NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71994521|ref|NP_491165|]
View 

AFG3-like protein spg-7 [Caenorhabditis elegans]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
126-732 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 746.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 126 IAVSVGILLALYAFMDyQSYREISWKEFYSDfLEAGLVERLEVVDKRwVRIVSSSGKYAGQTCYfnIGSVDSFERSLgaA 205
Cdd:COG0465   1 IALLLVLLFNLFSSSS-SSVKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGTKTRFTTY--RVNDPELVDLL--E 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 206 QHHLQYDADRQipvlykSEFNFkreIPNLISVAFP--LLFGYYIY---RMlkgggaaggagragggglggmfggfgQ--- 277
Cdd:COG0465  74 EKGVEVTAKPP------EESSW---LLSLLISLLPilLLIGLWIFfmrRM--------------------------Qggg 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 278 --------STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGE 349
Cdd:COG0465 119 ggamsfgkSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGE 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 350 ANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgrkrggkggmggHSEQENTLNQLLVEMDGFTT 429
Cdd:COG0465 199 AGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVgrqrga-glgggHDEREQTLNQLLVEMDGFEG 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 430 DEsSVIVIAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRtsLDKTVLSRKLAAHTPGFSGADISNV 509
Cdd:COG0465 278 NE-GVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDVDLEVIARRTPGFSGADLANL 354
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 510 CNEAALIAARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLG 589
Cdd:COG0465 355 VNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALG 434
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 590 YAQYLPKE-QYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPAP--- 665
Cdd:COG0465 435 YTMQLPEEdRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevf 514
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521 666 --GEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGK 732
Cdd:COG0465 515 lgRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
126-732 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 746.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 126 IAVSVGILLALYAFMDyQSYREISWKEFYSDfLEAGLVERLEVVDKRwVRIVSSSGKYAGQTCYfnIGSVDSFERSLgaA 205
Cdd:COG0465   1 IALLLVLLFNLFSSSS-SSVKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGTKTRFTTY--RVNDPELVDLL--E 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 206 QHHLQYDADRQipvlykSEFNFkreIPNLISVAFP--LLFGYYIY---RMlkgggaaggagragggglggmfggfgQ--- 277
Cdd:COG0465  74 EKGVEVTAKPP------EESSW---LLSLLISLLPilLLIGLWIFfmrRM--------------------------Qggg 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 278 --------STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGE 349
Cdd:COG0465 119 ggamsfgkSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGE 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 350 ANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgrkrggkggmggHSEQENTLNQLLVEMDGFTT 429
Cdd:COG0465 199 AGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVgrqrga-glgggHDEREQTLNQLLVEMDGFEG 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 430 DEsSVIVIAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRtsLDKTVLSRKLAAHTPGFSGADISNV 509
Cdd:COG0465 278 NE-GVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDVDLEVIARRTPGFSGADLANL 354
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 510 CNEAALIAARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLG 589
Cdd:COG0465 355 VNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALG 434
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 590 YAQYLPKE-QYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPAP--- 665
Cdd:COG0465 435 YTMQLPEEdRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevf 514
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521 666 --GEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGK 732
Cdd:COG0465 515 lgRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
278-731 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 687.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   278 STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITV 357
Cdd:TIGR01241  40 SKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   358 SGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIVI 437
Cdd:TIGR01241 120 SGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV-GRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNT-GVIVI 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   438 AATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLgpLRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIA 517
Cdd:TIGR01241 198 AATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA--KNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   518 ARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLPKE 597
Cdd:TIGR01241 276 ARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEE 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   598 -QYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSF-----ETPAPGEMAFD 671
Cdd:TIGR01241 356 dKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYgsdggDVFLGRGFAKA 435
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   672 KPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVG 731
Cdd:TIGR01241 436 KEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
278-742 1.86e-169

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 503.04  E-value: 1.86e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  278 STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITV 357
Cdd:CHL00176 168 SKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSI 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  358 SGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDeSSVIVI 437
Cdd:CHL00176 248 SGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAV-GRQRGAGIGGGNDEREQTLNQLLTEMDGFKGN-KGVIVI 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  438 AATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIA 517
Cdd:CHL00176 326 AATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHAR--NKKLSPDVSLELIARRTPGFSGADLANLLNEAAILT 403
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  518 ARDANHEISNKHFEQAIERVVAGMEKKTQVLQKeEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLP-K 596
Cdd:CHL00176 404 ARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeE 482
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  597 EQYLYSKDQLLDRMCMTLGGRVAEEIFFG--RITTGAQDDLQKVTQMAYSQVVKFGMSeKVGPLSFETPAPGE------M 668
Cdd:CHL00176 483 DQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfM 561
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994521  669 AFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGKR-PFVEKNTYE 742
Cdd:CHL00176 562 QRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
290-462 9.83e-107

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: 323.80  E-value: 9.83e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 290 VKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 369
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 370 GPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIVIAATNRVDILDSA 449
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAV-GRKRGAGLGGGHDEREQTLNQLLVEMDGFESNT-GVIVIAATNRPDVLDPA 158
                       170
                ....*....|...
gi 71994521 450 LLRPGRFDRQIYV 462
Cdd:cd19501 159 LLRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
547-729 6.28e-87

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.94  E-value: 6.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   547 VLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYSKDQLLDRMCMTLGGRVAEEIFFG 625
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   626 RITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPA-----PGEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDL 700
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKEI 161
                         170       180
                  ....*....|....*....|....*....
gi 71994521   701 LLEKRSDIERVALRLLEKEILNREDMIEL 729
Cdd:pfam01434 162 LTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
326-466 2.76e-19

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: 85.12  E-value: 2.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521    326 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDMFSMARKNSPCI 388
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994521    389 LFIDEIDAVGRKRGGKGGMGGHSEQENTLNQLlvemdgfttdESSVIVIAATNRVDILDSALLRPgRFDRQIYVPVPD 466
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLLLKS----------EKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
126-732 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 746.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 126 IAVSVGILLALYAFMDyQSYREISWKEFYSDfLEAGLVERLEVVDKRwVRIVSSSGKYAGQTCYfnIGSVDSFERSLgaA 205
Cdd:COG0465   1 IALLLVLLFNLFSSSS-SSVKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGTKTRFTTY--RVNDPELVDLL--E 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 206 QHHLQYDADRQipvlykSEFNFkreIPNLISVAFP--LLFGYYIY---RMlkgggaaggagragggglggmfggfgQ--- 277
Cdd:COG0465  74 EKGVEVTAKPP------EESSW---LLSLLISLLPilLLIGLWIFfmrRM--------------------------Qggg 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 278 --------STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGE 349
Cdd:COG0465 119 ggamsfgkSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGE 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 350 ANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgrkrggkggmggHSEQENTLNQLLVEMDGFTT 429
Cdd:COG0465 199 AGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVgrqrga-glgggHDEREQTLNQLLVEMDGFEG 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 430 DEsSVIVIAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRtsLDKTVLSRKLAAHTPGFSGADISNV 509
Cdd:COG0465 278 NE-GVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDVDLEVIARRTPGFSGADLANL 354
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 510 CNEAALIAARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLG 589
Cdd:COG0465 355 VNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALG 434
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 590 YAQYLPKE-QYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPAP--- 665
Cdd:COG0465 435 YTMQLPEEdRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevf 514
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521 666 --GEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGK 732
Cdd:COG0465 515 lgRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
278-731 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 687.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   278 STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITV 357
Cdd:TIGR01241  40 SKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   358 SGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIVI 437
Cdd:TIGR01241 120 SGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV-GRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNT-GVIVI 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   438 AATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLgpLRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIA 517
Cdd:TIGR01241 198 AATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHA--KNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   518 ARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLPKE 597
Cdd:TIGR01241 276 ARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEE 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   598 -QYLYSKDQLLDRMCMTLGGRVAEEIFFGRITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSF-----ETPAPGEMAFD 671
Cdd:TIGR01241 356 dKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYgsdggDVFLGRGFAKA 435
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   672 KPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVG 731
Cdd:TIGR01241 436 KEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
278-742 1.86e-169

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 503.04  E-value: 1.86e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  278 STARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITV 357
Cdd:CHL00176 168 SKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSI 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  358 SGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDeSSVIVI 437
Cdd:CHL00176 248 SGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAV-GRQRGAGIGGGNDEREQTLNQLLTEMDGFKGN-KGVIVI 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  438 AATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIA 517
Cdd:CHL00176 326 AATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHAR--NKKLSPDVSLELIARRTPGFSGADLANLLNEAAILT 403
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  518 ARDANHEISNKHFEQAIERVVAGMEKKTQVLQKeEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLP-K 596
Cdd:CHL00176 404 ARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPeE 482
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  597 EQYLYSKDQLLDRMCMTLGGRVAEEIFFG--RITTGAQDDLQKVTQMAYSQVVKFGMSeKVGPLSFETPAPGE------M 668
Cdd:CHL00176 483 DQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDpflgrfM 561
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994521  669 AFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGKR-PFVEKNTYE 742
Cdd:CHL00176 562 QRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTWK 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
277-733 5.33e-152

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 458.34  E-value: 5.33e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  277 QSTARVINREDIKVKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFIT 356
Cdd:PRK10733 136 KSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFT 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  357 VSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIV 436
Cdd:PRK10733 216 ISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAV-GRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNE-GIIV 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  437 IAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLG--PLRTSLDKTVLSRKlaahTPGFSGADISNVCNEAA 514
Cdd:PRK10733 294 IAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRrvPLAPDIDAAIIARG----TPGFSGADLANLVNEAA 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  515 LIAARDANHEISNKHFEQAIERVVAGMEKKTQVLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYL 594
Cdd:PRK10733 370 LFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFL 449
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  595 PKEQYLYSKDQLLDRMCMTL-GGRVAEEIFFG--RITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFeTPAPGEM--- 668
Cdd:PRK10733 450 PEGDAISASRQKLESQISTLyGGRLAEEIIYGpeHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLY-AEEEGEVflg 528
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994521  669 ---AFDKPYSEATAQLIDQEVRDLVMNALRRTRDLLLEKRSDIERVALRLLEKEILNREDMIELVGKR 733
Cdd:PRK10733 529 rsvAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR 596
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
290-462 9.83e-107

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: 323.80  E-value: 9.83e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 290 VKFADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGV 369
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 370 GPARVRDMFSMARKNSPCILFIDEIDAVgRKRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIVIAATNRVDILDSA 449
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAV-GRKRGAGLGGGHDEREQTLNQLLVEMDGFESNT-GVIVIAATNRPDVLDPA 158
                       170
                ....*....|...
gi 71994521 450 LLRPGRFDRQIYV 462
Cdd:cd19501 159 LLRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
290-545 5.17e-105

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 325.42  E-value: 5.17e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 290 VKFADVAGCEEAKIEIMEFV-NFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 368
Cdd:COG1222  75 VTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 369 VGPARVRDMFSMARKNSPCILFIDEIDAVgrkRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIVIAATNRVDILDS 448
Cdd:COG1222 155 EGARNVREVFELAREKAPSIIFIDEIDAI---AARRTDDGTSGEVQRTVNQLLAELDGFESRG-DVLIIAATNRPDLLDP 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 449 ALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRtsLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNK 528
Cdd:COG1222 231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMP--LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTME 308
                       250
                ....*....|....*..
gi 71994521 529 HFEQAIERVVAGMEKKT 545
Cdd:COG1222 309 DLEKAIEKVKKKTETAT 325
Peptidase_M41 pfam01434
Peptidase family M41;
547-729 6.28e-87

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.94  E-value: 6.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   547 VLQKEEKKTVAYHEAGHAIAGWFLQHADPLLKVSIIPRGKGLGYAQYLPKEQ-YLYSKDQLLDRMCMTLGGRVAEEIFFG 625
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   626 RITTGAQDDLQKVTQMAYSQVVKFGMSEKVGPLSFETPA-----PGEMAFDKPYSEATAQLIDQEVRDLVMNALRRTRDL 700
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKEI 161
                         170       180
                  ....*....|....*....|....*....
gi 71994521   701 LLEKRSDIERVALRLLEKEILNREDMIEL 729
Cdd:pfam01434 162 LTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
282-544 6.60e-87

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 280.18  E-value: 6.60e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  282 VINREDikVKFADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGS 360
Cdd:PRK03992 122 VIESPN--VTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  361 EFLEMFVGVGpAR-VRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGHsEQENTLNQLLVEMDGFtTDESSVIVIAA 439
Cdd:PRK03992 200 ELVQKFIGEG-ARlVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDR-EVQRTLMQLLAEMDGF-DPRGNVKIIAA 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  440 TNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAAR 519
Cdd:PRK03992 277 TNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR--KMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIR 354
                        250       260
                 ....*....|....*....|....*
gi 71994521  520 DANHEISNKHFEQAIERVVAGMEKK 544
Cdd:PRK03992 355 DDRTEVTMEDFLKAIEKVMGKEEKD 379
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
292-537 1.21e-75

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: 250.60  E-value: 1.21e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 292 FADVAGCEEAKIEIMEFVN-FLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 370
Cdd:COG0464 156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 371 PARVRDMFSMARKNSPCILFIDEIDAVgrKRGGKGGMGGHSEQEntLNQLLVEMDGFTTDessVIVIAATNRVDILDSAL 450
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADAL--AGKRGEVGDGVGRRV--VNTLLTEMEELRSD---VVVIAATNRPDLLDPAL 308
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 451 LRpgRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNKHF 530
Cdd:COG0464 309 LR--RFDEIIFFPLPDAEERLEIFRIHLR--KRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384

                ....*..
gi 71994521 531 EQAIERV 537
Cdd:COG0464 385 LEALERE 391
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
286-537 1.88e-69

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 232.77  E-value: 1.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   286 EDIKVKFADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLE 364
Cdd:TIGR01242 115 ERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   365 MFVGVGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGHsEQENTLNQLLVEMDGFTTdESSVIVIAATNRVD 444
Cdd:TIGR01242 195 KYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR-EVQRTLMQLLAELDGFDP-RGNVKVIAATNRPD 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   445 ILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHE 524
Cdd:TIGR01242 273 ILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTR--KMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY 350
                         250
                  ....*....|...
gi 71994521   525 ISNKHFEQAIERV 537
Cdd:TIGR01242 351 VTMDDFIKAVEKV 363
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
278-554 1.02e-63

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 227.10  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   278 STARVINREDIKVKFADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFIT 356
Cdd:TIGR01243 438 SAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIA 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   357 VSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMgghSEQENTLNQLLVEMDGFtTDESSVIV 436
Cdd:TIGR01243 518 VRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDT---SVTDRIVNQLLTEMDGI-QELSNVVV 593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   437 IAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLrtSLDKTVLSRKLAAHTPGFSGADISNVCNEAALI 516
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSM--PLAEDVDLEELAEMTEGYTGADIEAVCREAAMA 671
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   517 AARDA------------------NHEISNKHFEQAIERVVAGMEKKT----QVLQKEEKK 554
Cdd:TIGR01243 672 ALRESigspakeklevgeeeflkDLKVEMRHFLEALKKVKPSVSKEDmlryERLAKELKR 731
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
292-537 9.39e-59

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 206.16  E-value: 9.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  292 FADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 370
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  371 PARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGhSEQENTLNQLLVEMDGFTTdESSVIVIAATNRVDILDSAL 450
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGE-KEIQRTMLELLNQLDGFDS-RGDVKVIMATNRIESLDPAL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  451 LRPGRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNKHF 530
Cdd:PTZ00361 340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTS--KMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                 ....*..
gi 71994521  531 EQAIERV 537
Cdd:PTZ00361 418 RKAKEKV 424
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
292-462 1.97e-58

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: 196.02  E-value: 1.97e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 292 FADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVG 370
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 371 PARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGhSEQENTLNQLLVEMDGFTTdESSVIVIAATNRVDILDSAL 450
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGD-REVQRTMLELLNQLDGFDP-RGNIKVIMATNRPDILDPAL 159
                       170
                ....*....|..
gi 71994521 451 LRPGRFDRQIYV 462
Cdd:cd19502 160 LRPGRFDRKIEF 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
290-538 1.83e-57

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 201.53  E-value: 1.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  290 VKFADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 368
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  369 VGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGGHsEQENTLNQLLVEMDGFTTDeSSVIVIAATNRVDILDS 448
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADR-EVQRILLELLNQMDGFDQT-TNVKVIMATNRADTLDP 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  449 ALLRPGRFDRQIYVPVPDIKGRASIFRVHLGplRTSLDKTVLSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNK 528
Cdd:PTZ00454 300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTITS--KMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPK 377
                        250
                 ....*....|
gi 71994521  529 HFEQAIERVV 538
Cdd:PTZ00454 378 DFEKGYKTVV 387
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
292-536 1.19e-56

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 193.95  E-value: 1.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 292 FADVAGCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 371
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 372 ARVRDMFSMARKNsPCILFIDEIDAVgrkRGGKGGMGGHSEQENTLNQLLVEMDGFTtdeSSVIVIAATNRVDILDSALL 451
Cdd:COG1223  81 RNLRKLFDFARRA-PCVIFFDEFDAI---AKDRGDQNDVGEVKRVVNALLQELDGLP---SGSVVIAATNHPELLDSALW 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 452 RpgRFDRQIYVPVPDIKGRASIFRVHLGPLRTSLDKTvlSRKLAAHTPGFSGADISNVCNEAALIAARDANHEISNKHFE 531
Cdd:COG1223 154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELD--LKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229

                ....*
gi 71994521 532 QAIER 536
Cdd:COG1223 230 EALKQ 234
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
301-462 5.66e-53

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 180.94  E-value: 5.66e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 301 AKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFS 379
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 380 MARKNSPCILFIDEIDAVGRKRGGKGGMgghSEQENTLNQLLVEMDGFTTdESSVIVIAATNRVDILDSALLRPGRFDRQ 459
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSDSS---GVTDRVVSQLLTELDGIES-LKGVVVIAATNRPDMIDPALLRPGRLDKL 156

                ...
gi 71994521 460 IYV 462
Cdd:cd19511 157 IYV 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
301-462 7.28e-53

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: 180.56  E-value: 7.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 301 AKIEIMEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSM 380
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 381 ARKNSPCILFIDEIDAVgrkRGGKGGMGGHSEQENTLNQLLVEMDGFTTDEsSVIVIAATNRVDILDSALLRPGRFDRQI 460
Cdd:cd19481  81 ARRLAPCILFIDEIDAI---GRKRDSSGESGELRRVLNQLLTELDGVNSRS-KVLVIAATNRPDLLDPALLRPGRFDEVI 156

                ..
gi 71994521 461 YV 462
Cdd:cd19481 157 EF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
330-464 1.14e-52

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 178.94  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   330 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDAVgrkrGGKGGMGG 409
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL----AGSRGSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71994521   410 HSEQENTLNQLLVEMDGFTTDESSVIVIAATNRVDILDSALLrpGRFDRQIYVPV 464
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
294-462 5.08e-52

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 178.25  E-value: 5.08e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 372
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 373 RVRDMFSMARKNSPCILFIDEIDAVgrkrgGKGGMGGHSEQENTL-NQLLVEMDGFTTDeSSVIVIAATNRVDILDSALL 451
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDAL-----APKREEDQREVERRVvAQLLTLMDGMSSR-GKVVVIAATNRPDAIDPALR 154
                       170
                ....*....|.
gi 71994521 452 RPGRFDRQIYV 462
Cdd:cd19503 155 RPGRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
289-519 1.32e-51

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 192.43  E-value: 1.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   289 KVKFADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFV 367
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   368 GVGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGMGghseQENTLNQLLVEMDGFtTDESSVIVIAATNRVDILD 447
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEV----EKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALD 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71994521   448 SALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRTSLDktVLSRKLAAHTPGFSGADISNVCNEAALIAAR 519
Cdd:TIGR01243 329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAED--VDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
301-462 1.15e-47

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 166.13  E-value: 1.15e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 301 AKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFS 379
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 380 MARKNSPCILFIDEIDAVGRKRGGKGGMGGhseQENTLNQLLVEMDGFTTDEsSVIVIAATNRVDILDSALLRPGRFDRQ 459
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGV---TERVVNQLLTELDGLEEMN-GVVVIAATNRPDIIDPALLRAGRFDRL 156

                ...
gi 71994521 460 IYV 462
Cdd:cd19529 157 IYI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
294-463 2.73e-45

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 159.91  E-value: 2.73e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 372
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 373 RVRDMFSMARKNSPCILFIDEIDAVgrkrgGKGGMGGHSEQENTL-NQLLVEMDGFTTdESSVIVIAATNRVDILDSALL 451
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAI-----APKREKTHGEVERRIvSQLLTLMDGLKQ-RAHVIVMAATNRPNSIDPALR 154
                       170
                ....*....|..
gi 71994521 452 RPGRFDRQIYVP 463
Cdd:cd19519 155 RFGRFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
306-462 2.18e-44

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: 157.26  E-value: 2.18e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 306 MEFVNFLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNS 385
Cdd:cd19530  10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71994521 386 PCILFIDEIDAVGRKRGGKGGmgghSEQENTLNQLLVEMDGFtTDESSVIVIAATNRVDILDSALLRPGRFDRQIYV 462
Cdd:cd19530  90 PCVIFFDEVDALVPKRGDGGS----WASERVVNQLLTEMDGL-EERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
302-462 2.21e-44

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: 156.90  E-value: 2.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 302 KIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSM 380
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 381 ARKNSPCILFIDEIDAVGRKRGGKGGMGGHSeQENTLNQLLVEMDGFTTdESSVIVIAATNRVDILDSALLRPGRFDRQI 460
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGA-ADRVINQILTEMDGMNT-KKNVFIIGATNRPDIIDPAILRPGRLDQLI 159

                ..
gi 71994521 461 YV 462
Cdd:cd19528 160 YI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
294-460 1.09e-42

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: 152.56  E-value: 1.09e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNFLK-NPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 372
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 373 RVRDMFSMARKNSPCILFIDEIDAVGRKRGGKGGmgghsEQENTL-NQLLVEMDGFT---TDESSVIVIAATNRVDILDS 448
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQR-----EMERRIvSQLLTCMDELNnekTAGGPVLVIGATNRPDSLDP 155
                       170
                ....*....|..
gi 71994521 449 ALLRPGRFDRQI 460
Cdd:cd19518 156 ALRRAGRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
302-462 2.15e-38

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: 140.34  E-value: 2.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 302 KIEIMEFVNF-LKNPQQYKDlGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSM 380
Cdd:cd19527   2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 381 ARKNSPCILFIDEIDAVGRKRGGKGGMGghSEQENTLNQLLVEMDGFTTDESSVIVIAATNRVDILDSALLRPGRFDRQI 460
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSGDSG--GVMDRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                ..
gi 71994521 461 YV 462
Cdd:cd19527 159 YL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
313-461 1.27e-37

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: 137.95  E-value: 1.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 313 KNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFID 392
Cdd:cd19526  14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71994521 393 EIDAVGRKRGgkggmgghseQENT------LNQLLVEMDGfTTDESSVIVIAATNRVDILDSALLRPGRFDRQIY 461
Cdd:cd19526  94 EFDSIAPKRG----------HDSTgvtdrvVNQLLTQLDG-VEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
295-462 8.24e-36

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: 132.86  E-value: 8.24e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 295 VAGCEEAKIEIMEFVNF-LKNPQQYKdLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR 373
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 374 VRDMFSMARKNSPCILFIDEIDAVgrkrGGKGGMGGHSEQENTLNQLLVEMDGFTTDESS-VIVIAATNRVDILDSALLR 452
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSL----LSERGSGEHEASRRVKTEFLVQMDGVLNKPEDrVLVLGATNRPWELDEAFLR 155
                       170
                ....*....|
gi 71994521 453 pgRFDRQIYV 462
Cdd:cd19509 156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
289-462 2.36e-34

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: 129.21  E-value: 2.36e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 289 KVKFADVAGCEEAKIEIMEFVNF-LKNPQQYKdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMF 366
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 367 VGVGPARVRDMFSMARKNSPCILFIDEIDAVgrkrggkggMGGHSEQENTL-----NQLLVEMDGFTTDESSVIVIAATN 441
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSL---------CGTRGEGESEAsrrikTELLVQMNGVGNDSQGVLVLGATN 151
                       170       180
                ....*....|....*....|.
gi 71994521 442 RVDILDSALLRpgRFDRQIYV 462
Cdd:cd19521 152 IPWQLDSAIRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
294-456 2.31e-31

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: 120.22  E-value: 2.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKDLG-AKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 371
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 372 ARVRDMFSMARKNSPCILFIDEIDAVgrkrGGKGGMGGHSEQENTLNQLLVEMDGFTTDESS-VIVIAATNRVDILDSAL 450
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSF----LRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCrVIVMGATNRPQDLDEAI 156

                ....*...
gi 71994521 451 LR--PGRF 456
Cdd:cd19520 157 LRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
290-462 1.60e-29

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: 115.86  E-value: 1.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 290 VKFADVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVG 368
Cdd:cd19525  19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 369 VGPARVRDMFSMARKNSPCILFIDEIDAVgrkrGGKGGMGGHSEQENTLNQLLVEMDGFTT-DESSVIVIAATNRVDILD 447
Cdd:cd19525  98 EGEKMVRALFSVARCKQPAVIFIDEIDSL----LSQRGEGEHESSRRIKTEFLVQLDGATTsSEDRILVVGATNRPQEID 173
                       170
                ....*....|....*
gi 71994521 448 SALLRpgRFDRQIYV 462
Cdd:cd19525 174 EAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
294-462 3.75e-29

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: 113.79  E-value: 3.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKiPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 372
Cdd:cd19524   1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 373 RVRDMFSMARKNSPCILFIDEIDAVgrkrGGKGGMGGHSEQENTLNQLLVEMDGFTTD-ESSVIVIAATNRVDILDSALL 451
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSL----LSERSEGEHEASRRLKTEFLIEFDGVQSNgDDRVLVMGATNRPQELDDAVL 155
                       170
                ....*....|.
gi 71994521 452 RpgRFDRQIYV 462
Cdd:cd19524 156 R--RFTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
294-461 8.78e-29

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: 112.99  E-value: 8.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEAN-----VPFITVSGSEFLEMFV 367
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 368 GVGPARVRDMFSMARKNSPCILFIDEIDAVGRKRGgkggmgghSEQENT----LNQLLVEMDGFTTdESSVIVIAATNRV 443
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRS--------SKQEQIhasiVSTLLALMDGLDN-RGQVVVIGATNRP 151
                       170
                ....*....|....*...
gi 71994521 444 DILDSALLRPGRFDRQIY 461
Cdd:cd19517 152 DALDPALRRPGRFDREFY 169
ycf46 CHL00195
Ycf46; Provisional
282-549 6.60e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 118.20  E-value: 6.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  282 VINREDI------KVKFADVAGCEEAKieimEFVNFLKN--PQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVP 353
Cdd:CHL00195 211 IISQTEIlefysvNEKISDIGGLDNLK----DWLKKRSTsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLP 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  354 FITVSGSEFLEMFVGVGPARVRDMFSMARKNSPCILFIDEIDavgrkrggKGGMGGHSEQEN-TLNQLLVEMDGFTTDE- 431
Cdd:CHL00195 287 LLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEID--------KAFSNSESKGDSgTTNRVLATFITWLSEKk 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  432 SSVIVIAATNRVDILDSALLRPGRFDRQIYVPVPDIKGRASIFRVHLGPLRTSLDKTVLSRKLAAHTPGFSGADISNVCN 511
Cdd:CHL00195 359 SPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSII 438
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 71994521  512 EAALIAArDANHEISNKHFEQAIERVV--AGMEK-KTQVLQ 549
Cdd:CHL00195 439 EAMYIAF-YEKREFTTDDILLALKQFIplAQTEKeQIEALQ 478
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
294-462 7.28e-27

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: 107.76  E-value: 7.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKdlGAKIP-KGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 371
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 372 ARVRDMFSMARKNSPCILFIDEIDAVgrkRGGKGGMGGHSEQENTLNQLLVEMDGF----TTDESS--VIVIAATNRVDI 445
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSI---CSRRGTSEEHEASRRVKSELLVQMDGVggasENDDPSkmVMVLAATNFPWD 155
                       170
                ....*....|....*..
gi 71994521 446 LDSALLRpgRFDRQIYV 462
Cdd:cd19522 156 IDEALRR--RLEKRIYI 170
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
326-463 2.18e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 99.91  E-value: 2.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 326 PKGAILTGPPGTGKTLLAKATAGEA---NVPFITVSGSEFLEMFVG---VGPARVRDMFSMARKNSPCILFIDEIDAVGR 399
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994521 400 krggkggmgghSEQENTLNQLLVEMDgFTTDESSVIVIAATNRVDILDSALLRPGRFDRQIYVP 463
Cdd:cd00009  99 -----------GAQNALLRVLETLND-LRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
315-462 3.88e-23

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: 97.18  E-value: 3.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 315 PQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANV--PFItVSGSEFLEMFVGVGPARVRDMFSMARK-------NS 385
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAEEeqrrlgaNS 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994521 386 PC-ILFIDEIDAVGRKRGGKGGMGghSEQENTLNQLLVEMDGfTTDESSVIVIAATNRVDILDSALLRPGRFDRQIYV 462
Cdd:cd19504 103 GLhIIIFDEIDAICKQRGSMAGST--GVHDTVVNQLLSKIDG-VEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
294-462 6.88e-22

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: 92.82  E-value: 6.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKiEIMEFVN--FLKNPQQYkdlGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGP 371
Cdd:cd19507   1 DVGGLDNLK-DWLKKRKaaFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 372 ARVRDMFSMARKNSPCILFIDEIDavgrkrGGKGGMGGHSEQEnTLNQLLVEMDGFTTDESS-VIVIAATNRVDILDSAL 450
Cdd:cd19507  77 SRLRQMIQTAEAIAPCVLWIDEIE------KGFSNADSKGDSG-TSSRVLGTFLTWLQEKKKpVFVVATANNVQSLPPEL 149
                       170
                ....*....|..
gi 71994521 451 LRPGRFDRQIYV 462
Cdd:cd19507 150 LRKGRFDEIFFV 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
311-462 6.17e-21

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: 90.10  E-value: 6.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 311 FLKNPQQYKDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEflemfVGVGPARVRDMFSMARKNSpcILF 390
Cdd:cd19510   8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994521 391 IDEIDAVGRKRGGKGGMGGHSEQEN--TLNQLLVEMDGFTTDESSvIVIAATNRVDILDSALLRPGRFDRQIYV 462
Cdd:cd19510  81 LEDIDAAFESREHNKKNPSAYGGLSrvTFSGLLNALDGVASSEER-IVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
326-466 2.76e-19

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: 85.12  E-value: 2.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521    326 PKGAILTGPPGTGKTLLAKATAGEANVP---FITVSGSEFLE--------------MFVGVGPARVRDMFSMARKNSPCI 388
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994521    389 LFIDEIDAVGRKRGGKGGMGGHSEQENTLNQLlvemdgfttdESSVIVIAATNRVDILDSALLRPgRFDRQIYVPVPD 466
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLLLKS----------EKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
294-462 2.90e-16

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: 76.85  E-value: 2.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 294 DVAGCEEAKIEIMEFVNF-LKNPQQYKDLgAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPA 372
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 373 RVRDMFSMARKNSPCILFIDEIDAVgrkrgGKGGMGGHSEQENTLNQLLVEMDG-FTTDESSVIVIAATNRVDILDSALL 451
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDAL-----LSSQDDEASPVGRLQVELLAQLDGvLGSGEDGVLVVCTTSKPEEIDESLR 154
                       170
                ....*....|.
gi 71994521 452 RpgRFDRQIYV 462
Cdd:cd19523 155 R--YFSKRLLV 163
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
493-532 7.93e-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: 60.24  E-value: 7.93e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 71994521   493 KLAAHTPGFSGADISNVCNEAALIAARDANHEISNKHFEQ 532
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
321-462 1.26e-11

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: 63.55  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 321 LGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFL--------------EMFVGVGPARVRDMFSMARKNSP 386
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521 387 CILFIDEIDAVGRKRGGKGGMgghsEQENTLNQLLVEM---DGFTTDESSVIVIAATNRVDILDSALLRPGRFDRQIYV 462
Cdd:cd19505  87 CIIWIPNIHELNVNRSTQNLE----EDPKLLLGLLLNYlsrDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
330-394 1.11e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 61.25  E-value: 1.11e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521  330 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDMFSMARKNS----PCILFIDEI 394
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
325-397 2.32e-09

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: 57.39  E-value: 2.32e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71994521 325 IPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEM-FVGvgparvRDMFSMARKNSPCILFIDEIDAV 397
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKI 112
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
330-394 3.44e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 59.68  E-value: 3.44e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521 330 ILTGPPGTGKTLLAKATAGEANVPFITVSGSeflemFVGVgpARVRDMFSMARKNS----PCILFIDEI 394
Cdd:COG2256  53 ILWGPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
330-456 2.24e-08

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: 53.45  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   330 ILTGPPGTGKTLLAKATAgEA--NVPFITVSGSEFLE-------MFVGVGPARVRDMFSMARKNSPCILFIDEIDavgrk 400
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDGPLVRAAREGEIAVLDEIN----- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994521   401 rggkggmGGHSEQENTLNQLLVE-----MDGFTTD---ESSVIVIAATNRVDI----LDSALLRpgRF 456
Cdd:pfam07728  77 -------RANPDVLNSLLSLLDErrlllPDGGELVkaaPDGFRLIATMNPLDRglneLSPALRS--RF 135
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
326-395 2.47e-08

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 54.12  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   326 PKGAIL-TGPPGTGKTLLAKATAGEANV---PFITVSGSEFLE-----MFVGVGPARVR-----DMFSMARKNSPCILFI 391
Cdd:pfam07724   2 PIGSFLfLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                  ....
gi 71994521   392 DEID 395
Cdd:pfam07724  82 DEIE 85
PRK04195 PRK04195
replication factor C large subunit; Provisional
291-395 4.44e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 56.47  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521  291 KFADVAGCEEAKIEIMEFV-NFLKNpqqykdlgaKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEF-----LE 364
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 71994521  365 MFVGVGpARVRDMFSMARKnspcILFIDEID 395
Cdd:PRK04195  83 RVAGEA-ATSGSLFGARRK----LILLDEVD 108
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
123-218 5.30e-07

FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes. It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress, and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear.


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 48.75  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   123 WQQIAVSVGILLALYAFMDYQSYREISWKEFYSDfLEAGLVERLEVVDKRW-----VRIVSSSGKYAGQTCYFNIGSVDS 197
Cdd:pfam06480   4 WLLILLVLLLLFLLFLLSSSSSTKEISYSEFLEY-LEAGKVKKVVVQDDEIlptgvVEGTLKDGSKFTTYFIPSLPNVDS 82
                          90       100
                  ....*....|....*....|.
gi 71994521   198 FERSLGAAQHHLQYDADRQIP 218
Cdd:pfam06480  83 LLEKLEDALEEKGVKVSVKPP 103
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
293-395 8.94e-07

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 49.86  E-value: 8.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 293 ADVAGCEEAKIEIMEFVNFLKnpqqykdLGAKIpKGAIL--TGPPGTGKTLLAKATAGEANVPFITVS-G--SEFLEM-- 365
Cdd:cd19500  10 ADHYGLEDVKERILEYLAVRK-------LKGSM-KGPILclVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrg 81
                        90       100       110
                ....*....|....*....|....*....|....
gi 71994521 366 ----FVGVGPARVRDMFSMARKNSPCILfIDEID 395
Cdd:cd19500  82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
330-450 3.04e-06

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: 47.52  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 330 ILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMfvGV-GPARVRDMFSMARK-NSPCILFIDEIDAVGRKRGGKGGM 407
Cdd:cd19512  26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEKIS 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71994521 408 gghSEQENTLNQLLvemdgFTTDESS--VIVIAATNRVDILDSAL 450
Cdd:cd19512 104 ---EDLRAALNAFL-----YRTGEQSnkFMLVLASNQPEQFDWAI 140
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
324-394 5.63e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.77  E-value: 5.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 324 KIPKGAILTGPPGTGKTLLAKATA------GEANVPFITV----SGSEFLEMFV--------GVGPARVRDMFSMARKNS 385
Cdd:COG1401 219 KTKKNVILAGPPGTGKTYLARRLAealggeDNGRIEFVQFhpswSYEDFLLGYRpsldegkyEPTPGIFLRFCLKAEKNP 298
                        90
                ....*....|.
gi 71994521 386 --PCILFIDEI 394
Cdd:COG1401 299 dkPYVLIIDEI 309
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
327-362 1.90e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.04  E-value: 1.90e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 71994521 327 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF 362
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
330-441 5.71e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.48  E-value: 5.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 330 ILTGPPGTGKTLLAKATA-----GEANvpFITVSGSEFLEMF-----VGVGPARV----RDMFSMA-RKNSPCILFIDEI 394
Cdd:cd19499  45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 71994521 395 DAVgrkrggkggmggHSEQENTLNQL-----LVEMDGFTTDESSVIVIAATN 441
Cdd:cd19499 123 EKA------------HPDVQNLLLQVlddgrLTDSHGRTVDFKNTIIIMTSN 162
AAA_22 pfam13401
AAA domain;
330-397 7.84e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 43.10  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   330 ILTGPPGTGKTLLAK---ATAGEANVPFITV------SGSEFLEMFV------GVGPARVRDMFSM-----ARKNSPCIL 389
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAAlqqllLALAVAVVL 88

                  ....*...
gi 71994521   390 FIDEIDAV 397
Cdd:pfam13401  89 IIDEAQHL 96
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
327-365 8.00e-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: 45.76  E-value: 8.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 71994521   327 KGAILTGPPGTGKTLLAKATAGE--ANVPFITVSGSEF--LEM 365
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVysLEM 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
331-394 8.70e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 8.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521  331 LTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRD---MFSMARKNSpcILFIDEI 394
Cdd:PRK00080  56 LYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAleKPGDlaaILTNLEEGD--VLFIDEI 111
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
330-394 2.87e-04

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: 42.10  E-value: 2.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71994521   330 ILTGPPGTGKTLLAKATAGEANVPFITVSgseflemfvgvGPA--RVRDMFSMARKNSPC-ILFIDEI 394
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITS-----------GPAieRPGDLAAILTNLEPGdVLFIDEI 93
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
304-541 3.70e-04

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 43.02  E-value: 3.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 304 EIMEFVNFLknpQQYKDLGakipkgaILTGPPGTGKTLLAKATAGE-ANVPFITVSGS----EFL-----EMFVGVGPAR 373
Cdd:COG2842  38 RFAEALDEA---RALPGIG-------VVYGESGVGKTTAAREYANRnPNVIYVTASPSwtskELLeelaeELGIPAPPGT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 374 VRDMFSMAR---KNSPCILFIDEIDavgrkrggkggmggHSEQEnTLNQLlveMDGFttDESSV-IVIAATNRVDildsA 449
Cdd:COG2842 108 IADLRDRILerlAGTGRLLIIDEAD--------------HLKPK-ALEEL---RDIH--DETGVgVVLIGMERLP----A 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 450 LLRpgRFDrQIYvpvpdikGRASiFRVHLGPLrtSLDKTvlsRKLAAHTPGFSGAD---------------ISNVCNEAA 514
Cdd:COG2842 164 KLK--RYE-QLY-------SRIG-FWVEFKPL--SLEDV---RALAEAWGELTDPDllellhritrgnlrrLDRTLRLAA 227
                       250       260
                ....*....|....*....|....*..
gi 71994521 515 LIAARDANHEISNKHFEQAIERVVAGM 541
Cdd:COG2842 228 RAAKRNGLTKITLDHVRAAALMLGEGP 254
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
312-354 8.73e-04

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: 41.82  E-value: 8.73e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71994521 312 LKNPQQYKDLGAKIPKGAI-LTGPPGTGKTLLAKATAGEANVPF 354
Cdd:cd19497  35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPF 78
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
324-396 9.77e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 40.31  E-value: 9.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 324 KIPKGAI--LTGPPGTGKTLLAKATAGEANVP--FITVSGSEFLEMFVGVGPARV----------RDMFSMARK--NSPC 387
Cdd:cd00267  21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                ....*....
gi 71994521 388 ILFIDEIDA 396
Cdd:cd00267 101 LLLLDEPTS 109
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
297-463 9.97e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 42.52  E-value: 9.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   297 GCEEAKIEIMEFVNFLKNPQQYKDLGAKIPKGA---ILTGPPGTGKTLLAKATA------GEANVPFIT-VSGSEFLEMF 366
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAkiycglGVLRKPLVReVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   367 VGVGPARVRDMFSMARKNspcILFIDEIDAVgrkrggkggMGGHSEQEN-----TLNQLLVEMDgftTDESSVIVIAATN 441
Cdd:TIGR03922 360 IGESEAKTNEIIDSALGG---VLFLDEAYTL---------VETGYGQKDpfgleAIDTLLARME---NDRDRLVVIGAGY 424
                         170       180
                  ....*....|....*....|....*..
gi 71994521   442 RVDIlDSAL-----LRpGRFDRQIYVP 463
Cdd:TIGR03922 425 RKDL-DKFLevnegLR-SRFTRVIEFP 449
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
331-394 6.60e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 6.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71994521 331 LTGPPGTGKTLLAKATAGEANVPFITVSGseflemfvgvgPA--RVRDMFSM---ARKNSpcILFIDEI 394
Cdd:COG2255  59 LYGPPGLGKTTLAHIIANEMGVNIRITSG-----------PAieKPGDLAAIltnLEEGD--VLFIDEI 114
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
331-357 6.72e-03

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: 39.38  E-value: 6.72e-03
                        10        20
                ....*....|....*....|....*..
gi 71994521 331 LTGPPGTGKTLLAKATAGEANVPFITV 357
Cdd:COG0714  36 LEGVPGVGKTTLAKALARALGLPFIRI 62
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
330-447 6.95e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 37.10  E-value: 6.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521 330 ILTGPPGTGKTLLAKATAGEA---NVPFITVSgseFLEMFVgvgpARVRDMFSMARknsPCILFIDEIDAVGRKRGGKgg 406
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARASQGD-- 69
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71994521 407 mgghsEQENTLNQLLVEMDGFTtdESSVIVIAATNRVDILD 447
Cdd:cd01120  70 -----RSSELLEDLAKLLRAAR--NTGITVIATIHSDKFDI 103
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
322-397 8.60e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.21  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994521   322 GAKIPKGAI----LTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEmfvgvgPARVRDMFSMARKNSpcILFIDEIDAV 397
Cdd:TIGR00635  22 AAKMRQEALdhllLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK------PGDLAAILTNLEEGD--VLFIDEIHRL 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH