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Conserved domains on  [gi|489534406|ref|WP_003439135|]
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ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein [Clostridioides difficile]

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

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
35-463 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 660.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  35 TKPKTTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEK 114
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 115 YVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKR---HLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLD 191
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 192 EALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEH 271
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 272 FDKALERVIAGLESKNSALVEKEKKIVAYHEAGHALV------SDivgicPIQKISIVPRGQALGYVLQLPDEDRYIYTK 345
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVaallpgAD-----PVHKVTIIPRGRALGYTMQLPEEDRYLYTK 449
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 346 DELIGKIKILLAGKASEELIFNHKSTGAKDDLKKVTEIANQMVCEYGMS-NLGFMTI-DGNDKTFLCD------------ 411
Cdd:COG0465  450 EELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSeKLGPVAYgESEGEVFLGRdigqsrnyseet 529
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489534406 412 --KVQKEANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLIGK 463
Cdd:COG0465  530 arEIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
35-463 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 660.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  35 TKPKTTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEK 114
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 115 YVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKR---HLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLD 191
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 192 EALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEH 271
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 272 FDKALERVIAGLESKNSALVEKEKKIVAYHEAGHALV------SDivgicPIQKISIVPRGQALGYVLQLPDEDRYIYTK 345
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVaallpgAD-----PVHKVTIIPRGRALGYTMQLPEEDRYLYTK 449
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 346 DELIGKIKILLAGKASEELIFNHKSTGAKDDLKKVTEIANQMVCEYGMS-NLGFMTI-DGNDKTFLCD------------ 411
Cdd:COG0465  450 EELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSeKLGPVAYgESEGEVFLGRdigqsrnyseet 529
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489534406 412 --KVQKEANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLIGK 463
Cdd:COG0465  530 arEIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
36-462 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: 591.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   36 KPKTTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKY 115
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  116 VGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHL---ESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDE 192
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglgGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  193 ALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHF 272
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  273 DKALERVIAGLESKNSALVEKEKKIVAYHEAGHALVSDIV-GICPIQKISIVPRGQALGYVLQLPDEDRYIYTKDELIGK 351
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLkDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  352 IKILLAGKASEELIFNHKSTGAKDDLKKVTEIANQMVCEYGMSN-LGFMTID------------GNDKTF---LCDKVQK 415
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDkLGPVAYGsdggdvflgrgfAKAKEYseeTAREIDE 448
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 489534406  416 EANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLIG 462
Cdd:TIGR01241 449 EVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
35-461 4.23e-164

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 477.62  E-value: 4.23e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  35 TKPKT--TFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFV 112
Cdd:CHL00176 174 MEADTgiTFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFV 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 113 EKYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLE---SNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDL 189
Cdd:CHL00176 254 EMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDI 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 190 LDEALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITS 269
Cdd:CHL00176 334 LDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITM 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 270 EHFDKALERVIAGLESknSALVE-KEKKIVAYHEAGHALVSDIVGIC-PIQKISIVPRGQALGYVLQLPDEDRYIYTKDE 347
Cdd:CHL00176 414 KEIDTAIDRVIAGLEG--TPLEDsKNKRLIAYHEVGHAIVGTLLPNHdPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQ 491
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 348 LIGKIKILLAGKASEELIFNHKS--TGAKDDLKKVTEIANQMVCEYGMSNLGFMTIDGNDKTF----------------L 409
Cdd:CHL00176 492 ILARIVGALGGRAAEEVVFGSTEvtTGASNDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDpflgrfmqrnseyseeI 571
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489534406 410 CDKVQKEANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLI 461
Cdd:CHL00176 572 ADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIV 623
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
39-206 1.47e-104

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: 308.39  E-value: 1.47e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  39 TTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGV 118
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 119 GAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRH---LESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALL 195
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGaglGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489534406 196 RPGRFDRHIHI 206
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
292-460 9.07e-63

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 202.06  E-value: 9.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  292 EKEKKIVAYHEAGHALVSDIV-GICPIQKISIVPRGQALGYVLQLPDEDRYIYTKDELIGKIKILLAGKASEELIFNHKS 370
Cdd:pfam01434   5 EEEKKIVAYHEAGHALVGLLLpGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIFGEVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  371 TGAKDDLKKVTEIANQMVCEYGMSN-LGFMTIDGNDKTFLC---------------DKVQKEANRIVEICYKETLEMLKD 434
Cdd:pfam01434  85 TGASNDLEKATKIARQMVTEFGMSDkLGPVSLEESDGNVFLgrgmgkrkpyseetaDIIDEEVKRLLEEAYERAKEILTE 164
                         170       180
                  ....*....|....*....|....*.
gi 489534406  435 NLEDLHSVSKFLFEKETMTHEELKDL 460
Cdd:pfam01434 165 HRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
75-210 7.41e-22

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: 91.67  E-value: 7.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406    75 PKGVLFYGPPGTGKTLLASAVAGE---TNSSFFNVTGSEFVE--------------KYVGVGAKRVRTLFEKARKEAPSI 137
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489534406   138 IFIDEIDavgakRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPgRFDRHIHIGAPN 210
Cdd:smart00382  82 LILDEIT-----SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
35-463 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 660.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  35 TKPKTTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEK 114
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 115 YVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKR---HLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLD 191
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgagLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 192 EALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEH 271
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 272 FDKALERVIAGLESKNSALVEKEKKIVAYHEAGHALV------SDivgicPIQKISIVPRGQALGYVLQLPDEDRYIYTK 345
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVaallpgAD-----PVHKVTIIPRGRALGYTMQLPEEDRYLYTK 449
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 346 DELIGKIKILLAGKASEELIFNHKSTGAKDDLKKVTEIANQMVCEYGMS-NLGFMTI-DGNDKTFLCD------------ 411
Cdd:COG0465  450 EELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSeKLGPVAYgESEGEVFLGRdigqsrnyseet 529
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489534406 412 --KVQKEANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLIGK 463
Cdd:COG0465  530 arEIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
36-462 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: 591.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   36 KPKTTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKY 115
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  116 VGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHL---ESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDE 192
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglgGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  193 ALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHF 272
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  273 DKALERVIAGLESKNSALVEKEKKIVAYHEAGHALVSDIV-GICPIQKISIVPRGQALGYVLQLPDEDRYIYTKDELIGK 351
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLkDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  352 IKILLAGKASEELIFNHKSTGAKDDLKKVTEIANQMVCEYGMSN-LGFMTID------------GNDKTF---LCDKVQK 415
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDkLGPVAYGsdggdvflgrgfAKAKEYseeTAREIDE 448
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 489534406  416 EANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLIG 462
Cdd:TIGR01241 449 EVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
35-461 4.23e-164

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 477.62  E-value: 4.23e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  35 TKPKT--TFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFV 112
Cdd:CHL00176 174 MEADTgiTFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFV 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 113 EKYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLE---SNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDL 189
Cdd:CHL00176 254 EMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDI 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 190 LDEALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITS 269
Cdd:CHL00176 334 LDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITM 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 270 EHFDKALERVIAGLESknSALVE-KEKKIVAYHEAGHALVSDIVGIC-PIQKISIVPRGQALGYVLQLPDEDRYIYTKDE 347
Cdd:CHL00176 414 KEIDTAIDRVIAGLEG--TPLEDsKNKRLIAYHEVGHAIVGTLLPNHdPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQ 491
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 348 LIGKIKILLAGKASEELIFNHKS--TGAKDDLKKVTEIANQMVCEYGMSNLGFMTIDGNDKTF----------------L 409
Cdd:CHL00176 492 ILARIVGALGGRAAEEVVFGSTEvtTGASNDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDpflgrfmqrnseyseeI 571
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489534406 410 CDKVQKEANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLI 461
Cdd:CHL00176 572 ADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIV 623
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
38-466 3.36e-139

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 414.05  E-value: 3.36e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  38 KTTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVG 117
Cdd:PRK10733 148 KTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 118 VGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHL---ESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEAL 194
Cdd:PRK10733 228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPAL 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 195 LRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHFDK 274
Cdd:PRK10733 308 LRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEK 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 275 ALERVIAGLESKNSALVEKEKKIVAYHEAGHALVSDIVGIC-PIQKISIVPRGQALGYVLQLPDEDRYIYTKDELIGKIK 353
Cdd:PRK10733 388 AKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHdPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQIS 467
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 354 ILLAGKASEELIF--NHKSTGAKDDLKKVTEIANQMVCEYGMSN-LG-FMTIDGNDKTFLCDKVQK-------------- 415
Cdd:PRK10733 468 TLYGGRLAEEIIYgpEHVSTGASNDIKVATNLARNMVTQWGFSEkLGpLLYAEEEGEVFLGRSVAKakhmsdetariidq 547
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489534406 416 EANRIVEICYKETLEMLKDNLEDLHSVSKFLFEKETMTHEELKDLIGKEAV 466
Cdd:PRK10733 548 EVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDV 598
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
36-279 1.33e-121

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 357.78  E-value: 1.33e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  36 KPKTTFRDVAGLDEVKEELFE-IVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEK 114
Cdd:COG1222   72 SPDVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 115 YVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKR-HLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEA 193
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 194 LLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHFD 273
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLE 311

                 ....*.
gi 489534406 274 KALERV 279
Cdd:COG1222  312 KAIEKV 317
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
36-292 2.21e-109

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 328.72  E-value: 2.21e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  36 KPKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEK 114
Cdd:PRK03992 125 SPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 115 YVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRhLESNN----EKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLL 190
Cdd:PRK03992 205 FIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR-TDSGTsgdrEVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 191 DEALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSE 270
Cdd:PRK03992 284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTME 363
                        250       260
                 ....*....|....*....|..
gi 489534406 271 HFDKALERVIAGLESKNSALVE 292
Cdd:PRK03992 364 DFLKAIEKVMGKEEKDSMEEPG 385
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
39-206 1.47e-104

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: 308.39  E-value: 1.47e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  39 TTFRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGV 118
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 119 GAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRH---LESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALL 195
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGaglGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489534406 196 RPGRFDRHIHI 206
Cdd:cd19501  161 RPGRFDRQVYV 171
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
36-280 4.38e-93

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: 286.31  E-value: 4.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   36 KPKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEK 114
Cdd:TIGR01242 116 RPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRK 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  115 YVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLES---NNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLD 191
Cdd:TIGR01242 196 YIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGtsgDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILD 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  192 EALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEH 271
Cdd:TIGR01242 276 PALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDD 355

                  ....*....
gi 489534406  272 FDKALERVI 280
Cdd:TIGR01242 356 FIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
41-279 6.36e-88

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: 274.10  E-value: 6.36e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  41 FRDVAGLDEVKEELFEIVD-FMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVG 119
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 120 AKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNkdSNVLIIGATNRLDLLDEALLRpgR 199
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR--SDVVVIAATNRPDLLDPALLR--R 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 200 FDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHFDKALERV 279
Cdd:COG0464  312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
22-297 6.50e-77

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: 254.83  E-value: 6.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   22 KMERDNQTDDSLSTKPKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETN 100
Cdd:TIGR01243 433 KMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  101 SSFFNVTGSEFVEKYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHL-ESNNEKDQTLNQLLVEMDGFNKDSNVL 179
Cdd:TIGR01243 513 ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGArFDTSVTDRIVNQLLTEMDGIQELSNVV 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  180 IIGATNRLDLLDEALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFA 259
Cdd:TIGR01243 593 VIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAA 672
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 489534406  260 VRDDSECITSEHFDKALERVIAGLESKNSALVEKEKKI 297
Cdd:TIGR01243 673 LRESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKV 710
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
40-206 6.97e-75

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: 232.61  E-value: 6.97e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  40 TFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGV 118
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 119 GAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLES---NNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALL 195
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGtggDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 489534406 196 RPGRFDRHIHI 206
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
37-261 1.96e-70

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: 237.50  E-value: 1.96e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   37 PKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKY 115
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  116 VGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALL 195
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALR 332
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534406  196 RPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVR 261
Cdd:TIGR01243 333 RPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
32-280 8.39e-68

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 221.95  E-value: 8.39e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  32 SLSTKPKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSE 110
Cdd:PTZ00454 135 QMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 111 FVEKYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRH---LESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRL 187
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFdaqTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRA 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 188 DLLDEALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECI 267
Cdd:PTZ00454 295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVI 374
                        250
                 ....*....|...
gi 489534406 268 TSEHFDKALERVI 280
Cdd:PTZ00454 375 LPKDFEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
37-280 3.82e-66

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 218.87  E-value: 3.82e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  37 PKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKY 115
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 116 VGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRH-LESNNEKD--QTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDE 192
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYdATSGGEKEiqRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 193 ALLRPGRFDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHF 272
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                 ....*...
gi 489534406 273 DKALERVI 280
Cdd:PTZ00361 418 RKAKEKVL 425
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
50-206 8.37e-65

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: 205.98  E-value: 8.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  50 VKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFEK 129
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489534406 130 ARKEAPSIIFIDEIDAVGAKRHLESNNEK-DQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGElRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
50-206 8.47e-64

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: 203.28  E-value: 8.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  50 VKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFE 128
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489534406 129 KARKEAPSIIFIDEIDAVGAKRHLE-SNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
Peptidase_M41 pfam01434
Peptidase family M41;
292-460 9.07e-63

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 202.06  E-value: 9.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  292 EKEKKIVAYHEAGHALVSDIV-GICPIQKISIVPRGQALGYVLQLPDEDRYIYTKDELIGKIKILLAGKASEELIFNHKS 370
Cdd:pfam01434   5 EEEKKIVAYHEAGHALVGLLLpGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIFGEVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  371 TGAKDDLKKVTEIANQMVCEYGMSN-LGFMTIDGNDKTFLC---------------DKVQKEANRIVEICYKETLEMLKD 434
Cdd:pfam01434  85 TGASNDLEKATKIARQMVTEFGMSDkLGPVSLEESDGNVFLgrgmgkrkpyseetaDIIDEEVKRLLEEAYERAKEILTE 164
                         170       180
                  ....*....|....*....|....*.
gi 489534406  435 NLEDLHSVSKFLFEKETMTHEELKDL 460
Cdd:pfam01434 165 HRDELEALAEALLEKETLDAEEIREL 190
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
43-206 3.44e-62

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: 199.44  E-value: 3.44e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAK 121
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 122 RVRTLFEKARKEAPSIIFIDEIDAVGAKRHlESNNEKDQTL-NQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRF 200
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKRE-EDQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRF 159

                 ....*.
gi 489534406 201 DRHIHI 206
Cdd:cd19503  160 DREVEI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
41-278 4.33e-61

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 199.34  E-value: 4.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  41 FRDVAGLDEVKEELFEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGA 120
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 121 KRVRTLFEKARkEAPSIIFIDEIDAVGAKR-HLESNNEKDQTLNQLLVEMDGFNkdSNVLIIGATNRLDLLDEALLRpgR 199
Cdd:COG1223   81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRgDQNDVGEVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR--R 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489534406 200 FDRHIHIGAPNYHTRFEILKVHTDDKPIDKSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHFDKALER 278
Cdd:COG1223  156 FDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQ 234
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
50-206 1.82e-59

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: 192.33  E-value: 1.82e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  50 VKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFE 128
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489534406 129 KARKEAPSIIFIDEIDAVGAKRHLES-NNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGdSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 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 ...
43-207 1.87e-56

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: 184.56  E-value: 1.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAK 121
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 122 RVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFD 201
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 489534406 202 RHIHIG 207
Cdd:cd19519  161 REIDIG 166
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
78-207 7.11e-56

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: 181.64  E-value: 7.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   78 VLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNE 157
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489534406  158 KDQTLNQLLVEMDGF-NKDSNVLIIGATNRLDLLDEALLrpGRFDRHIHIG 207
Cdd:pfam00004  81 SRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
50-206 3.30e-54

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: 178.47  E-value: 3.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  50 VKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFE 128
Cdd:cd19528    1 VKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 129 KARKEAPSIIFIDEIDAVGAKR---HLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIH 205
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARggnIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 489534406 206 I 206
Cdd:cd19528  161 I 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
47-206 4.86e-54

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: 178.07  E-value: 4.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  47 LDEVKEEL-FEIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRT 125
Cdd:cd19530    1 LDHVREELtMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 126 LFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIH 205
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                 .
gi 489534406 206 I 206
Cdd:cd19530  161 V 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
44-206 8.01e-51

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: 169.84  E-value: 8.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  44 VAGLDEVKEELFEIVDF-MKSPQKYqKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKR 122
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 123 VRTLFEKARKEAPSIIFIDEIDAVGAKRHlESNNEKDQTL-NQLLVEMDGFNKDSN--VLIIGATNRLDLLDEALLRpgR 199
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERG-SGEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR--R 156

                 ....*..
gi 489534406 200 FDRHIHI 206
Cdd:cd19509  157 FEKRIYI 163
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
50-204 7.59e-49

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: 164.52  E-value: 7.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  50 VKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFE 128
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534406 129 KARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHI 204
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
43-204 2.62e-48

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: 163.34  E-value: 2.62e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDFMKSPQK-YQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAK 121
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 122 RVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSN----VLIIGATNRLDLLDEALLRP 197
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPALRRA 160

                 ....*..
gi 489534406 198 GRFDRHI 204
Cdd:cd19518  161 GRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
56-206 1.93e-44

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: 153.05  E-value: 1.93e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  56 EIVDFMKSPQKYQKM---GAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKRVRTLFEKARK 132
Cdd:cd19527    4 EILDTIQLPLEHPELfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489534406 133 EAPSIIFIDEIDAVGAKR--HLESNNEKDQTLNQLLVEMDGFNK-DSNVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19527   84 AKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSSsGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
36-206 3.53e-44

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: 152.71  E-value: 3.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  36 KPKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQkmGAKIP-KGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVE 113
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 114 KYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSN-VLIIGATNRLDLLDE 192
Cdd:cd19521   79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQgVLVLGATNIPWQLDS 158
                        170
                 ....*....|....
gi 489534406 193 ALLRpgRFDRHIHI 206
Cdd:cd19521  159 AIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
43-202 5.01e-43

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: 149.58  E-value: 5.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNS-----SFFNVTGSEFVEKYV 116
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 117 GVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLR 196
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*.
gi 489534406 197 PGRFDR 202
Cdd:cd19517  161 PGRFDR 166
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
43-206 5.58e-41

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: 143.84  E-value: 5.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKiPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAK 121
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 122 RVRTLFEKARKEAPSIIFIDEIDAVGAKRHlESNNEKDQTL-NQLLVEMDGF--NKDSNVLIIGATNRLDLLDEALLRpg 198
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERS-EGEHEASRRLkTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR-- 156

                 ....*...
gi 489534406 199 RFDRHIHI 206
Cdd:cd19524  157 RFTKRVYV 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
33-206 3.33e-39

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: 140.12  E-value: 3.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  33 LSTKPKTTFRDVAGLDEVKEELFEIVDF-MKSPQKYQKMGAKiPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEF 111
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 112 VEKYVGVGAKRVRTLFEKARKEAPSIIFIDEIDAVGAKRHlESNNEKDQTL-NQLLVEMDGFN--KDSNVLIIGATNRLD 188
Cdd:cd19525   92 TSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRG-EGEHESSRRIkTEFLVQLDGATtsSEDRILVVGATNRPQ 170
                        170
                 ....*....|....*...
gi 489534406 189 LLDEALLRpgRFDRHIHI 206
Cdd:cd19525  171 EIDEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
43-206 1.49e-37

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: 135.11  E-value: 1.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDF-MKSPQKYQkmGAKIP-KGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGA 120
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 121 KRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTL-NQLLVEMDGF-----NKDSN--VLIIGATNRLDLLDE 192
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVkSELLVQMDGVggaseNDDPSkmVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 489534406 193 ALLRpgRFDRHIHI 206
Cdd:cd19522  159 ALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
43-200 3.16e-37

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: 134.09  E-value: 3.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELFEIVDF-MKSPQKYQKMG-AKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGA 120
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 121 KRVRTLFEKARKEAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSN--VLIIGATNRLDLLDEALLR-- 196
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAILRrm 160

                 ....
gi 489534406 197 PGRF 200
Cdd:cd19520  161 PKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
64-206 7.15e-35

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: 127.99  E-value: 7.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  64 PQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFN-VTGSEFVEKYVGVGAKRVRTLFEKARKEAPS------ 136
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESEANIRKLFADAEEEQRRlgansg 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489534406 137 --IIFIDEIDAVGAKRHLESNNE--KDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19504  104 lhIIIFDEIDAICKQRGSMAGSTgvHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
45-207 2.22e-27

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: 106.85  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  45 AGLDEVKEELFEIVDfmkspqkyqkmgAKIPKGVLFYGPPGTGKTLLASAVAGET---NSSFFNVTGSEFVEKYVG---V 118
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 119 GAKRVRTLFEKARKEAPSIIFIDEIDAVGAKrhlesnnEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPG 198
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYD 141

                 ....*....
gi 489534406 199 RFDRHIHIG 207
Cdd:cd00009  142 RLDIRIVIP 150
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
56-206 4.49e-24

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: 97.81  E-value: 4.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  56 EIVDFMKSPQKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEfvekyVGVGAKRVRTLFEKARKEap 135
Cdd:cd19510    4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ-- 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489534406 136 SIIFIDEIDA------VGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19510   77 SIILLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
ycf46 CHL00195
Ycf46; Provisional
37-287 5.50e-22

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 98.55  E-value: 5.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  37 PKTTFRDVAGLDEVKEEL-FEIVDFMKSPQKYqkmGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKY 115
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLkKRSTSFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 116 VGVGAKRVRTLFEKARKEAPSIIFIDEIDavgaKRHLESNNEKDQ-TLNQLLVEMDGF--NKDSNVLIIGATNRLDLLDE 192
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEID----KAFSNSESKGDSgTTNRVLATFITWlsEKKSPVFVVATANNIDLLPL 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 193 ALLRPGRFDRHIHIGAPNYHTRFEILKVHTDD-KPID-KSVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSEcITSE 270
Cdd:CHL00195 376 EILRKGRFDEIFFLDLPSLEEREKIFKIHLQKfRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKRE-FTTD 454
                        250
                 ....*....|....*....
gi 489534406 271 HFDKALERVI--AGLESKN 287
Cdd:CHL00195 455 DILLALKQFIplAQTEKEQ 473
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
75-210 7.41e-22

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: 91.67  E-value: 7.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406    75 PKGVLFYGPPGTGKTLLASAVAGE---TNSSFFNVTGSEFVE--------------KYVGVGAKRVRTLFEKARKEAPSI 137
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489534406   138 IFIDEIDavgakRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEALLRPgRFDRHIHIGAPN 210
Cdd:smart00382  82 LILDEIT-----SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
43-206 8.61e-22

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: 91.87  E-value: 8.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEELF-EIVDFMKSPQKYQKMgAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAK 121
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 122 RVRTLFEKARKEAPSIIFIDEIDAVGAKRhLESNNEKDQTLNQLLVEMDGF--NKDSNVLIIGATNRLDLLDEALLRpgR 199
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR--Y 156

                 ....*..
gi 489534406 200 FDRHIHI 206
Cdd:cd19523  157 FSKRLLV 163
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
43-202 5.19e-20

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: 86.65  E-value: 5.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  43 DVAGLDEVKEEL-FEIVDFMKSPQKYqkmGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAK 121
Cdd:cd19507    1 DVGGLDNLKDWLkKRKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 122 RVRTLFEKARKEAPSIIFIDEIDAV--GAKRHLESNNEKdQTLNQLLVEMDgfNKDSNVLIIGATNRLDLLDEALLRPGR 199
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEKGfsNADSKGDSGTSS-RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGR 154

                 ...
gi 489534406 200 FDR 202
Cdd:cd19507  155 FDE 157
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
46-204 2.52e-11

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: 65.64  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   46 GLDEVKEELFEIVDFMKSPQKYQKMGAKIP---KGVLFYGPPGTGKTLLASAVA----GET---NSSFFNVTGSEFVEKY 115
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiycGLGvlrKPLVREVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  116 VGVGAKRVRTLFEKArkeAPSIIFIDEIDAVGAKRHLESNNEKDQTLNQLLVEMDGFNKDSNVLIIGATNRLD-LLD-EA 193
Cdd:TIGR03922 360 IGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARMENDRDRLVVIGAGYRKDLDkFLEvNE 436
                         170
                  ....*....|.
gi 489534406  194 LLRpGRFDRHI 204
Cdd:TIGR03922 437 GLR-SRFTRVI 446
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
78-143 7.22e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.92  E-value: 7.22e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  78 VLFYGPPGTGKTLLASAVAGETNSSFFNVTGsefvekyVGVGAKRVRTLFEKARKEA----PSIIFIDEI 143
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
78-184 9.41e-11

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.57  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  78 VLFYGPPGTGKTLLASAVAGETNSSF--FNVTGSefvekyvgvGAKRVRTLFEKARKEAPS----IIFIDEIdavgakrH 151
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFeaLSAVTS---------GVKDLREVIEEARQRRSAgrrtILFIDEI-------H 102
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489534406 152 LESnneKDQtlnQ--LL--VEmDGfnkdsNVLIIGAT 184
Cdd:PRK13342 103 RFN---KAQ---QdaLLphVE-DG-----TITLIGAT 127
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
230-274 1.32e-10

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: 56.39  E-value: 1.32e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 489534406  230 SVNLELLAKKTHGFNGAHLSNIANEAAIFAVRDDSECITSEHFDK 274
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK04195 PRK04195
replication factor C large subunit; Provisional
37-144 4.11e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 61.86  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  37 PKTtFRDVAGLDEVKEELFEIVDfmkspqKYQKmgAKIPKGVLFYGPPGTGKTLLASAVAG-------ETNSSffNVTGS 109
Cdd:PRK04195  10 PKT-LSDVVGNEKAKEQLREWIE------SWLK--GKPKKALLLYGPPGVGKTSLAHALANdygweviELNAS--DQRTA 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489534406 110 EFVEKYVGVGAKRvRTLFEKARKeapsIIFIDEID 144
Cdd:PRK04195  79 DVIERVAGEAATS-GSLFGARRK----LILLDEVD 108
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
76-205 5.47e-10

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: 57.54  E-value: 5.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  76 KGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEfVEKYVGVGAKRVRTLFEKARKEAPS-IIFIDEIDAVGAKRHLES 154
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWANTSRRGlLLFVDEADAFLRKRSTEK 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489534406 155 NNEKDQ-TLNQLLVEMDGFNKDsnVLIIGATNRLDLLDEALlrPGRFDRHIH 205
Cdd:cd19512  102 ISEDLRaALNAFLYRTGEQSNK--FMLVLASNQPEQFDWAI--NDRIDEMVE 149
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
75-206 3.51e-09

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: 55.46  E-value: 3.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  75 PKGVLFYGPPGTGKTLLASAVAGET--------------NSSFFNVTGSEFVEKYVGVGAKRVRTLFEKARKEAPSIIFI 140
Cdd:cd19505   12 SKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPCIIWI 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 141 DEIDAVGAKRHLESNNEKDQTLNQLLVEM--DGFNKDS--NVLIIGATNRLDLLDEALLRPGRFDRHIHI 206
Cdd:cd19505   92 PNIHELNVNRSTQNLEEDPKLLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
77-200 5.63e-09

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: 54.22  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   77 GVLFYGPPGTGKTLLASAVAGET-NSSFFNVTGSEFVEK--------YVGVGAKRVRTLFEKARKEApSIIFIDEIDavg 147
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEedlfgrrnIDPGGASWVDGPLVRAAREG-EIAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534406  148 aKRHLESNNekdqTLNQLLVE-----MDGFN----KDSNVLIIGATNRLDL----LDEALLRpgRF 200
Cdd:pfam07728  77 -RANPDVLN----SLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
78-194 9.99e-09

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 55.15  E-value: 9.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  78 VLFYGPPGTGKTLLASAVAGETN---------SSFFNVTGSEFVEKYVGVGAKRVRTLFEKAR-----KEAPSIIFIDEI 143
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQeliddKDALVFVLIDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489534406 144 DAVGAKRH-LESNNEKD---QTLNQLLVEMDGFNKDSNVLIIGATNRLDLLDEAL 194
Cdd:cd19508  135 ESLAAARSaSSSGTEPSdaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
42-195 3.06e-08

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: 53.33  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  42 RDVAGLDEVKEElfeIVDFMKSPQKYQKMGAKIpkgVLFYGPPGTGKTLLASAVAGETNSSFFNVT-G--SEFVE----- 113
Cdd:cd19500   10 ADHYGLEDVKER---ILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEirghr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 114 -KYVGVGAKRVRTLFEKARKEAPsIIFIDEIDAVGAKRH-------LE------SNNEKDQTLNqllVEMDgfnkDSNVL 179
Cdd:cd19500   84 rTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGSSFRgdpasalLEvldpeqNSTFSDHYLD---VPFD----LSKVL 155
                        170
                 ....*....|....*.
gi 489534406 180 IIGATNRLDLLDEALL 195
Cdd:cd19500  156 FIATANSLDTIPGPLL 171
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
73-200 6.11e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 51.69  E-value: 6.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  73 KIPKGVLFYGPPGTGKT----LLASAVAGETNSSFFNVT------GSEFVEKYVGVGA----KRVRTLF----EKARKE- 133
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVQfhpswsYEDFLLGYRPSLDegkyEPTPGIFlrfcLKAEKNp 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 134 -APSIIFIDEIdavgakrhlesnN---------------EKDQTLNQLLVEMDGFNKD------SNVLIIGATNR----L 187
Cdd:COG1401  299 dKPYVLIIDEI------------NranvekyfgellsllESDKRGEELSIELPYSGEGeefsipPNLYIIGTMNTddrsL 366
                        170
                 ....*....|...
gi 489534406 188 DLLDEALLRpgRF 200
Cdd:COG1401  367 ALSDKALRR--RF 377
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
76-186 6.55e-07

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 49.06  E-value: 6.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  76 KGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVGVGAKR--VRTLFEKARKEAPSIIFIDEIDAVGAKRHLE 153
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489534406 154 SNNEKD-----QTLNQLLVEMDGfnkDSNVLIIGATNR 186
Cdd:cd19506  107 TEKQLDpkrlkKDLPKILKSLKP---EDRVLIVGTTSR 141
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
74-149 9.81e-07

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 48.92  E-value: 9.81e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534406  74 IPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEkyVGVGAKRVRTLFekaRKEAPSIIFIDEIDAVGAK 149
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE--VGYVGRDVESII---RDLVEGIVFIDEIDKIAKR 115
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
79-144 1.41e-06

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: 48.33  E-value: 1.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489534406  79 LFYGPPGTGKTLLASAVAGE---TNSSFFNVTGSEFVEKYVG----------VGAKRVRTLFEKARKEAPSIIFIDEID 144
Cdd:cd19499   45 LFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
19-143 1.98e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.74  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  19 AQTKMERDNQTDDSLstKPKTtFRDVAGLDEVKEELfEIvdFMKSPQKYQKmgakIPKGVLFYGPPGTGKTLLASAVAGE 98
Cdd:PRK00080   5 PETLEEEEDEIERSL--RPKS-LDEFIGQEKVKENL-KI--FIEAAKKRGE----ALDHVLLYGPPGLGKTTLANIIANE 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489534406  99 TNSSFFNVTGSefvekyvgvgakrvrtLFEKARK--------EAPSIIFIDEI 143
Cdd:PRK00080  75 MGVNIRITSGP----------------ALEKPGDlaailtnlEEGDVLFIDEI 111
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
75-144 2.07e-06

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: 47.58  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   75 PKGV-LFYGPPGTGKTLLASAVAGETNSSFFNVT---GSEFVEK------------YVGVGAKRvrTLFEKARKEAPSII 138
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGDERALIridMSEYMEEhsvsrligappgYVGYEEGG--QLTEAVRRKPYSIV 79

                  ....*.
gi 489534406  139 FIDEID 144
Cdd:pfam07724  80 LIDEIE 85
PRK13341 PRK13341
AAA family ATPase;
79-143 2.47e-06

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 50.05  E-value: 2.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  79 LFYGPPGTGKTLLASAVAGETNSSFFNVTGsefvekyVGVGAKRVRTLFEKARKEAP-----SIIFIDEI 143
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERLErhgkrTILFIDEV 118
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
78-222 3.34e-06

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: 48.63  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  78 VLFYGPPGTGKTLLASAVAGETNSSF----FN-------VTGSE-FVEKYvgvGAKRVRT--LFEkarkeapSIIFIDEI 143
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFiriqFTpdllpsdILGTYiYDQQT---GEFEFRPgpLFA-------NVLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 144 DAVGAKrhlesnnekdqTLNQLLVEMDgfnkDSNVLIIGAT-------------NRLDL-----LDEALLRpgRFDRHIH 205
Cdd:COG0714  104 NRAPPK-----------TQSALLEAME----ERQVTIPGGTyklpepflviatqNPIEQegtypLPEAQLD--RFLLKLY 166
                        170
                 ....*....|....*..
gi 489534406 206 IGAPNYHTRFEILKVHT 222
Cdd:COG0714  167 IGYPDAEEEREILRRHT 183
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
69-133 1.23e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.66  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  69 KMGAKipkGVLFYGPPGTGKTLLASAVAGE--TNSSFFNVTGSEF--------------VEKYVGVGAKRVRTLFEKARK 132
Cdd:COG1224   61 KMAGK---GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIysaelkkteflmqaLRKAIGVRVREKRKVYEGVVK 137

                 .
gi 489534406 133 E 133
Cdd:COG1224  138 E 138
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
36-143 3.05e-05

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: 44.03  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   36 KPKTtFRDVAGLDEVKEELfEIvdFMKSpqkyQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGSefveky 115
Cdd:pfam05496   2 RPRT-LDEYIGQEKVKENL-KI--FIEA----AKQRGEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGP------ 67
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489534406  116 vgvgakrvrtLFEKARK--------EAPSIIFIDEI 143
Cdd:pfam05496  68 ----------AIERPGDlaailtnlEPGDVLFIDEI 93
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
79-301 3.10e-05

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 45.57  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  79 LF-YGPPGTGKTLLASAVAGETNSSFFN-----VTGSEFVEKYvgVGAKRVRTLFE-KARKEAPSIIFIDEIDAVGAKrh 151
Cdd:COG0593   37 LFlYGGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDF--INAIRNNTIEEfKEKYRSVDVLLIDDIQFLAGK-- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 152 lesnnEKDQ-----TLNQLLvemdgfnkDSNVLIIGATNR----LDLLDEALLRpgRFDR--HIHIGAPNYHTRFEILKV 220
Cdd:COG0593  113 -----EATQeeffhTFNALR--------EAGKQIVLTSDRppkeLPGLEERLRS--RLEWglVVDIQPPDLETRIAILRK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 221 HTDDK--PIDKSVnLELLAKKTHGfNGAHLsnianEAAI-----FAVRDDSEcITSEHFDKALERVIAGLESKNSalVEK 293
Cdd:COG0593  178 KAADRglELPDEV-LEYLARRIER-NVREL-----EGALnrldaYALLTGRP-ITLELAREVLKDLLRAQKKEIT--IED 247

                 ....*...
gi 489534406 294 EKKIVAYH 301
Cdd:COG0593  248 IQKAVAEY 255
44 PHA02544
clamp loader, small subunit; Provisional
73-219 3.45e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 45.75  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  73 KIPKGVLFYGPPGTGKTLLASAVAGETNSSFFNVTGS----EFVEKYVGVGAKRVrTLFEKarkeaPSIIFIDEIDAVG- 147
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-SLTGG-----GKVIIIDEFDRLGl 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489534406 148 --AKRHLESNNEKDQtlnqllvemdgfnkdSNVLIIGATNRLDLLDEALLrpGRFdRHIHIGAPNYHTRFEILK 219
Cdd:PHA02544 115 adAQRHLRSFMEAYS---------------KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQIEMMK 170
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
40-147 1.03e-04

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: 44.21  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406   40 TFRDVAGLDEVKEELfEIvdFMKSpqkyQKMGAKIPKGVLFYGPPGTGKTLLASAVAGETNSSfFNVTGSEFVEKYVGVG 119
Cdd:TIGR00635   2 LLAEFIGQEKVKEQL-QL--FIEA----AKMRQEALDHLLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEKPGDLA 73
                          90       100
                  ....*....|....*....|....*...
gi 489534406  120 AkrVRTLFEKArkeapSIIFIDEIDAVG 147
Cdd:TIGR00635  74 A--ILTNLEEG-----DVLFIDEIHRLS 94
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
78-193 2.23e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.95  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  78 VLFYGPPGTGKTLLASAVAGETNSSFFNVTGSEFVEKYVgvgAKRVRTLFEKARKeapsIIFIDEIDAVGAKRHLESNNE 157
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL---EAIEDLIEEKKLD----IIIIDSLSSLARASQGDRSSE 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489534406 158 KDQTLNQLLvemdGFNKDSNVLIIgATNRLDLLDEA 193
Cdd:cd01120   74 LLEDLAKLL----RAARNTGITVI-ATIHSDKFDID 104
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
24-103 2.75e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.76  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  24 ERDNQTDDSLstKPKTtFRDVAGLDEVKEELfEIvdFMKSpqkyqkmgAKI----PKGVLFYGPPGTGKTLLASAVAGET 99
Cdd:COG2255   13 EEEDALERSL--RPKR-LDEYIGQEKVKENL-KI--FIEA--------AKKrgeaLDHVLLYGPPGLGKTTLAHIIANEM 78

                 ....
gi 489534406 100 NSSF 103
Cdd:COG2255   79 GVNI 82
rfc PRK00440
replication factor C small subunit; Reviewed
36-145 3.02e-04

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 42.55  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  36 KPKTtFRDVAGLDEVKEELfeivdfmkspQKYQKMGAkIPKgVLFYGPPGTGKTLLASAVA----GET-NSSFFNVTGSE 110
Cdd:PRK00440  12 RPRT-LDEIVGQEEIVERL----------KSYVKEKN-MPH-LLFAGPPGTGKTTAALALArelyGEDwRENFLELNASD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489534406 111 fvEKYVGVGAKRVRtlfEKAR----KEAP-SIIFIDEIDA 145
Cdd:PRK00440  79 --ERGIDVIRNKIK---EFARtapvGGAPfKIIFLDEADN 113
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
56-279 4.89e-04

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 41.86  E-value: 4.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  56 EIVDFMKSPQKYQKMGakipkgvLFYGPPGTGKTLLASAVAGETNSSFF-----NVTGSEFVEK---YVGVGAK--RVRT 125
Cdd:COG2842   38 RFAEALDEARALPGIG-------VVYGESGVGKTTAAREYANRNPNVIYvtaspSWTSKELLEElaeELGIPAPpgTIAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 126 LFEKAR---KEAPSIIFIDEIDavgakrHLesnneKDQTLNQLlveMDGFNK-DSNVLIIGaTNRLDlldeALLRP---- 197
Cdd:COG2842  111 LRDRILerlAGTGRLLIIDEAD------HL-----KPKALEEL---RDIHDEtGVGVVLIG-MERLP----AKLKRyeql 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406 198 -GRFDRHIHIGAPNYhTRFEILKVHTDDKPIDKSvnLELLAKKTHGFNGAhLSNIANEAAIFAVRDDSECITSEHFDKAL 276
Cdd:COG2842  172 ySRIGFWVEFKPLSL-EDVRALAEAWGELTDPDL--LELLHRITRGNLRR-LDRTLRLAARAAKRNGLTKITLDHVRAAA 247

                 ...
gi 489534406 277 ERV 279
Cdd:COG2842  248 LML 250
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
57-111 7.23e-04

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: 41.53  E-value: 7.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489534406   57 IVDFMKSpqkyQKMGAKipkGVLFYGPPGTGKTLLASAVAGETNSS--FFNVTGSEF 111
Cdd:pfam06068  39 IVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEV 88
PRK08116 PRK08116
hypothetical protein; Validated
77-98 8.71e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.16  E-value: 8.71e-04
                         10        20
                 ....*....|....*....|..
gi 489534406  77 GVLFYGPPGTGKTLLASAVAGE 98
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
76-96 1.36e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 1.36e-03
                         10        20
                 ....*....|....*....|.
gi 489534406  76 KGVLFYGPPGTGKTLLASAVA 96
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALG 120
ycf2 CHL00206
Ycf2; Provisional
102-322 1.87e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 41.05  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  102 SFFNVTGSEFVEKyvgVGAKRVRTLFEKARKEAPSIIFIDEIdavgakRHLESNNEKDQTLNQLL--VEMDGFNKDS-NV 178
Cdd:CHL00206 1703 TMMNALTMDMMPK---IDRFYITLQFELAKAMSPCIIWIPNI------HDLNVNESNYLSLGLLVnsLSRDCERCSTrNI 1773
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534406  179 LIIGATNRLDLLDEALLRPGRFDRHIHIGAPNYHTR---FEILK----VHTDDKPIdksvNLELLAKKTHGFNGAHLSNI 251
Cdd:CHL00206 1774 LVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQrkhFFTLSytrgFHLEKKMF----HTNGFGSITMGSNARDLVAL 1849
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489534406  252 ANEAAIFAVRDDSECITSEHFDKALERVIAGLESKNSALVEKEkkiVAYHEAGHALVSD-IVGICPIQKISI 322
Cdd:CHL00206 1850 TNEALSISITQKKSIIDTNTIRSALHRQTWDLRSQVRSVQDHG---ILFYQIGRAVAQNvLLSNCPIDPISI 1918
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
78-97 3.16e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.67  E-value: 3.16e-03
                          10        20
                  ....*....|....*....|
gi 489534406   78 VLFYGPPGTGKTLLASAVAG 97
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
PRK06835 PRK06835
DNA replication protein DnaC; Validated
57-98 4.08e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 39.11  E-value: 4.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489534406  57 IVDFMKspqKYQKMGAKIPKGVLFYGPPGTGKTLLASAVAGE 98
Cdd:PRK06835 168 ILEKCK---NFIENFDKNNENLLFYGNTGTGKTFLSNCIAKE 206
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
78-97 4.43e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 39.25  E-value: 4.43e-03
                         10        20
                 ....*....|....*....|
gi 489534406  78 VLFYGPPGTGKTLLASAVAG 97
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
73-96 7.41e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 38.42  E-value: 7.41e-03
                         10        20
                 ....*....|....*....|....
gi 489534406  73 KIPKGVLFYGPPGTGKTLLASAVA 96
Cdd:COG0470   16 RLPHALLLHGPPGIGKTTLALALA 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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