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Conserved domains on  [gi|488945221|ref|WP_002856296|]
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MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Campylobacter]

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];
29-620 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 853.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  29 FAIVMIIIFKGFFDGNGSfggalngnevNKNVPYSELKKLIESGQINQVSIGQTTIKAI-SSSHNTVYTAKKVNDPELVS 107
Cdd:COG0465    1 IALLLVLLFNLFSSSSSS----------VKEISYSEFLQLVEAGKVKSVTIQGDRITGTlKDGTKTRFTTYRVNDPELVD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 108 LLDSKNIAYGA--YSETNWFTDILfSWVLPVFIFFGIWMFLASRMQKnMGSSILGIGSSK-KLVNSEKPKVKFSDVAGVE 184
Cdd:COG0465   71 LLEEKGVEVTAkpPEESSWLLSLL-ISLLPILLLIGLWIFFMRRMQG-GGGGAMSFGKSKaKLYDEDKPKVTFDDVAGVD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 185 EAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFE 264
Cdd:COG0465  149 EAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 265 NAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTeSSPVIVLAATNRPEVLDAALLRPGRFDRQ 344
Cdd:COG0465  229 QAKKNAPCIIFIDEIDAVGRQRGA-GLGGGHDEREQTLNQLLVEMDGFEG-NEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 345 VLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEAVERAIAGL 424
Cdd:COG0465  307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGP 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 425 EKKSRRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGlAALGYTLNTPEENKFLMQKHELIAEVDVLLGGRAA 504
Cdd:COG0465  387 ERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAA 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 505 EEVFIGEISTGASNDLERATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERY 582
Cdd:COG0465  466 EELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRdiGQSRNYSEETAREIDEEVRRIIDEAY 545
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 488945221 583 KDVKDTLNTYKGAIETMVAALYEEETIEGNKVREIIKE 620
Cdd:COG0465  546 ERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
29-620 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 853.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  29 FAIVMIIIFKGFFDGNGSfggalngnevNKNVPYSELKKLIESGQINQVSIGQTTIKAI-SSSHNTVYTAKKVNDPELVS 107
Cdd:COG0465    1 IALLLVLLFNLFSSSSSS----------VKEISYSEFLQLVEAGKVKSVTIQGDRITGTlKDGTKTRFTTYRVNDPELVD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 108 LLDSKNIAYGA--YSETNWFTDILfSWVLPVFIFFGIWMFLASRMQKnMGSSILGIGSSK-KLVNSEKPKVKFSDVAGVE 184
Cdd:COG0465   71 LLEEKGVEVTAkpPEESSWLLSLL-ISLLPILLLIGLWIFFMRRMQG-GGGGAMSFGKSKaKLYDEDKPKVTFDDVAGVD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 185 EAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFE 264
Cdd:COG0465  149 EAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 265 NAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTeSSPVIVLAATNRPEVLDAALLRPGRFDRQ 344
Cdd:COG0465  229 QAKKNAPCIIFIDEIDAVGRQRGA-GLGGGHDEREQTLNQLLVEMDGFEG-NEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 345 VLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEAVERAIAGL 424
Cdd:COG0465  307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGP 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 425 EKKSRRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGlAALGYTLNTPEENKFLMQKHELIAEVDVLLGGRAA 504
Cdd:COG0465  387 ERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAA 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 505 EEVFIGEISTGASNDLERATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERY 582
Cdd:COG0465  466 EELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRdiGQSRNYSEETAREIDEEVRRIIDEAY 545
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 488945221 583 KDVKDTLNTYKGAIETMVAALYEEETIEGNKVREIIKE 620
Cdd:COG0465  546 ERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
124-619 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: 727.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  124 WFTDILFSWVLPVFIFFGIWMFLASRMQKnMGSSILGIGSSK-KLVNSEKPKVKFSDVAGVEEAKEEVKEIVDFLKYPER 202
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQG-GGGRAFSFGKSKaKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  203 YIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAI 282
Cdd:TIGR01241  80 FTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  283 GKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTESSpVIVLAATNRPEVLDAALLRPGRFDRQVLVDKPDFKGRCDILKVH 362
Cdd:TIGR01241 160 GRQRGA-GLGGGNDEREQTLNQLLVEMDGFGTNTG-VIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  363 MKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEAVERAIAGLEKKSRRINEKEKKIVTYH 442
Cdd:TIGR01241 238 AKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  443 ECGHALIAETTKGAKRVSKVSVIPRGLaALGYTLNTPEENKFLMQKHELIAEVDVLLGGRAAEEVFIGEISTGASNDLER 522
Cdd:TIGR01241 318 EAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  523 ATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERYKDVKDTLNTYKGAIETMV 600
Cdd:TIGR01241 397 ATNIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLA 476
                         490
                  ....*....|....*....
gi 488945221  601 AALYEEETIEGNKVREIIK 619
Cdd:TIGR01241 477 KALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
20-632 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 532.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  20 KNPIFI-FAIFAIVMIIIFKGFFDGNGSFGGALNGNEVNKNVPYSELK--KLIES---GQINQVSI---GQTTIKAISSS 90
Cdd:CHL00176   6 KYAILIsLPLIVEKFTVWDVFYYSSVEDGLKSPNNPDVVQNKASSRMTygRFLEYldmGWIKKVDLydnGRTAIVEASSP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  91 HNTVYTAKK-----VNDPELVSLLDSKNIAYGAY--SETNWFTDILFSWVLPVFIFFGIWMFL--ASRMQKNMGSSILGI 161
Cdd:CHL00176  86 ELGNRPQRIrvelpVGASELIQKLKEANIDFDAHppVLKSNIVTILSNLLLPLILIGVLWFFFqrSSNFKGGPGQNLMNF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 162 GSSKKLVNSE-KPKVKFSDVAGVEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFF 240
Cdd:CHL00176 166 GKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 241 SVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFgTESSPVI 320
Cdd:CHL00176 246 SISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGA-GIGGGNDEREQTLNQLLTEMDGF-KGNKGVI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 321 VLAATNRPEVLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLA 400
Cdd:CHL00176 324 VIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 401 GRDSKKYVEQNDLVEAVERAIAGLEKKSrRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGlAALGYTLNTPE 480
Cdd:CHL00176 404 ARRKKATITMKEIDTAIDRVIAGLEGTP-LEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRG-QAKGLTWFTPE 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 481 ENKFLMQKHELIAEVDVLLGGRAAEEVFIG--EISTGASNDLERATDIIKAMISMYGMSEIAGLMvLEKQRNTFLSGGQT 558
Cdd:CHL00176 482 EDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMSSIGPIS-LESNNSTDPFLGRF 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221 559 IK---DYSEKMAESLDDYVKKTLDERYKDVKDTLNTYKGAIETMVAALYEEETIEGNKVREIIKEFedqNSLPTRLQ 632
Cdd:CHL00176 561 MQrnsEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSY---TILPPKKT 634
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
175-347 6.70e-108

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: 322.64  E-value: 6.70e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 175 VKFSDVAGVEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGV 254
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 255 GASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTeSSPVIVLAATNRPEVLDAA 334
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGA-GLGGGHDEREQTLNQLLVEMDGFES-NTGVIVIAATNRPDVLDPA 158
                        170
                 ....*....|...
gi 488945221 335 LLRPGRFDRQVLV 347
Cdd:cd19501  159 LLRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
429-617 1.11e-72

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 232.11  E-value: 1.11e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  429 RRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGLAaLGYTLNTPEENKFLMQKHELIAEVDVLLGGRAAEEVF 508
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  509 IGEISTGASNDLERATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERYKDVK 586
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 488945221  587 DTLNTYKGAIETMVAALYEEETIEGNKVREI 617
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
211-351 3.13e-18

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: 82.04  E-value: 3.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221   211 PKGLLLVGPPGTGKTLLAKAVAGEADVP---FFSVSGSSFIE--------------MFVGVGASRVRDLFENAKKEAPAI 273
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488945221   274 VFIDEIDAIGKSRAASGMMGGNDEREQTLNQllaemdgfgtESSPVIVLAATNRPEVLDAALLRPgRFDRQVLVDKPD 351
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLLLK----------SEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
214-243 6.72e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.61  E-value: 6.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEA-----DVPFFSVS 243
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTAA 127
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
29-620 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 853.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  29 FAIVMIIIFKGFFDGNGSfggalngnevNKNVPYSELKKLIESGQINQVSIGQTTIKAI-SSSHNTVYTAKKVNDPELVS 107
Cdd:COG0465    1 IALLLVLLFNLFSSSSSS----------VKEISYSEFLQLVEAGKVKSVTIQGDRITGTlKDGTKTRFTTYRVNDPELVD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 108 LLDSKNIAYGA--YSETNWFTDILfSWVLPVFIFFGIWMFLASRMQKnMGSSILGIGSSK-KLVNSEKPKVKFSDVAGVE 184
Cdd:COG0465   71 LLEEKGVEVTAkpPEESSWLLSLL-ISLLPILLLIGLWIFFMRRMQG-GGGGAMSFGKSKaKLYDEDKPKVTFDDVAGVD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 185 EAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFE 264
Cdd:COG0465  149 EAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 265 NAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTeSSPVIVLAATNRPEVLDAALLRPGRFDRQ 344
Cdd:COG0465  229 QAKKNAPCIIFIDEIDAVGRQRGA-GLGGGHDEREQTLNQLLVEMDGFEG-NEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 345 VLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEAVERAIAGL 424
Cdd:COG0465  307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGP 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 425 EKKSRRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGlAALGYTLNTPEENKFLMQKHELIAEVDVLLGGRAA 504
Cdd:COG0465  387 ERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAA 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 505 EEVFIGEISTGASNDLERATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERY 582
Cdd:COG0465  466 EELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRdiGQSRNYSEETAREIDEEVRRIIDEAY 545
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 488945221 583 KDVKDTLNTYKGAIETMVAALYEEETIEGNKVREIIKE 620
Cdd:COG0465  546 ERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
124-619 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: 727.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  124 WFTDILFSWVLPVFIFFGIWMFLASRMQKnMGSSILGIGSSK-KLVNSEKPKVKFSDVAGVEEAKEEVKEIVDFLKYPER 202
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQG-GGGRAFSFGKSKaKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  203 YIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAI 282
Cdd:TIGR01241  80 FTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  283 GKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTESSpVIVLAATNRPEVLDAALLRPGRFDRQVLVDKPDFKGRCDILKVH 362
Cdd:TIGR01241 160 GRQRGA-GLGGGNDEREQTLNQLLVEMDGFGTNTG-VIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  363 MKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEAVERAIAGLEKKSRRINEKEKKIVTYH 442
Cdd:TIGR01241 238 AKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  443 ECGHALIAETTKGAKRVSKVSVIPRGLaALGYTLNTPEENKFLMQKHELIAEVDVLLGGRAAEEVFIGEISTGASNDLER 522
Cdd:TIGR01241 318 EAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  523 ATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERYKDVKDTLNTYKGAIETMV 600
Cdd:TIGR01241 397 ATNIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLA 476
                         490
                  ....*....|....*....
gi 488945221  601 AALYEEETIEGNKVREIIK 619
Cdd:TIGR01241 477 KALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
20-632 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 532.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  20 KNPIFI-FAIFAIVMIIIFKGFFDGNGSFGGALNGNEVNKNVPYSELK--KLIES---GQINQVSI---GQTTIKAISSS 90
Cdd:CHL00176   6 KYAILIsLPLIVEKFTVWDVFYYSSVEDGLKSPNNPDVVQNKASSRMTygRFLEYldmGWIKKVDLydnGRTAIVEASSP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  91 HNTVYTAKK-----VNDPELVSLLDSKNIAYGAY--SETNWFTDILFSWVLPVFIFFGIWMFL--ASRMQKNMGSSILGI 161
Cdd:CHL00176  86 ELGNRPQRIrvelpVGASELIQKLKEANIDFDAHppVLKSNIVTILSNLLLPLILIGVLWFFFqrSSNFKGGPGQNLMNF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 162 GSSKKLVNSE-KPKVKFSDVAGVEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFF 240
Cdd:CHL00176 166 GKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 241 SVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFgTESSPVI 320
Cdd:CHL00176 246 SISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGA-GIGGGNDEREQTLNQLLTEMDGF-KGNKGVI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 321 VLAATNRPEVLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLA 400
Cdd:CHL00176 324 VIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 401 GRDSKKYVEQNDLVEAVERAIAGLEKKSrRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGlAALGYTLNTPE 480
Cdd:CHL00176 404 ARRKKATITMKEIDTAIDRVIAGLEGTP-LEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRG-QAKGLTWFTPE 481
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 481 ENKFLMQKHELIAEVDVLLGGRAAEEVFIG--EISTGASNDLERATDIIKAMISMYGMSEIAGLMvLEKQRNTFLSGGQT 558
Cdd:CHL00176 482 EDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMSSIGPIS-LESNNSTDPFLGRF 560
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221 559 IK---DYSEKMAESLDDYVKKTLDERYKDVKDTLNTYKGAIETMVAALYEEETIEGNKVREIIKEFedqNSLPTRLQ 632
Cdd:CHL00176 561 MQrnsEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSY---TILPPKKT 634
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
23-622 4.59e-166

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 489.55  E-value: 4.59e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  23 IFIFAIFAIVMIIIFKGF--FDGNGsfggalngnevnKNVPYSELKKLIESGQINQVSIGQTTIKAISSSHNTVYTAKKV 100
Cdd:PRK10733   5 LILWLVIAVVLMSVFQSFgpSESNG------------RKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 101 NDPELVSLLDSKNIAYGAY--SETNWFTDILFSWvLPVFIFFGIWMFLASRMQKNMGSSILGIGSSK-KLVNSEKPKVKF 177
Cdd:PRK10733  73 NDPKLLDNLLTKNVKVVGEppEEPSLLASIFISW-FPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKaRMLTEDQIKTTF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 178 SDVAGVEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGAS 257
Cdd:PRK10733 152 ADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 258 RVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGF-GTESspVIVLAATNRPEVLDAALL 336
Cdd:PRK10733 232 RVRDMFEQAKKAAPCIIFIDEIDAVGRQRGA-GLGGGHDEREQTLNQMLVEMDGFeGNEG--IIVIAATNRPDVLDPALL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 337 RPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEA 416
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 417 VERAIAGLEKKSRRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGlAALGYTLNTPEENKFLMQKHELIAEVD 496
Cdd:PRK10733 389 KDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRG-RALGVTFFLPEGDAISASRQKLESQIS 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 497 VLLGGRAAEEVFIG--EISTGASNDLERATDIIKAMISMYGMSEIAG-LMVLEKQRNTFLsgGQTI---KDYSEKMAESL 570
Cdd:PRK10733 468 TLYGGRLAEEIIYGpeHVSTGASNDIKVATNLARNMVTQWGFSEKLGpLLYAEEEGEVFL--GRSVakaKHMSDETARII 545
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488945221 571 DDYVKKTLDERYKDVKDTLNTYKGAIETMVAALYEEETIEGNKVREIIKEFE 622
Cdd:PRK10733 546 DQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRD 597
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
175-347 6.70e-108

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: 322.64  E-value: 6.70e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 175 VKFSDVAGVEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGV 254
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 255 GASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsGMMGGNDEREQTLNQLLAEMDGFGTeSSPVIVLAATNRPEVLDAA 334
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGA-GLGGGHDEREQTLNQLLVEMDGFES-NTGVIVIAATNRPDVLDPA 158
                        170
                 ....*....|...
gi 488945221 335 LLRPGRFDRQVLV 347
Cdd:cd19501  159 LLRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
171-419 1.91e-104

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 320.03  E-value: 1.91e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 171 EKPKVKFSDVAG-VEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIE 249
Cdd:COG1222   71 ESPDVTFDDIGGlDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 250 MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAASGMMGgndEREQTLNQLLAEMDGFgTESSPVIVLAATNRPE 329
Cdd:COG1222  151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG---EVQRTVNQLLAELDGF-ESRGDVLIIAATNRPD 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 330 VLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVE 409
Cdd:COG1222  227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                        250
                 ....*....|
gi 488945221 410 QNDLVEAVER 419
Cdd:COG1222  307 MEDLEKAIEK 316
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
171-428 7.72e-88

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 279.02  E-value: 7.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 171 EKPKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIE 249
Cdd:PRK03992 124 ESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQ 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 250 MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAASGmMGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPE 329
Cdd:PRK03992 204 KFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSG-TSGDREVQRTLMQLLAEMDGF-DPRGNVKIIAATNRID 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 330 VLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVE 409
Cdd:PRK03992 282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*....
gi 488945221 410 QNDLVEAVERAIAGLEKKS 428
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKDS 380
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
171-419 4.94e-80

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: 257.81  E-value: 4.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  171 EKPKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIE 249
Cdd:TIGR01242 115 ERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  250 MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAASGMmGGNDEREQTLNQLLAEMDGFGTESSpVIVLAATNRPE 329
Cdd:TIGR01242 195 KYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGT-SGDREVQRTLMQLLAELDGFDPRGN-VKVIAATNRPD 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  330 VLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVE 409
Cdd:TIGR01242 273 ILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVT 352
                         250
                  ....*....|
gi 488945221  410 QNDLVEAVER 419
Cdd:TIGR01242 353 MDDFIKAVEK 362
Peptidase_M41 pfam01434
Peptidase family M41;
429-617 1.11e-72

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 232.11  E-value: 1.11e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  429 RRINEKEKKIVTYHECGHALIAETTKGAKRVSKVSVIPRGLAaLGYTLNTPEENKFLMQKHELIAEVDVLLGGRAAEEVF 508
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  509 IGEISTGASNDLERATDIIKAMISMYGMSEIAGLMVLEKQRNTFLSGG--QTIKDYSEKMAESLDDYVKKTLDERYKDVK 586
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 488945221  587 DTLNTYKGAIETMVAALYEEETIEGNKVREI 617
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
193-419 3.04e-72

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: 238.66  E-value: 3.04e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 193 IVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPA 272
Cdd:COG0464  173 VALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPC 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 273 IVFIDEIDAIGKSRAASGmmGGNDEREqtLNQLLAEMDGFgteSSPVIVLAATNRPEVLDAALLRpgRFDRQVLVDKPDF 352
Cdd:COG0464  253 VLFIDEADALAGKRGEVG--DGVGRRV--VNTLLTEMEEL---RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDA 323
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221 353 KGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEAVER 419
Cdd:COG0464  324 EERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALER 390
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
171-438 2.23e-65

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: 228.64  E-value: 2.23e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  171 EKPKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIE 249
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  250 MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAASgmmGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPE 329
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGAR---FDTSVTDRIVNQLLTEMDGI-QELSNVVVIAATNRPD 601
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  330 VLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVE 409
Cdd:TIGR01243 602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPA 681
                         250       260
                  ....*....|....*....|....*....
gi 488945221  410 QNDLVEAVERAIAGLEKKSRRINEKEKKI 438
Cdd:TIGR01243 682 KEKLEVGEEEFLKDLKVEMRHFLEALKKV 710
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
197-345 1.50e-58

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 194.48  E-value: 1.50e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19502   23 LKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEGARLVRELFEMAREKAPSIIFI 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488945221 277 DEIDAIGKSRAASGmMGGNDEREQTLNQLLAEMDGFGTESSpVIVLAATNRPEVLDAALLRPGRFDRQV 345
Cdd:cd19502  103 DEIDAIGAKRFDSG-TGGDREVQRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPALLRPGRFDRKI 169
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
193-347 6.95e-58

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: 192.11  E-value: 6.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 193 IVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPA 272
Cdd:cd19481    8 AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPC 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945221 273 IVFIDEIDAIGKSRAASGMmggNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19481   88 ILFIDEIDAIGRKRDSSGE---SGELRRVLNQLLTELDGV-NSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
177-437 1.16e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 194.72  E-value: 1.16e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 177 FSDVAGVEEAKEEVKEIVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGA 256
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 257 SRVRDLFENAkKEAPAIVFIDEIDAIGKSRAASGMMGgndEREQTLNQLLAEMDGFgteSSPVIVLAATNRPEVLDAALL 336
Cdd:COG1223   81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVG---EVKRVVNALLQELDGL---PSGSVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 337 RpgRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVEA 416
Cdd:COG1223  154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231
                        250       260
                 ....*....|....*....|.
gi 488945221 417 VEraiaglEKKSRRINEKEKK 437
Cdd:COG1223  232 LK------QRKERKKEPKKEG 246
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
153-421 1.88e-55

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 194.99  E-value: 1.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 153 NMGSSILGI--GSSKKLVNSEK----PKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKT 225
Cdd:PTZ00361 152 NKTHSVVGIllDEVDPLVSVMKvdkaPLESYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKT 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 226 LLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAASgMMGGNDEREQTLNQL 305
Cdd:PTZ00361 232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDA-TSGGEKEIQRTMLEL 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 306 LAEMDGFGTeSSPVIVLAATNRPEVLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLA 385
Cdd:PTZ00361 311 LNQLDGFDS-RGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELS 389
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 488945221 386 GADLANIINEAALLAGRDSKKYVEQNDLVEAVERAI 421
Cdd:PTZ00361 390 GADIKAICTEAGLLALRERRMKVTQADFRKAKEKVL 425
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
173-402 8.54e-55

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 199.36  E-value: 8.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  173 PKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMF 251
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  252 VGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsgmMGGNDEReQTLNQLLAEMDGFgTESSPVIVLAATNRPEVL 331
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE---VTGEVEK-RVVAQLLTLMDGL-KGRGRVIVIGATNRPDAL 327
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221  332 DAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGR 402
Cdd:TIGR01243 328 DPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
179-345 1.34e-54

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: 183.65  E-value: 1.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 179 DVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGAS 257
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 258 RVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsgmmgGNDEREQTL-NQLLAEMDGFgTESSPVIVLAATNRPEVLDAALL 336
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE-----DQREVERRVvAQLLTLMDGM-SSRGKVVVIAATNRPDAIDPALR 154

                 ....*....
gi 488945221 337 RPGRFDRQV 345
Cdd:cd19503  155 RPGRFDREV 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
170-421 2.71e-54

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 190.74  E-value: 2.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 170 SEKPKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFI 248
Cdd:PTZ00454 137 SEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFV 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 249 EMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRaASGMMGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRP 328
Cdd:PTZ00454 217 QKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKR-FDAQTGADREVQRILLELLNQMDGF-DQTTNVKVIMATNRA 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 329 EVLDAALLRPGRFDRQVLVDKPDFKGRCDILKVHMKDVKISPKVKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYV 408
Cdd:PTZ00454 295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVI 374
                        250
                 ....*....|...
gi 488945221 409 EQNDLVEAVERAI 421
Cdd:PTZ00454 375 LPKDFEKGYKTVV 387
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
197-347 8.14e-54

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: 181.33  E-value: 8.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19511   13 LKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221 277 DEIDAIGKSRAASgmmGGNDEREQTLNQLLAEMDGFGTESSpVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19511   93 DEIDSLAPRRGQS---DSSGVTDRVVSQLLTELDGIESLKG-VVVIAATNRPDMIDPALLRPGRLDKLIYV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
214-348 9.43e-54

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: 180.10  E-value: 9.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  214 LLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsgmmG 293
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS----G 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488945221  294 GNDEREQTLNQLLAEMDGFGTESSPVIVLAATNRPEVLDAALLrpGRFDRQVLVD 348
Cdd:pfam00004  77 GDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
197-347 9.97e-51

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: 173.07  E-value: 9.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19529   13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221 277 DEIDAIGKSRaasGMMGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19529   93 DEIDSIAPRR---GTTGDSGVTERVVNQLLTELDGL-EEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
197-347 1.44e-48

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: 167.30  E-value: 1.44e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19528   13 VEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221 277 DEIDAIGKSRAASgMMGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19528   93 DELDSIAKARGGN-IGDAGGAADRVINQILTEMDGM-NTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
198-345 2.27e-46

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: 161.42  E-value: 2.27e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 198 KYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFID 277
Cdd:cd19518   21 LPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFID 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488945221 278 EIDAIGKSR-AASGMMggndEReQTLNQLLAEMDGFGTESS---PVIVLAATNRPEVLDAALLRPGRFDRQV 345
Cdd:cd19518  101 EIDAITPKReSAQREM----ER-RIVSQLLTCMDELNNEKTaggPVLVIGATNRPDSLDPALRRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
193-347 4.09e-45

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: 158.03  E-value: 4.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 193 IVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPA 272
Cdd:cd19530   12 ILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945221 273 IVFIDEIDAIGKSRAASGMMGGnderEQTLNQLLAEMDGfGTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19530   92 VIFFDEVDALVPKRGDGGSWAS----ERVVNQLLTEMDG-LEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
197-345 4.61e-45

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 157.98  E-value: 4.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19519   20 LRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFI 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488945221 277 DEIDAIGKSRAASgmmGGNDEReQTLNQLLAEMDGFgTESSPVIVLAATNRPEVLDAALLRPGRFDRQV 345
Cdd:cd19519  100 DEIDAIAPKREKT---HGEVER-RIVSQLLTLMDGL-KQRAHVIVMAATNRPNSIDPALRRFGRFDREI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
197-347 2.26e-43

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: 2.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYiKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19527   13 LEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221 277 DEIDAIGKSRAASGMMGGNDEReqTLNQLLAEMDGFGTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19527   92 DELDSLAPSRGNSGDSGGVMDR--VVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
197-347 3.51e-38

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: 139.02  E-value: 3.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYiKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:cd19509   19 SLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFI 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488945221 277 DEIDAIGKSRAAsgmmgGNDEREQTL-NQLLAEMDGFGT-ESSPVIVLAATNRPEVLDAALLRpgRFDRQVLV 347
Cdd:cd19509   98 DEIDSLLSERGS-----GEHEASRRVkTEFLVQMDGVLNkPEDRVLVLGATNRPWELDEAFLR--RFEKRIYI 163
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
198-346 3.67e-38

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: 138.72  E-value: 3.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 198 KYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFID 277
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488945221 278 EIDAIGKSRaasgmmgGNDER---EQTLNQLLAEMDgfGTES-SPVIVLAATNRPEVLDAALLRPGRFDRQVL 346
Cdd:cd19526   94 EFDSIAPKR-------GHDSTgvtDRVVNQLLTQLD--GVEGlDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
172-347 1.99e-37

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: 136.92  E-value: 1.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 172 KPKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIklGAKIP-KGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIE 249
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 250 MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsgmmGGNDEREQTLNQLLAEMDGFGTESSPVIVLAATNRPE 329
Cdd:cd19521   79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPW 154
                        170
                 ....*....|....*...
gi 488945221 330 VLDAALLRpgRFDRQVLV 347
Cdd:cd19521  155 QLDSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
197-344 1.10e-32

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: 123.77  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVA-----GEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAP 271
Cdd:cd19517   20 LLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWVGEAERQLRLLFEEAYRMQP 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221 272 AIVFIDEIDAIGKSRAAsgmmggndEREQT----LNQLLAEMDGFGTESSpVIVLAATNRPEVLDAALLRPGRFDRQ 344
Cdd:cd19517  100 SIIFFDEIDGLAPVRSS--------KQEQIhasiVSTLLALMDGLDNRGQ-VVVIGATNRPDALDPALRRPGRFDRE 167
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
168-347 1.05e-30

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: 118.94  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 168 VNSEKPKVKFSDVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKiPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSS 246
Cdd:cd19525   12 IMDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 247 FIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsgmmGGNDEREQTLNQLLAEMDGFGTESSP-VIVLAAT 325
Cdd:cd19525   91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE----GEHESSRRIKTEFLVQLDGATTSSEDrILVVGAT 166
                        170       180
                 ....*....|....*....|..
gi 488945221 326 NRPEVLDAALLRpgRFDRQVLV 347
Cdd:cd19525  167 NRPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
179-347 3.44e-30

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: 116.49  E-value: 3.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 179 DVAGVEEAKEEVKEIVDF-LKYPERYIKLGAKiPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGAS 257
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 258 RVRDLFENAKKEAPAIVFIDEIDAIGKSRAAsgmmGGNDEREQTLNQLLAEMDGFGTESSP-VIVLAATNRPEVLDAALL 336
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLKTEFLIEFDGVQSNGDDrVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 488945221 337 RpgRFDRQVLV 347
Cdd:cd19524  156 R--RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
212-347 5.76e-30

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: 116.24  E-value: 5.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 212 KGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRaasgm 291
Cdd:cd19522   34 KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRR----- 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945221 292 mGGNDEREQTL---NQLLAEMDGFGTESSP------VIVLAATNRPEVLDAALLRpgRFDRQVLV 347
Cdd:cd19522  109 -GTSEEHEASRrvkSELLVQMDGVGGASENddpskmVMVLAATNFPWDIDEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
197-341 1.05e-28

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: 112.52  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 197 LKYPERYIKLG-AKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVF 275
Cdd:cd19520   20 LQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQKLVAAVFSLASKLQPSIIF 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488945221 276 IDEIDAIGKSRA-----ASGMMGgndereqtlNQLLAEMDGFGTE-SSPVIVLAATNRPEVLDAALLR--PGRF 341
Cdd:cd19520  100 IDEIDSFLRQRSstdheATAMMK---------AEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAILRrmPKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
200-345 1.50e-28

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: 112.20  E-value: 1.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 200 PERYIKLGAKIPKGLLLVGPPGTGKTLLAKAV-----AGEADVpffsVSGSSFIEMFVGVGASRVRDLFENAKKEAPA-- 272
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488945221 273 ------IVFIDEIDAIGKSRAASGmmGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPEVLDAALLRPGRFDRQV 345
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGSMA--GSTGVHDTVVNQLLSKIDGV-EQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
201-428 1.85e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 107.41  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 201 ERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEID 280
Cdd:CHL00195 249 KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEID 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 281 aigKSRAASGMMGGNDereqTLNQLLAEMDGFGTE-SSPVIVLAATNRPEVLDAALLRPGRFDRQVLVDKPDFKGRCDIL 359
Cdd:CHL00195 329 ---KAFSNSESKGDSG----TTNRVLATFITWLSEkKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIF 401
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945221 360 KVHMKdvKISP----KVKVEDIARLTAGLAGADLANIINEAALLAgRDSKKYVEQNDLVEAVERAI--AGLEKKS 428
Cdd:CHL00195 402 KIHLQ--KFRPkswkKYDIKKLSKLSNKFSGAEIEQSIIEAMYIA-FYEKREFTTDDILLALKQFIplAQTEKEQ 473
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
211-349 8.00e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 97.99  E-value: 8.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 211 PKGLLLVGPPGTGKTLLAKAVAGEA---DVPFFSVSGSSFIEMFVG---VGASRVRDLFENAKKEAPAIVFIDEIDAIGK 284
Cdd:cd00009   19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945221 285 sraasgmmggndEREQTLNQLLAEMDGFGTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLVDK 349
Cdd:cd00009   99 ------------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
196-343 1.08e-21

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 92.05  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 196 FLKYPERYiklGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVF 275
Cdd:cd19507   19 FSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLW 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488945221 276 IDEIDaigksRAASGMMGGNDerEQTLNQLLAEMDGFGTE-SSPVIVLAATNRPEVLDAALLRPGRFDR 343
Cdd:cd19507   96 IDEIE-----KGFSNADSKGD--SGTSSRVLGTFLTWLQEkKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
193-347 1.68e-19

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: 85.48  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 193 IVDFLKYPERYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSfiemfVGVGASRVRDLFENAKKEapA 272
Cdd:cd19510    5 LKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ--S 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221 273 IVFIDEIDA--IGKSRAASGMMGGNDEREQTLNQLLAEMDGFgTESSPVIVLAATNRPEVLDAALLRPGRFDRQVLV 347
Cdd:cd19510   78 IILLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGV-ASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
208-347 1.85e-18

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: 83.01  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 208 AKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRA 287
Cdd:cd19523   30 LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQD 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221 288 ASGMMGGndeREQTlnQLLAEMDG-FGTESSPVIVLAATNRPEVLDAALLRpgRFDRQVLV 347
Cdd:cd19523  110 DEASPVG---RLQV--ELLAQLDGvLGSGEDGVLVVCTTSKPEEIDESLRR--YFSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
211-351 3.13e-18

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: 82.04  E-value: 3.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221   211 PKGLLLVGPPGTGKTLLAKAVAGEADVP---FFSVSGSSFIE--------------MFVGVGASRVRDLFENAKKEAPAI 273
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488945221   274 VFIDEIDAIGKSRAASGMMGGNDEREQTLNQllaemdgfgtESSPVIVLAATNRPEVLDAALLRPgRFDRQVLVDKPD 351
Cdd:smart00382  82 LILDEITSLLDAEQEALLLLLEELRLLLLLK----------SEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
209-345 2.03e-12

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: 65.24  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 209 KIPKGL----LLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEMFVGvGASRVRDLFENAKKEAPA-IVFIDEIDAIG 283
Cdd:cd19512   16 KKNKGLyrniLFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTSRRGlLLFVDEADAFL 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488945221 284 KSRAASGMmggNDEREQTLNQLLAEMdgfGTESSPVIVLAATNRPEVLDAALlrPGRFDRQV 345
Cdd:cd19512   95 RKRSTEKI---SEDLRAALNAFLYRT---GEQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
210-290 1.11e-11

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: 63.94  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 210 IPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEM-FVGVGA-SRVRDLFEnakkeapAIVFIDEIDAIGKSRA 287
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVE-------GIVFIDEIDKIAKRGG 117

                 ...
gi 488945221 288 ASG 290
Cdd:cd19498  118 SSG 120
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
204-343 3.32e-11

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 62.01  E-value: 3.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 204 IKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFI--------------EMFVGVGASRVRDLFENAKKE 269
Cdd:cd19505    5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAM 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488945221 270 APAIVFIDEIDAIGKSRAASGMMGGNDEREQTLNQLLAEmDGFGTESSPVIVLAATNRPEVLDAALLRPGRFDR 343
Cdd:cd19505   85 SPCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSR-DFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
214-427 1.28e-10

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: 62.88  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEADVPFF----------------SVSGSSFIEMFVGVGAsrvrdLFENakkeapaIVFID 277
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGP-----LFAN-------VLLAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 278 EIDaigksRAasgmmggndeREQTLNQLLAEMD------GFGT--ESSPVIVLAATNRPEV-----LDAALLRpgRFDRQ 344
Cdd:COG0714  102 EIN-----RA----------PPKTQSALLEAMEerqvtiPGGTykLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 345 VLVDKPDFKGRCDILKVHM--KDVKISPKVKVEDIARLTAGLAGADLANIINEAALlagrdskkyveqnDLVEAVeRAIA 422
Cdd:COG0714  165 LYIGYPDAEEEREILRRHTgrHLAEVEPVLSPEELLALQELVRQVHVSEAVLDYIV-------------DLVRAT-REHP 230

                 ....*
gi 488945221 423 GLEKK 427
Cdd:COG0714  231 DLRKG 235
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
213-341 1.40e-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: 56.53  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  213 GLLLVGPPGTGKTLLAKAVAgEA--DVPFFSVSGSSF---------IEMFVGVGASRVRDLFENAKKeaPAIVFIDEIDA 281
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAARE--GEIAVLDEINR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488945221  282 IGKSRAASgmmggndereqtLNQLLAE-----MDGFGTESSP---VIVLAATNRP----EVLDAALLRpgRF 341
Cdd:pfam07728  78 ANPDVLNS------------LLSLLDErrlllPDGGELVKAApdgFRLIATMNPLdrglNELSPALRS--RF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
214-279 1.76e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 1.76e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFiemfvgvGASRVRDLFENAKKEAPA----IVFIDEI 279
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRSAgrrtILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
214-279 4.10e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 59.30  E-value: 4.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEADVPFFSVSGssfiemfVGVGASRVRDLFENAKKEA----PAIVFIDEI 279
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
372-415 3.19e-08

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 49.84  E-value: 3.19e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 488945221  372 VKVEDIARLTAGLAGADLANIINEAALLAGRDSKKYVEQNDLVE 415
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
214-353 4.43e-08

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: 53.60  E-value: 4.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEADV---------------------PFFSVSGSSFIEMFvgvgaSRVRDLFENakKEAPA 272
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDD--KDALV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 273 IVFIDEIDAIGKSRAAsgMMGGNDERE--QTLNQLLAEMDGFGTeSSPVIVLAATNRPEVLDAAllrpgrfdrqvLVDKP 350
Cdd:cd19508  128 FVLIDEVESLAAARSA--SSSGTEPSDaiRVVNAVLTQIDRIKR-YHNNVILLTSNLLEKIDVA-----------FVDRA 193

                 ...
gi 488945221 351 DFK 353
Cdd:cd19508  194 DIK 196
PRK04195 PRK04195
replication factor C large subunit; Provisional
209-282 1.64e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 54.16  E-value: 1.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488945221 209 KIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSF-----IEMFVGvGASRVRDLFENAKKeapaIVFIDEIDAI 282
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIERVAG-EAATSGSLFGARRK----LILLDEVDGI 110
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
202-247 8.50e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.89  E-value: 8.50e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488945221 202 RYIKLGAKIPKGLLLVGPPGTGKTLLAKAVAGE--ADVPFFSVSGSSF 247
Cdd:COG1224   55 KMIKEGKMAGKGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
215-285 1.02e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 50.29  E-value: 1.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488945221 215 LLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEM-FVG--VGASRVRdLFENA----KKEAPAIVFIDEIDAIGKS 285
Cdd:cd19497   54 LLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLK-LLQAAdydvERAQRGIVYIDEIDKIARK 130
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
193-285 2.62e-06

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 48.32  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 193 IVDFLKYPERYIKLGAKIpkgLLLVGPPGTGKTLLAKAVAGEADVPF--FSVSG-SSFIEM------FVGVGASRVRDLF 263
Cdd:cd19500   22 ILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvRDEAEIrghrrtYVGAMPGRIIQAL 98
                         90       100
                 ....*....|....*....|..
gi 488945221 264 ENAKKEAPAIVfIDEIDAIGKS 285
Cdd:cd19500   99 KKAGTNNPVFL-LDEIDKIGSS 119
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
215-284 5.87e-06

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 49.00  E-value: 5.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221 215 LLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEM-FVG--VGASRVRdLFENA----KKEAPAIVFIDEIDAIGK 284
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVGedVENILLK-LLQAAdydvEKAQRGIVYIDEIDKIAR 187
ycf2 CHL00206
Ycf2; Provisional
204-449 1.25e-05

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 48.75  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  204 IKLGAKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIE---------------------------------- 249
Cdd:CHL00206 1623 LRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDnkpkgfliddididdsddiddsddidrdldtell 1702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  250 ---------MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKsraasgmmggNDEREQTLNQLLAEMDGFGTESSP-- 318
Cdd:CHL00206 1703 tmmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNV----------NESNYLSLGLLVNSLSRDCERCSTrn 1772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  319 VIVLAATNRPEVLDAALLRPGRFD-----RQVLVdkPDFKGRCDILkVHMKDVKISPKV-KVEDIARLTAGLAGADLANI 392
Cdd:CHL00206 1773 ILVIASTHIPQKVDPALIAPNKLNtcikiRRLLI--PQQRKHFFTL-SYTRGFHLEKKMfHTNGFGSITMGSNARDLVAL 1849
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488945221  393 INEAALLAGRDSKKYVEQNDLVEAVERAIAGLEKKSRRINEKEkkiVTYHECGHALI 449
Cdd:CHL00206 1850 TNEALSISITQKKSIIDTNTIRSALHRQTWDLRSQVRSVQDHG---ILFYQIGRAVA 1903
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
204-247 1.46e-05

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 47.69  E-value: 1.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488945221  204 IKLGAKIPKGLLLVGPPGTGKTLLAKAVAGE--ADVPFFSVSGSSF 247
Cdd:pfam06068  43 IKEGKIAGRAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
211-420 1.80e-05

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.54  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 211 PKGLLLVGPPGTGKTLLAKAV-------AGEADVPFFSV------SGSSF------IEMFV--------GVGASRVRDLF 263
Cdd:COG1474   51 PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqASTRYrvlsriLEELGsgedipstGLSTDELFDRL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 264 ENA--KKEAPAIVFIDEIDAIGKsraasgmmggnDEREQTLNQLLAEMDGFgtESSPVIVLAATNRPEV---LDAAL--- 335
Cdd:COG1474  131 YEAldERDGVLVVVLDEIDYLVD-----------DEGDDLLYQLLRANEEL--EGARVGVIGISNDLEFlenLDPRVkss 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 336 LRPG-----RFDRQVLVdkpdfkgrcDILKvHMKDVKISPKVKVEDIARLTAGLAGADLAN------IINEAALLAGRDS 404
Cdd:COG1474  198 LGEEeivfpPYDADELR---------DILE-DRAELAFYDGVLSDEVIPLIAALAAQEHGDarkaidLLRVAGEIAEREG 267
                        250
                 ....*....|....*.
gi 488945221 405 KKYVEQNDLVEAVERA 420
Cdd:COG1474  268 SDRVTEEHVREAREKI 283
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
23-121 2.72e-05

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 43.36  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221   23 IFIFAIFAIVMIIIFKGFFdgngsfggaLNGNEVNKNVPYSELKKLIESGQINQVSIGQTTIKAISSSHNTVYTAKKVN- 101
Cdd:pfam06480   1 LLLWLLILLVLLLLFLLFL---------LSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFTt 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 488945221  102 ------------DPELVSLLDSKNIAYGAYSE 121
Cdd:pfam06480  72 yfipslpnvdslLEKLEDALEEKGVKVSVKPP 103
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
205-310 3.11e-05

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: 47.15  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  205 KLGAKIP---KGLLLVGPPGTGKTLLAKAVA------GEADVP-FFSVSGSSFIEMFVGVGASRVRDLFENAkkeAPAIV 274
Cdd:TIGR03922 303 ERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSA---LGGVL 379
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 488945221  275 FIDEIDAIGKSRAASGMMGGNdereQTLNQLLAEMD 310
Cdd:TIGR03922 380 FLDEAYTLVETGYGQKDPFGL----EAIDTLLARME 411
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
211-282 8.81e-05

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: 43.34  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  211 PKG-LLLVGPPGTGKTLLAKAVAGEADV---PFFSVSGSSFIE-----MFVG-----VGASRVRDLFENAKKEAPAIVFI 276
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....*.
gi 488945221  277 DEIDAI 282
Cdd:pfam07724  82 DEIEKA 87
44 PHA02544
clamp loader, small subunit; Provisional
203-287 2.43e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.44  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 203 YIKLGaKIPKGLLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSS----FIEMFVGVGASRVrDLFENAKkeapaIVFIDE 278
Cdd:PHA02544  36 IVKKG-RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSDcridFVRNRLTRFASTV-SLTGGGK-----VIIIDE 108

                 ....*....
gi 488945221 279 IDAIGKSRA 287
Cdd:PHA02544 109 FDRLGLADA 117
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
214-285 4.25e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 4.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSfIEmfvgvgasRVRDL---FENAKKEapAIVFIDEIDAIGKS 285
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPA-LE--------KPGDLaaiLTNLEEG--DVLFIDEIHRLSPV 117
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
214-233 4.85e-04

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: 43.11  E-value: 4.85e-04
                         10        20
                 ....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAG 233
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
215-284 4.95e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 42.73  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 215 LLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSFIEM-FVG--VgasrvrdlfEN---------------AKKeapAIVFI 276
Cdd:COG1219  113 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVGedV---------ENillkllqaadydvekAER---GIIYI 180

                 ....*...
gi 488945221 277 DEIDAIGK 284
Cdd:COG1219  181 DEIDKIAR 188
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
214-337 5.92e-04

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 43.25  E-value: 5.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVA---------GEADVPFF--------SVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFI 276
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdlaeEASLEDLLAEALEKRGGEPEDALERLLRNGRLLLLL 262
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488945221 277 DEIDAIGKSraasgmmggnDEREQTLNQLLAEMDGFgtESSPVIVlaaTNRPEVLDAALLR 337
Cdd:COG5635  263 DGLDEVPDE----------ADRDEVLNQLRRFLERY--PKARVII---TSRPEGYDSSELE 308
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
211-322 8.93e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.56  E-value: 8.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221  211 PKGLLLVGPPGTGKTLLAKAV---AGEADVPFFSVSGSSFIEMFVGVGASRVRDLFENAKKEAPAIVFIDEIDAIGKSRA 287
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEALTREGLLRQLLDELESSLLEAWRAALLEALA 103
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 488945221  288 ASGMMGGnDEREQTLNQLLAEMDGFGTESSP-VIVL 322
Cdd:pfam13191 104 PVPELPG-DLAERLLDLLLRLLDLLARGERPlVLVL 138
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
214-279 1.06e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.18  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488945221  214 LLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSfIEmfvgvgasRVRDL---FENAkkEAPAIVFIDEI 279
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPA-IE--------RPGDLaaiLTNL--EPGDVLFIDEI 93
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
214-280 1.20e-03

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: 40.24  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVA-----GEADvpFFSVSGSSFIEMFVG----------VGASRVRDLFENAKKEAPAIVFIDE 278
Cdd:cd19499   44 FLFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDE 121

                 ..
gi 488945221 279 ID 280
Cdd:cd19499  122 IE 123
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
214-322 1.40e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 39.02  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEA---DVPFFSVSgssfiemFVGVGASRVRDLFENAKkeaPAIVFIDEIDAIgksraasG 290
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS-------FLDTILEAIEDLIEEKK---LDIIIIDSLSSL-------A 63
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488945221 291 MMGGNDEREQTLNQLLAEMDGFGTESSPVIVL 322
Cdd:cd01120   64 RASQGDRSSELLEDLAKLLRAARNTGITVIAT 95
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
214-233 1.42e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.60  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|
gi 488945221  214 LLLVGPPGTGKTLLAKAVAG 233
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
374-457 1.45e-03

Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 41.85  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 374 VEDIARLTAGLAgaDLANIINEAALLAGRDSKKYVEQNDlveaVERAIaglEKKSRRINEKEKKIVTYHECGHALIAetT 453
Cdd:COG1067  435 AEDQEKLSTRFA--EIADLLREADYWARKAGAELITAEH----VEQAL---DAKEYRSNRIEEKIQESILDGTILID--T 503

                 ....
gi 488945221 454 KGAK 457
Cdd:COG1067  504 EGEK 507
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
214-470 1.48e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 40.95  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEA-----DVPFFSVSGSSFIEMFvgVGASRVRDLFENAKK-EAPAIVFIDEIDAI-GKSR 286
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEAlennpGARVVYLTAEEFTNDF--INAIRNNTIEEFKEKyRSVDVLLIDDIQFLaGKEA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 287 AasgmmggndERE--QTLNQLLaemdgfgtESSPVIVLAATNRPEVLDAAL--LRpGRFDRQVLVD--KPDFKGRCDIL- 359
Cdd:COG0593  115 T---------QEEffHTFNALR--------EAGKQIVLTSDRPPKELPGLEerLR-SRLEWGLVVDiqPPDLETRIAILr 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 360 -KVHMKDVKISPKVkVEDIA-RLT---AGLAGAdLANIInEAALLAGRD-SKkyveqnDLVEAVERAIAGLEKKSRRINE 433
Cdd:COG0593  177 kKAADRGLELPDEV-LEYLArRIErnvRELEGA-LNRLD-AYALLTGRPiTL------ELAREVLKDLLRAQKKEITIED 247
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488945221 434 KEKKIVTYHECGHALIaettKGAKRVSKVsVIPRGLA 470
Cdd:COG0593  248 IQKAVAEYFGVSVADL----LSKSRTREI-ARPRQIA 279
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
209-279 1.90e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 41.29  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 209 KIPKGLLLVGPPGTGKT----LLAKAVAGEAD-----VPFF-SVSGSSFIEMFVGVGAS---RVRD-LF----ENAKKE- 269
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpSWSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNp 298
                         90
                 ....*....|.
gi 488945221 270 -APAIVFIDEI 279
Cdd:COG1401  299 dKPYVLIIDEI 309
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
212-235 3.92e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 3.92e-03
                         10        20
                 ....*....|....*....|....
gi 488945221 212 KGLLLVGPPGTGKTLLAKAVAGEA 235
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEA 123
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
209-232 4.81e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 39.57  E-value: 4.81e-03
                         10        20
                 ....*....|....*....|....
gi 488945221 209 KIPKGLLLVGPPGTGKTLLAKAVA 232
Cdd:COG0470   16 RLPHALLLHGPPGIGKTTLALALA 39
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
215-290 5.49e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.82  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488945221 215 LLVGPPGTGKTLLAKAVAG---EADVP-------FFSVSGSSFIE--MFVGVGASRVRDLFENAKKEAPAIVFIDEIDAI 282
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAWrivQGDVPevmadctIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                 ....*...
gi 488945221 283 GKSRAASG 290
Cdd:PRK11034 291 IGAGAASG 298
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
212-232 6.33e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 39.62  E-value: 6.33e-03
                         10        20
                 ....*....|....*....|...
gi 488945221 212 KG--LLLVGPPGTGKTLLAKAVA 232
Cdd:COG0466  351 KGpiLCLVGPPGVGKTSLGKSIA 373
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
214-279 6.54e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 6.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEADVPFFSVSGSSfIEmfvgvgasRVRDLfenakkeapA----------IVFIDEI 279
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPA-IE--------KPGDL---------AailtnleegdVLFIDEI 114
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
214-243 6.72e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.61  E-value: 6.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 488945221 214 LLLVGPPGTGKTLLAKAVAGEA-----DVPFFSVS 243
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTAA 127
 
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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