMFSVARRNAPAFVFVDEIDAIAgrha 601
Cdd:cd19529    28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLskwvgESEKA----IREIFRKARQVAPCVIFFDEIDSIA---- 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685333866  602 rkdPRRRATFEA---------LIAQLDGEKEKtgidrfslrQAVIFICATNRPDELDLEFVRSGRIDRRLYI 664
Cdd:cd19529   100 ---PRRGTTGDSgvtervvnqLLTELDGLEEM---------NGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
Peptidase_M41 pfam01434
Peptidase family M41;
758-961 1.81e-25

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 104.61  E-value: 1.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   758 VSYEKKRLLAVHEAGHIVLAHLFPRFDWHAFSQLLPGGKETAVSVFYPREDmvdQGYTTFGYMKMQMVVAHGGRCAERVV 837
Cdd:pfam01434    3 ISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEED---KLLYTKEQLLARIAVLLGGRAAEELI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   838 FGDdVSDGGKDDLEKITKIAREMVispqnTKLGLTqlvKKIGMVDLPDNPDGELIKYRWDHphvmPADMSIEVSELFTRE 917
Cdd:pfam01434   80 FGE-VTTGASNDLEKATKIARQMV-----TEFGMS---DKLGPVSLEESDGNVFLGRGMGK----RKPYSEETADIIDEE 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 685333866   918 LTRYIEETEELAMNALRANRHILDLITGELLERSRITGLEVEEI 961
Cdd:pfam01434  147 VKRLLEEAYERAKEILTEHRDELEALAEALLEKETLDAEEIREL 190
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
527-665 4.72e-25

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: 102.51  E-value: 4.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTdSEKSGAA--KINEMFSVARRNAPAFVFVDEIDAIAGRharkd 604
Cdd:cd19519    35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESesNLRKAFEEAEKNAPAIIFIDEIDAIAPK----- 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685333866  605 pRRRATFEA---LIAQLdgekeKTGIDRFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIG 665
Cdd:cd19519   109 -REKTHGEVerrIVSQL-----LTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREIDIG 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
505-664 8.53e-25

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: 101.82  E-value: 8.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  505 LDELMIYmgnPMQYYEKDVPF----VRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAE-----FTDSEksgaAKINE 575
Cdd:cd19528     5 LQELVQY---PVEHPDKFLKFgmtpSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPElltmwFGESE----ANVRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  576 MFSVARRNAPAFVFVDEIDAIA-GRHARKDPRRRATfEALIAQLDGEkektgIDRFSLRQAVIFICATNRPDELDLEFVR 654
Cdd:cd19528    78 IFDKARAAAPCVLFFDELDSIAkARGGNIGDAGGAA-DRVINQILTE-----MDGMNTKKNVFIIGATNRPDIIDPAILR 151
                         170
                  ....*....|
gi 685333866  655 SGRIDRRLYI 664
Cdd:cd19528   152 PGRLDQLIYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
514-664 5.16e-23

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: 96.40  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  514 NPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKSgaakINEMFSVARRNAPAFV 588
Cdd:cd19530    18 RPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLnkyvgESERA----VRQVFQRARASAPCVI 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685333866  589 FVDEIDAIAGRhaRKDPRRRATfEALIAQLdgekeKTGIDRFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYI 664
Cdd:cd19530    94 FFDEVDALVPK--RGDGGSWAS-ERVVNQL-----LTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
500-664 5.66e-23

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: 96.65  E-value: 5.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  500 DVWDLLDELMIYmgnPM---QYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAKI-NE 575
Cdd:cd19509     6 DAKEALKEAVIL---PSlrpDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIvRA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  576 MFSVARRNAPAFVFVDEIDAIAGRHARKD--PRRRATFEALIaQLDGEKEKTGidrfslrQAVIFICATNRPDELDLEFV 653
Cdd:cd19509    83 LFALARELQPSIIFIDEIDSLLSERGSGEheASRRVKTEFLV-QMDGVLNKPE-------DRVLVLGATNRPWELDEAFL 154
                         170
                  ....*....|.
gi 685333866  654 RsgRIDRRLYI 664
Cdd:cd19509   155 R--RFEKRIYI 163
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
527-664 9.19e-21

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: 90.18  E-value: 9.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTD-----SEKSGAAkineMFSVARRNAPAFVFVDEIDAIAGRHA 601
Cdd:cd19520    36 KGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDkwygeSQKLVAA----VFSLASKLQPSIIFIDEIDSFLRQRS 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685333866  602 RKDPRRRATFEALIAQL-DGEKEKTgidrfslRQAVIFICATNRPDELDLEFVRsgRIDRRLYI 664
Cdd:cd19520   112 STDHEATAMMKAEFMSLwDGLSTDG-------NCRVIVMGATNRPQDLDEAILR--RMPKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
482-664 6.55e-20

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: 88.12  E-value: 6.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  482 VGDVSETKSMYKEVVLggdvwdlldeLMIYMGNPMQYYEKdvPFvRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAE 561
Cdd:cd19522     2 IADLEEAKKLLEEAVV----------LPMWMPEFFKGIRR--PW-KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSST 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  562 FTDSEKSGAAK-INEMFSVARRNAPAFVFVDEIDAIAGRHARKDPR---RRATFEALIaQLDGEKEKTGIDrfSLRQAVI 637
Cdd:cd19522    69 LTSKYRGESEKlVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHeasRRVKSELLV-QMDGVGGASEND--DPSKMVM 145
                         170       180
                  ....*....|....*....|....*..
gi 685333866  638 FICATNRPDELDLEFVRsgRIDRRLYI 664
Cdd:cd19522   146 VLAATNFPWDIDEALRR--RLEKRIYI 170
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
528-664 2.02e-19

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: 86.41  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  528 GVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKSgaakINEMFSVARRNAPAFVFVDEIDAIA---GR 599
Cdd:cd19527    28 GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELInmyigESEAN----VREVFQKARDAKPCVIFFDELDSLApsrGN 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685333866  600 HARKDPRRRATFEALIAQLDGEKektgidrfSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYI 664
Cdd:cd19527   104 SGDSGGVMDRVVSQLLAELDGMS--------SSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
527-663 2.48e-19

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: 86.41  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLA-----KESGLPFVFASGAEFTdSEKSGAA--KINEMFSVARRNAPAFVFVDEIDAIAG- 598
Cdd:cd19517    35 RGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCL-SKWVGEAerQLRLLFEEAYRMQPSIIFFDEIDGLAPv 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685333866  599 RHARKDPRRRATFEALIAQLDGekektgidrFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLY 663
Cdd:cd19517   114 RSSKQEQIHASIVSTLLALMDG---------LDNRGQVVVIGATNRPDALDPALRRPGRFDREFY 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
523-663 3.43e-19

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: 85.56  E-value: 3.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  523 VPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTD-----SEKSgaakINEMFSVARRNAPAFVFVDEIDAIA 597
Cdd:cd19526    24 LRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyigaSEQN----VRDLFSRAQSAKPCILFFDEFDSIA 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685333866  598 grharkdPRR--------RATFEALIAQLDGEKEKTGidrfslrqaVIFICATNRPDELDLEFVRSGRIDRRLY 663
Cdd:cd19526   100 -------PKRghdstgvtDRVVNQLLTQLDGVEGLDG---------VYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
527-664 3.55e-19

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: 86.58  E-value: 3.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDS-EKSGAAKINEMFSVARRNAPAFVFVDEIDAIAGRH--ARK 603
Cdd:cd19525    56 KGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKwVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRgeGEH 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685333866  604 DPRRRATFEALIaQLDGEKEktgidrfSLRQAVIFICATNRPDELDlEFVRSgRIDRRLYI 664
Cdd:cd19525   136 ESSRRIKTEFLV-QLDGATT-------SSEDRILVVGATNRPQEID-EAARR-RLVKRLYI 186
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
527-666 3.57e-18

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: 82.19  E-value: 3.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKES---GLPFVFASGAEFT----DSEKSGAAKINEMFSVARRNAPAFVFVDEIDAIagr 599
Cdd:cd00009    20 KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLeglvVAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL--- 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685333866  600 harkdprRRATFEALIAQLDgekekTGIDRFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGL 666
Cdd:cd00009    97 -------SRGAQNALLRVLE-----TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
527-664 1.82e-17

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: 80.66  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAK-INEMFSVARRNAPAFVFVDEIDAIAG--RHARK 603
Cdd:cd19524    34 RGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKlVRALFAVARELQPSIIFIDEVDSLLSerSEGEH 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685333866  604 DPRRRATFEALIaQLDGeKEKTGIDRfslrqaVIFICATNRPDELDLEFVRsgRIDRRLYI 664
Cdd:cd19524   114 EASRRLKTEFLI-EFDG-VQSNGDDR------VLVMGATNRPQELDDAVLR--RFTKRVYV 164
ycf46 CHL00195
Ycf46; Provisional
524-713 6.48e-17

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 85.07  E-value: 6.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  524 PFVRGVLLSGPPGTGKTLFARTLAKESGLPF-------VFAS--GaeftDSEksgaAKINEMFSVARRNAPAFVFVDEID 594
Cdd:CHL00195  257 PTPRGLLLVGIQGTGKSLTAKAIANDWQLPLlrldvgkLFGGivG----ESE----SRMRQMIRIAEALSPCILWIDEID 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  595 -AIAGRHARKDP----RRRATFealiaqldgekektgIDRFSLRQAVIFICAT-NRPDELDLEFVRSGRIDRRLYIGLPD 668
Cdd:CHL00195  329 kAFSNSESKGDSgttnRVLATF---------------ITWLSEKKSPVFVVATaNNIDLLPLEILRKGRFDEIFFLDLPS 393
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 685333866  669 AKQRVQIFGVHSAG--KNLAEDIDFGKLVFRTVGFSGADIRNLVNEA 713
Cdd:CHL00195  394 LEEREKIFKIHLQKfrPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEA 440
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
527-664 3.66e-16

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: 77.21  E-value: 3.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-----DSEKsgaaKINEMFSVARRNAPAFVFVDEIDAIAGRHA 601
Cdd:cd19521    41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVskwmgESEK----LVKQLFAMARENKPSIIFIDEVDSLCGTRG 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685333866  602 --RKDPRRRATFEALIaQLDGekekTGIDrfslRQAVIFICATNRPDELDLEFVRsgRIDRRLYI 664
Cdd:cd19521   117 egESEASRRIKTELLV-QMNG----VGND----SQGVLVLGATNIPWQLDSAIRR--RFEKRIYI 170
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
527-649 6.37e-14

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: 70.25  E-value: 6.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAKINEMFSVARR-NAPAFVFVDEIDAIAgrharkdp 605
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTsRRGLLLFVDEADAFL-------- 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 685333866  606 RRRAT---FEALIAQLDGEKEKTGidrfSLRQAVIFICATNRPDELD 649
Cdd:cd19512    95 RKRSTekiSEDLRAALNAFLYRTG----EQSNKFMLVLASNQPEQFD 137
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
527-664 6.87e-14

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: 70.30  E-value: 6.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAKI-NEMFSVARRNAPAFVFVDEIDA-IAGRHARKD 604
Cdd:cd19523    34 RSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKIlQASFLAARCRQPSVLFISDLDAlLSSQDDEAS 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  605 PRRRATFEaLIAQLDGEKEktgidrfSLRQAVIFICATNRPDELDLEFVRsgRIDRRLYI 664
Cdd:cd19523   114 PVGRLQVE-LLAQLDGVLG-------SGEDGVLVVCTTSKPEEIDESLRR--YFSKRLLV 163
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
504-664 1.00e-13

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: 69.69  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  504 LLDELMIYMGNPMQYYEKDVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSgaakINEMFSVARRN 583
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDR----LNHLLNTAPKQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  584 apAFVFVDEID-AIAGRHARKDPRR------RATFEALIAQLDG---EKEKtgidrfslrqavIFICATNRPDELDLEFV 653
Cdd:cd19510    77 --SIILLEDIDaAFESREHNKKNPSaygglsRVTFSGLLNALDGvasSEER------------IVFMTTNHIERLDPALI 142
                         170
                  ....*....|.
gi 685333866  654 RSGRIDRRLYI 664
Cdd:cd19510   143 RPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
527-668 4.75e-13

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: 67.78  E-value: 4.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866    527 RGVLLSGPPGTGKTLFARTLAKE---SGLPFVFASGAEFTD---------------SEKSGAAKINEMFSVARRNAPAFV 588
Cdd:smart00382    3 EVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEevldqllliivggkkASGSGELRLRLALALARKLKPDVL 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866    589 FVDEIDAIAGRHARKDPRRRATFEALIaqldgekektgidRFSLRQAVIFICATNRPDELDLEFVRSgRIDRRLYIGLPD 668
Cdd:smart00382   83 ILDEITSLLDAEQEALLLLLEELRLLL-------------LLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
524-664 9.51e-13

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: 67.01  E-value: 9.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  524 PFVRGVLLSGPPGTGKTLFARTLAKESGLPFV-FASGAEFTDSEKSGAAKINEMFSVARRNAPAFVFVDEID---AIAGR 599
Cdd:cd19507    29 PTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLrLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkgfSNADS 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685333866  600 HARKDPRRRaTFEALIAQLdgeKEKTgidrfslrqAVIFICAT-NRPDELDLEFVRSGRIDRRLYI 664
Cdd:cd19507   109 KGDSGTSSR-VLGTFLTWL---QEKK---------KPVFVVATaNNVQSLPPELLRKGRFDEIFFV 161
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
688-730 8.74e-12

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: 60.63  E-value: 8.74e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 685333866   688 DIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSSIYQQDI 730
Cdd:pfam17862    1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDL 43
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
515-664 1.90e-07

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: 52.11  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  515 PMQYYEK-DVPFVRGVLLSGPPGTGKTLFARTLAKE-SGLPFVFASGAEFTD-----SEKSgaakINEMFSVA----RRN 583
Cdd:cd19504    23 PPEIVEQlGCKHVKGILLYGPPGTGKTLMARQIGKMlNAREPKIVNGPEILNkyvgeSEAN----IRKLFADAeeeqRRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  584 APA----FVFVDEIDAI-AGRHARKDPR--RRATFEALIAQLDGEKEKTGIdrfslrqavIFICATNRPDELDLEFVRSG 656
Cdd:cd19504    99 GANsglhIIIFDEIDAIcKQRGSMAGSTgvHDTVVNQLLSKIDGVEQLNNI---------LVIGMTNRKDLIDEALLRPG 169

                  ....*...
gi 685333866  657 RIDRRLYI 664
Cdd:cd19504   170 RLEVQMEI 177
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
529-605 2.57e-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: 52.00  E-value: 2.57e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGaakiNEMFSVARRNAPAFVFVDEIDAIAGRHARKDP 605
Cdd:cd19498    49 ILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGYVG----RDVESIIRDLVEGIVFIDEIDKIAKRGGSSGP 121
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
529-593 1.37e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.01  E-value: 1.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEftdsekSGAAKINEMFSVARRNAPAF----VFVDEI 593
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT------SGVKDLREVIEEARQRRSAGrrtiLFIDEI 101
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
530-646 1.37e-06

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: 49.86  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  530 LLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTD-SEKSG---------AAKINEMFSVARRNAPAFVfVDEIDAIaGR 599
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDeAEIRGhrrtyvgamPGRIIQALKKAGTNNPVFL-LDEIDKI-GS 118
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 685333866  600 HARKDPrrratFEALIAQLDGEKEKTGIDR-----FSLRQaVIFICATNRPD 646
Cdd:cd19500   119 SFRGDP-----ASALLEVLDPEQNSTFSDHyldvpFDLSK-VLFIATANSLD 164
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
527-584 3.51e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 50.74  E-value: 3.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESG--LPFVFASGAEFTDSEKsgaaKINEMFSVARRNA 584
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEIYSAEL----KKTEFLMQALRKA 120
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
529-593 9.35e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 49.28  E-value: 9.35e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEftdsekSGAAKINEMFSVARRNA----PAFVFVDEI 593
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSAVT------SGVKDIREVIEEARERRaygrRTILFVDEI 114
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
527-566 1.91e-05

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: 48.07  E-value: 1.91e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 685333866   527 RGVLLSGPPGTGKTLFARTLAKESG--LPFVFASGAEFTDSE 566
Cdd:pfam06068   51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLE 92
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
529-597 4.22e-05

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: 46.44  E-value: 4.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-------DSEkSGAAKI--NEMFSVARRNApAFVFVDEIDAIA 597
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeagyvgeDVE-NILLKLlqAADYDVERAQR-GIVYIDEIDKIA 128
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
529-554 9.68e-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: 45.54  E-value: 9.68e-05
                          10        20
                  ....*....|....*....|....*.
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPF 554
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPF 59
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
529-597 2.32e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.76  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFT-------DSE--------KSGaakinemFSVARrnapA---FVFV 590
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTeagyvgeDVEnillkllqAAD-------YDVEK----AqrgIVYI 179

                  ....*..
gi 685333866  591 DEIDAIA 597
Cdd:PRK05342  180 DEIDKIA 186
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
529-557 3.04e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 44.27  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....*....
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFA 557
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTLARILDVPFAIA 140
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
520-663 6.55e-04

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 43.74  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  520 EKDVPfvrgVLLSGPPGTGKTLFARTLAKES---GLPFVF----ASGAEFTDSEKSGAAKinEMFSVARRNAPAF----- 587
Cdd:COG3284   342 DRDIP----VLILGETGTGKELFARAIHAASpraDGPFVAvncaAIPEELIESELFGYEP--GAFTGARRKGRPGkieqa 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  588 ----VFVDEIDAIAGRHARkdprrratfeALIAQLDgEKEKTGIDRFSLRQAVI-FICATNRPDEldlEFVRSGRIDRRL 662
Cdd:COG3284   416 dggtLFLDEIGDMPLALQA----------RLLRVLQ-EREVTPLGGTKPIPVDVrLIAATHRDLR---ELVAAGRFREDL 481

                  .
gi 685333866  663 Y 663
Cdd:COG3284   482 Y 482
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
529-593 2.05e-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: 39.79  E-value: 2.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685333866   529 VLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFtdsEKSG--AAKINEMfsvarrNAPAFVFVDEI 593
Cdd:pfam05496   36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---ERPGdlAAILTNL------EPGDVLFIDEI 93
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
528-654 2.25e-03

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.20  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866   528 GVLLSGPPGTGKTLFARTLAKE-SGLPFVFASGAEFTDSE--------KSGAAKINEmfSVARRNA--PAFVFVDEIDAI 596
Cdd:pfam07728    1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTEEdlfgrrniDPGGASWVD--GPLVRAAreGEIAVLDEINRA 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685333866   597 agrharkdprRRATFEALIAQLDgEKEKTGIDRFSLRQA----VIFICATNRPD----ELDLEFVR 654
Cdd:pfam07728   79 ----------NPDVLNSLLSLLD-ERRLLLPDGGELVKAapdgFRLIATMNPLDrglnELSPALRS 133
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
529-559 2.57e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.27  E-value: 2.57e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASG 559
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 84
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
524-651 2.85e-03

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: 39.43  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  524 PFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSE--KSGAAKINEM-FSVARRNAPAFVFVDEID-----A 595
Cdd:cd19506    24 PLVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYpgKNGLQMMLHLvLKVARQLQPSVIWIGDAEktfykK 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 685333866  596 IAGRHARKDPRR-RATFEALIAQLDGEkektgiDRfslrqaVIFICATNRPDELDLE 651
Cdd:cd19506   104 VPKTEKQLDPKRlKKDLPKILKSLKPE------DR------VLIVGTTSRPFEADLK 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
522-593 4.55e-03

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 38.90  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685333866  522 DVPFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSE---------------KSGAAKINEMFSVARRNAPA 586
Cdd:cd19505     8 GLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmlilKESLHRLNLQFELAKAMSPC 87

                  ....*..
gi 685333866  587 FVFVDEI 593
Cdd:cd19505    88 IIWIPNI 94
PRK04195 PRK04195
replication factor C large subunit; Provisional
527-599 4.77e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 40.67  E-value: 4.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685333866  527 RGVLLSGPPGTGKTLFARTLAKESGLPFVfasgaEFTDSEKSGAAKINEMFSVARRNAPAF------VFVDEIDAIAGR 599
Cdd:PRK04195   40 KALLLYGPPGVGKTSLAHALANDYGWEVI-----ELNASDQRTADVIERVAGEAATSGSLFgarrklILLDEVDGIHGN 113
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
529-557 5.10e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 38.94  E-value: 5.10e-03
                           10        20
                   ....*....|....*....|....*....
gi 685333866   529 VLLSGPPGTGKTLFARTLAKESGLPFVFA 557
Cdd:TIGR02173    3 ITISGPPGSGKTTVAKILAEKLSLKLISA 31
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
529-559 6.29e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 40.06  E-value: 6.29e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 685333866  529 VLLSGPPGTGKTLFARTLAKESGLPFVFASG 559
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
527-584 9.11e-03

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 38.77  E-value: 9.11e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685333866   527 RGVLLSGPPGTGKTLFARTL----AKESGLPFVFAS---------------GAEFTDSEKSGAAKINEMFSVARRNA 584
Cdd:pfam06745   20 RVVLITGGPGTGKTIFGLQFlyngALKYGEPGVFVTleeppedlrenarsfGWDLEKLEEEGKLAIIDASTSGIGIA 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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