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Conserved domains on  [gi|66792806|ref|NP_473411|]
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AFG3-like protein 1 [Mus musculus]

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];
149-739 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 770.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 149 VAAGFLYFYFRDPG---KEITWKHFVQYyLARGLVDRLEVVNKQfVRVIPVPGTtSERFVwFNIGSVDTFERNLESAQWE 225
Cdd:COG0465   3 LLLVLLFNLFSSSSssvKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGT-KTRFT-TYRVNDPELVDLLEEKGVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 226 LGIEPTNQAAVVyttesdGSFLRSLVPTLVLVSILLYAMRRGPMGTGRggrgggLFSVGETTAKIL-KNNIDVRFADVAG 304
Cdd:COG0465  79 VTAKPPEESSWL------LSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYdEDKPKVTFDDVAG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 305 CEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDM 384
Cdd:COG0465 147 VDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 385 FAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQ 464
Cdd:COG0465 227 FEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 465 IYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDAlsrkLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERV 544
Cdd:COG0465 307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEV----IARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRV 382
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 545 IGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPRE-QFLYTREQLFDRMCMMLGG 623
Cdd:COG0465 383 IAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGG 462
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 624 RVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLV 697
Cdd:COG0465 463 RAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYG-ESEGEVFLgrdigqSRNYSEETAREIDEEVRRII 541
                       570       580       590       600
                ....*....|....*....|....*....|....*....|..
gi 66792806 698 RSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGP 739
Cdd:COG0465 542 DEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
149-739 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 770.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 149 VAAGFLYFYFRDPG---KEITWKHFVQYyLARGLVDRLEVVNKQfVRVIPVPGTtSERFVwFNIGSVDTFERNLESAQWE 225
Cdd:COG0465   3 LLLVLLFNLFSSSSssvKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGT-KTRFT-TYRVNDPELVDLLEEKGVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 226 LGIEPTNQAAVVyttesdGSFLRSLVPTLVLVSILLYAMRRGPMGTGRggrgggLFSVGETTAKIL-KNNIDVRFADVAG 304
Cdd:COG0465  79 VTAKPPEESSWL------LSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYdEDKPKVTFDDVAG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 305 CEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDM 384
Cdd:COG0465 147 VDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 385 FAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQ 464
Cdd:COG0465 227 FEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 465 IYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDAlsrkLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERV 544
Cdd:COG0465 307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEV----IARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRV 382
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 545 IGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPRE-QFLYTREQLFDRMCMMLGG 623
Cdd:COG0465 383 IAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGG 462
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 624 RVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLV 697
Cdd:COG0465 463 RAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYG-ESEGEVFLgrdigqSRNYSEETAREIDEEVRRII 541
                       570       580       590       600
                ....*....|....*....|....*....|....*....|..
gi 66792806 698 RSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGP 739
Cdd:COG0465 542 DEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
281-738 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: 706.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   281 FSVGETTAKIL-KNNIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANV 359
Cdd:TIGR01241  35 FSFGKSKAKLLnEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   360 PFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNV 439
Cdd:TIGR01241 115 PFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   440 VVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDgslsKDALSRKLAALTPGFTGADISNVCNE 519
Cdd:TIGR01241 195 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLA----PDVDLKAVARRTPGFSGADLANLLNE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   520 AALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQ 599
Cdd:TIGR01241 271 AALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQ 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   600 YLPRE-QFLYTREQLFDRMCMMLGGRVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSF-----DFPRQG 673
Cdd:TIGR01241 351 FLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYgsdggDVFLGR 430
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66792806   674 ETMVEKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLG 738
Cdd:TIGR01241 431 GFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
280-749 3.81e-166

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 494.57  E-value: 3.81e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  280 LFSVGETTAKILKN-NIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN 358
Cdd:CHL00176 162 LMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  359 VPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTN 438
Cdd:CHL00176 242 VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  439 VVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRKlaalTPGFTGADISNVCN 518
Cdd:CHL00176 322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARR----TPGFSGADLANLLN 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  519 EAALIAARHLSPSVQERHFEQAIERVIGGLEkKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYA 598
Cdd:CHL00176 398 EAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLT 476
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  599 QYLP-REQFLYTREQLFDRMCMMLGGRVAEQLFFG--QITTGAQDDLRKVTQSAYAQIVQFGMSeKLGQVSFDFPRQGET 675
Cdd:CHL00176 477 WFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDP 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  676 MV------EKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGPR-PFAEKSTY 748
Cdd:CHL00176 556 FLgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTW 635

                 .
gi 66792806  749 E 749
Cdd:CHL00176 636 K 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
297-467 1.03e-114

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: 344.60  E-value: 1.03e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 297 VRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGV 376
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 377 GPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALT 456
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                       170
                ....*....|.
gi 66792806 457 RPGRFDRQIYI 467
Cdd:cd19501 161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
554-736 1.25e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.17  E-value: 1.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   554 VLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPREQ-FLYTREQLFDRMCMMLGGRVAEQLFFG 632
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   633 QITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGET------MVEKPYSEATAQLIDEEVRCLVRSAYNRTLE 706
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGNVflgrgmGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 66792806   707 LLTQCREQVEKVGRRLLEKEVLEKADMIEL 736
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
333-471 1.17e-21

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: 92.05  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806    333 PKGAMLTGPPGTGKTLLAKATAGEANVP---FITVNGSEFLE--------------MFVGVGPARVRDMFAMARKHAPCI 395
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66792806    396 LFIDEIDAIGRKRgrghlggqSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPgRFDRQIYIGPPD 471
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
149-739 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 770.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 149 VAAGFLYFYFRDPG---KEITWKHFVQYyLARGLVDRLEVVNKQfVRVIPVPGTtSERFVwFNIGSVDTFERNLESAQWE 225
Cdd:COG0465   3 LLLVLLFNLFSSSSssvKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGT-KTRFT-TYRVNDPELVDLLEEKGVE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 226 LGIEPTNQAAVVyttesdGSFLRSLVPTLVLVSILLYAMRRGPMGTGRggrgggLFSVGETTAKIL-KNNIDVRFADVAG 304
Cdd:COG0465  79 VTAKPPEESSWL------LSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYdEDKPKVTFDDVAG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 305 CEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDM 384
Cdd:COG0465 147 VDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 385 FAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQ 464
Cdd:COG0465 227 FEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 465 IYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDAlsrkLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERV 544
Cdd:COG0465 307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEV----IARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRV 382
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 545 IGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPRE-QFLYTREQLFDRMCMMLGG 623
Cdd:COG0465 383 IAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGG 462
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 624 RVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLV 697
Cdd:COG0465 463 RAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYG-ESEGEVFLgrdigqSRNYSEETAREIDEEVRRII 541
                       570       580       590       600
                ....*....|....*....|....*....|....*....|..
gi 66792806 698 RSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGP 739
Cdd:COG0465 542 DEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
281-738 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: 706.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   281 FSVGETTAKIL-KNNIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANV 359
Cdd:TIGR01241  35 FSFGKSKAKLLnEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   360 PFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNV 439
Cdd:TIGR01241 115 PFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   440 VVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDgslsKDALSRKLAALTPGFTGADISNVCNE 519
Cdd:TIGR01241 195 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLA----PDVDLKAVARRTPGFSGADLANLLNE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   520 AALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQ 599
Cdd:TIGR01241 271 AALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQ 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   600 YLPRE-QFLYTREQLFDRMCMMLGGRVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSF-----DFPRQG 673
Cdd:TIGR01241 351 FLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYgsdggDVFLGR 430
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66792806   674 ETMVEKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLG 738
Cdd:TIGR01241 431 GFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
280-749 3.81e-166

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 494.57  E-value: 3.81e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  280 LFSVGETTAKILKN-NIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN 358
Cdd:CHL00176 162 LMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  359 VPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTN 438
Cdd:CHL00176 242 VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  439 VVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRKlaalTPGFTGADISNVCN 518
Cdd:CHL00176 322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARR----TPGFSGADLANLLN 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  519 EAALIAARHLSPSVQERHFEQAIERVIGGLEkKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYA 598
Cdd:CHL00176 398 EAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLT 476
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  599 QYLP-REQFLYTREQLFDRMCMMLGGRVAEQLFFG--QITTGAQDDLRKVTQSAYAQIVQFGMSeKLGQVSFDFPRQGET 675
Cdd:CHL00176 477 WFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDP 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  676 MV------EKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGPR-PFAEKSTY 748
Cdd:CHL00176 556 FLgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTW 635

                 .
gi 66792806  749 E 749
Cdd:CHL00176 636 K 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
245-740 1.03e-156

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 470.67  E-value: 1.03e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  245 SFLRSLVPTLVLVSILLYAMRRGPMGTGRGGrggglFSVGETTAKIL-KNNIDVRFADVAGCEEAKLEIMEFVNFLKNPK 323
Cdd:PRK10733 101 SIFISWFPMLLLIGVWIFFMRQMQGGGGKGA-----MSFGKSKARMLtEDQIKTTFADVAGCDEAKEEVAELVEYLREPS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  324 QYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDA 403
Cdd:PRK10733 176 RFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDA 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  404 IGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHL 483
Cdd:PRK10733 256 VGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHM 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  484 RPLKLDGSLSKDALSRKlaalTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTV 563
Cdd:PRK10733 336 RRVPLAPDIDAAIIARG----TPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKEST 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  564 AYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPR-EQFLYTREQLFDRMCMMLGGRVAEQLFFG--QITTGAQD 640
Cdd:PRK10733 412 AYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEgDAISASRQKLESQISTLYGGRLAEEIIYGpeHVSTGASN 491
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  641 DLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQ 714
Cdd:PRK10733 492 DIKVATNLARNMVTQWGFSEKLGPLLYA-EEEGEVFLgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDI 570
                        490       500
                 ....*....|....*....|....*.
gi 66792806  715 VEKVGRRLLEKEVLEKADMIELLGPR 740
Cdd:PRK10733 571 LHAMKDALMKYETIDAPQIDDLMARR 596
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
297-467 1.03e-114

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: 344.60  E-value: 1.03e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 297 VRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGV 376
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 377 GPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALT 456
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                       170
                ....*....|.
gi 66792806 457 RPGRFDRQIYI 467
Cdd:cd19501 161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
296-552 4.13e-113

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 346.61  E-value: 4.13e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 296 DVRFADVAGCEEAKLEIMEFV-NFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:COG1222  74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGqsEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 454
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 455 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDalsrKLAALTPGFTGADISNVCNEAALIAARHLSPSVQE 534
Cdd:COG1222 232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLD----KLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307
                       250
                ....*....|....*...
gi 66792806 535 RHFEQAIERVIGGLEKKT 552
Cdd:COG1222 308 EDLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
296-551 1.95e-93

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 297.51  E-value: 1.95e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  296 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  375 GVGpAR-VRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDP 453
Cdd:PRK03992 207 GEG-ARlVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  454 ALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSkdalSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQ 533
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD----LEELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*...
gi 66792806  534 ERHFEQAIERVIGGLEKK 551
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
554-736 1.25e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.17  E-value: 1.25e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   554 VLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPREQ-FLYTREQLFDRMCMMLGGRVAEQLFFG 632
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   633 QITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGET------MVEKPYSEATAQLIDEEVRCLVRSAYNRTLE 706
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGNVflgrgmGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 66792806   707 LLTQCREQVEKVGRRLLEKEVLEKADMIEL 736
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
296-544 1.31e-78

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: 258.69  E-value: 1.31e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 296 DVRFADVAGCEEAKLEIMEFVN-FLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:COG0464 153 EAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYV 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHlGGQSEQEntLNQMLVEMDGFNSstNVVVLAGTNRPDILDPA 454
Cdd:COG0464 233 GETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG-DGVGRRV--VNTLLTEMEELRS--DVVVIAATNRPDLLDPA 307
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 455 LTRpgRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDgslsKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQE 534
Cdd:COG0464 308 LLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD----EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTT 381
                       250
                ....*....|
gi 66792806 535 RHFEQAIERV 544
Cdd:COG0464 382 EDLLEALERE 391
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
296-545 1.73e-78

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: 257.03  E-value: 1.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   296 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 454
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   455 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRklaaLTPGFTGADISNVCNEAALIAARHLSPSVQE 534
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAK----MTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 66792806   535 RHFEQAIERVI 545
Cdd:TIGR01242 354 DDFIKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
296-550 1.07e-73

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 254.83  E-value: 1.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   296 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHlgGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 454
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   455 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPS--- 531
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSM----PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSpak 682
                         250       260       270
                  ....*....|....*....|....*....|....
gi 66792806   532 ---------------VQERHFEQAIERVIGGLEK 550
Cdd:TIGR01243 683 eklevgeeeflkdlkVEMRHFLEALKKVKPSVSK 716
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
299-465 1.97e-68

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: 223.37  E-value: 1.97e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 299 FADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVG 377
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 378 PARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTR 457
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                ....*...
gi 66792806 458 PGRFDRQI 465
Cdd:cd19502 162 PGRFDRKI 169
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
299-545 1.36e-64

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 222.34  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  299 FADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVG 377
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  378 PARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTR 457
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  458 PGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHF 537
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKM----TLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                 ....*...
gi 66792806  538 EQAIERVI 545
Cdd:PTZ00361 418 RKAKEKVL 425
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
296-545 1.61e-62

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 215.40  E-value: 1.61e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  296 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 454
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  455 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQE 534
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKM----NLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILP 376
                        250
                 ....*....|.
gi 66792806  535 RHFEQAIERVI 545
Cdd:PTZ00454 377 KDFEKGYKTVV 387
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
296-590 3.31e-62

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: 222.86  E-value: 3.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   296 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 374
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKrgRGHLGGQSEQEnTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 454
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPK--REEVTGEVEKR-VVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   455 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPS--- 531
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNM----PLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREgki 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   532 ----------------VQERHFEQAIERV-------------------IGGLEKKTQVLQpsekttvayhEAghavVGWF 576
Cdd:TIGR01243 407 nfeaeeipaevlkelkVTMKDFMEALKMVepsairevlvevpnvrwsdIGGLEEVKQELR----------EA----VEWP 472
                         330
                  ....*....|....
gi 66792806   577 LEHADPLLKVSIIP 590
Cdd:TIGR01243 473 LKHPEIFEKMGIRP 486
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
308-467 4.12e-62

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 205.59  E-value: 4.12e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 308 AKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAM 387
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 388 ARKHAPCILFIDEIDAIGRKRGRghLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
299-543 2.10e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 204.35  E-value: 2.10e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 299 FADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGP 378
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 379 ARVRDMFAMARKhAPCILFIDEIDAIGRKRGRGHLGGqsEQENTLNQMLVEMDGFNSstNVVVLAGTNRPDILDPALTRp 458
Cdd:COG1223  81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 459 gRFDRQIYIGPPDIKGRSSIFKVHLRPLKldgsLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFE 538
Cdd:COG1223 155 -RFDEVIEFPLPDKEERKEILELNLKKFP----LPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229

                ....*
gi 66792806 539 QAIER 543
Cdd:COG1223 230 EALKQ 234
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
301-467 3.12e-58

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: 195.59  E-value: 3.12e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 379
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 380 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRP 458
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 66792806 459 GRFDRQIYI 467
Cdd:cd19503 157 GRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
308-467 8.05e-57

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: 191.34  E-value: 8.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 308 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFA 386
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 387 MARKHAPCILFIDEIDAIGRKRGRGhlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIY 466
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQS--DSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                .
gi 66792806 467 I 467
Cdd:cd19511 159 V 159
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
308-467 2.03e-54

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: 185.01  E-value: 2.03e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 308 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFA 386
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 387 MARKHAPCILFIDEIDAIGRKRGRGhlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIY 466
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTT--GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                .
gi 66792806 467 I 467
Cdd:cd19529 159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
309-467 1.42e-53

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: 182.71  E-value: 1.42e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 309 KLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAM 387
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 388 ARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
337-468 2.47e-53

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: 180.87  E-value: 2.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   337 MLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlGGQ 416
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 66792806   417 SEQENTLNQMLVEMDGFNSST-NVVVLAGTNRPDILDPALtrPGRFDRQIYIG 468
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPAL--LGRFDRIIEFP 129
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
301-468 1.80e-51

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: 176.86  E-value: 1.80e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 379
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 380 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHlgGQSEQEnTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPG 459
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 66792806 460 RFDRQIYIG 468
Cdd:cd19519 158 RFDREIDIG 166
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
313-467 6.31e-48

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: 166.89  E-value: 6.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 313 MEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHA 392
Cdd:cd19530  10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66792806 393 PCILFIDEIDAIGRKRGRghlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19530  90 PCVIFFDEVDALVPKRGD---GGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
301-465 1.66e-44

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: 157.57  E-value: 1.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNFLKNPKQ-YQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 379
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 380 RVRDMFAMARKHAPCILFIDEIDAIGRKRGrghlGGQSEQENTL-NQMLVEMDGFN----SSTNVVVLAGTNRPDILDPA 454
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRE----SAQREMERRIvSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                       170
                ....*....|.
gi 66792806 455 LTRPGRFDRQI 465
Cdd:cd19518 157 LRRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
320-466 1.41e-43

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: 154.89  E-value: 1.41e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 320 KNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFID 399
Cdd:cd19526  14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66792806 400 EIDAIGRKRGRGHLGgqsEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIY 466
Cdd:cd19526  94 EFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
309-467 8.19e-41

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: 146.89  E-value: 8.19e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 309 KLEIMEFVNF-LKNPKQYQDlGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAM 387
Cdd:cd19527   2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 388 ARKHAPCILFIDEIDAIGRKRGR-GHLGGQSEQenTLNQMLVEMDGFNSST-NVVVLAGTNRPDILDPALTRPGRFDRQI 465
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                ..
gi 66792806 466 YI 467
Cdd:cd19527 159 YL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
302-467 3.45e-36

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 134.02  E-value: 3.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 302 VAGCEEAKLEIMEFVNF-LKNPKQYQdLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPAR 380
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 381 VRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGFNSSTN--VVVLAGTNRPDILDPALTR 457
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155
                       170
                ....*....|
gi 66792806 458 pgRFDRQIYI 467
Cdd:cd19509 156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
296-467 2.30e-34

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 129.21  E-value: 2.30e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 296 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMF 373
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 374 VGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGF-NSSTNVVVLAGTNRPDIL 451
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIkTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                       170
                ....*....|....*.
gi 66792806 452 DPALTRpgRFDRQIYI 467
Cdd:cd19521 157 DSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
301-466 4.29e-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: 122.62  E-value: 4.29e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN-----VPFITVNGSEFLEMFV 374
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 375 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRgrghlggQSEQENT----LNQMLVEMDGFNSSTNVVVLAGTNRPDI 450
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                       170
                ....*....|....*.
gi 66792806 451 LDPALTRPGRFDRQIY 466
Cdd:cd19517 154 LDPALRRPGRFDREFY 169
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
289-467 5.84e-32

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: 122.79  E-value: 5.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 289 KILKNNIDVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGS 367
Cdd:cd19525  11 EIMDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISAS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 368 EFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRgrghlgGQSEQENTL---NQMLVEMDGFNSSTN--VVVL 442
Cdd:cd19525  90 SLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR------GEGEHESSRrikTEFLVQLDGATTSSEdrILVV 163
                       170       180
                ....*....|....*....|....*
gi 66792806 443 AGTNRPDILDPALTRpgRFDRQIYI 467
Cdd:cd19525 164 GATNRPQEIDEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
301-467 1.57e-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: 118.16  E-value: 1.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGP 378
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 379 ARVRDMFAMARKHAPCILFIDEIDAIGRKRgrghlGGQSEQENTL---NQMLVEMDGF-------NSSTNVVVLAGTNRP 448
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR-----GTSEEHEASRrvkSELLVQMDGVggasendDPSKMVMVLAATNFP 153
                       170
                ....*....|....*....
gi 66792806 449 DILDPALTRpgRFDRQIYI 467
Cdd:cd19522 154 WDIDEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
301-461 2.17e-30

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: 117.53  E-value: 2.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLG-AKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGP 378
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 379 ARVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlggqSEQENTL---NQMLVEMDGFNSSTN--VVVLAGTNRPDILDP 453
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDE 154
                       170
                ....*....|
gi 66792806 454 ALTR--PGRF 461
Cdd:cd19520 155 AILRrmPKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
322-467 5.97e-30

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: 116.82  E-value: 5.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 322 PKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANV--PFItVNGSEFLEMFVGVGPARVRDMFAMARKHAPC----- 394
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAEEEQRRlgans 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66792806 395 ---ILFIDEIDAIGRKRGRGHlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19504 103 glhIIIFDEIDAICKQRGSMA-GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
333-469 4.11e-29

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: 113.40  E-value: 4.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 333 PKGAMLTGPPGTGKTLLAKATAGEA---NVPFITVNGSEFLEMFVG---VGPARVRDMFAMARKHAPCILFIDEIDAIGR 406
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66792806 407 KrgrghlggqsEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGP 469
Cdd:cd00009  99 G----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
301-467 1.12e-28

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: 112.64  E-value: 1.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 379
Cdd:cd19524   1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 380 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGF--NSSTNVVVLAGTNRPDILDPALT 456
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVL 155
                       170
                ....*....|.
gi 66792806 457 RpgRFDRQIYI 467
Cdd:cd19524 156 R--RFTKRVYV 164
ycf46 CHL00195
Ycf46; Provisional
323-524 2.00e-26

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 113.96  E-value: 2.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  323 KQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEID 402
Cdd:CHL00195 249 KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEID 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  403 -AIGRKRGRGHLGGQSEQENTLNQMLVEmdgfnSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKV 481
Cdd:CHL00195 329 kAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKI 403
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 66792806  482 HLRPLKLDGSLSKDAlsRKLAALTPGFTGADISNVCNEAALIA 524
Cdd:CHL00195 404 HLQKFRPKSWKKYDI--KKLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
323-467 9.11e-22

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 92.82  E-value: 9.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 323 KQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEID 402
Cdd:cd19507  21 KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66792806 403 aigrkRGRGHLGGQSEQENT---LNQMLVEMDgfNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19507 101 -----KGFSNADSKGDSGTSsrvLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
333-471 1.17e-21

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: 92.05  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806    333 PKGAMLTGPPGTGKTLLAKATAGEANVP---FITVNGSEFLE--------------MFVGVGPARVRDMFAMARKHAPCI 395
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66792806    396 LFIDEIDAIGRKRgrghlggqSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPgRFDRQIYIGPPD 471
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
318-467 1.73e-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: 85.87  E-value: 1.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 318 FLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEflemfVGVGPARVRDMFAMARKHApcILF 397
Cdd:cd19510   8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66792806 398 IDEIDA---IGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19510  81 LEDIDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
301-467 2.69e-16

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 76.85  E-value: 2.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 301 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLgAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 379
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 380 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQentlNQMLVEMDGFNSST--NVVVLAGTNRPDILDPALTR 457
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQ----VELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
                       170
                ....*....|
gi 66792806 458 pgRFDRQIYI 467
Cdd:cd19523 156 --YFSKRLLV 163
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
328-467 3.78e-14

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: 70.87  E-value: 3.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 328 LGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFL--------------EMFVGVGPARVRDMFAMARKHAP 393
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66792806 394 CILFIDEIDAIGRKRgrghLGGQSEQENT--LNQML--VEMDGFNSST-NVVVLAGTNRPDILDPALTRPGRFDRQIYI 467
Cdd:cd19505  87 CIIWIPNIHELNVNR----STQNLEEDPKllLGLLLnyLSRDFEKSSTrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
500-539 9.83e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 60.24  E-value: 9.83e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 66792806   500 KLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQ 539
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK04195 PRK04195
replication factor C large subunit; Provisional
298-418 1.59e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 64.17  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  298 RFADVAGCEEAKLEIMEFV-NFLKNpkqyqdlgaKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEF-----LE 371
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 66792806  372 MFVGVGpARVRDMFAMARKhapcILFIDEIDAIgrkRGRGHLGGQSE 418
Cdd:PRK04195  83 RVAGEA-ATSGSLFGARRK----LILLDEVDGI---HGNEDRGGARA 121
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
337-465 2.98e-10

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 59.08  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 337 MLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMfvGV-GPARVRDMFAMARK-HAPCILFIDEIDAIGRKRGRGHLg 414
Cdd:cd19512  26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEKI- 102
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 66792806 415 gQSEQENTLNQMLVEMdGFNSSTNVVVLAgTNRPDILDPALTrpGRFDRQI 465
Cdd:cd19512 103 -SEDLRAALNAFLYRT-GEQSNKFMLVLA-SNQPEQFDWAIN--DRIDEMV 148
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
332-412 3.75e-10

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: 59.70  E-value: 3.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 332 IPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEM-FVGvgparvRDMFAMARKHAPCILFIDEIDAI-GRKRG 409
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIaKRGGS 118

                ...
gi 66792806 410 RGH 412
Cdd:cd19498 119 SGP 121
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
337-404 4.00e-09

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: 56.43  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   337 MLTGPPGTGKTLLAKATAGEANV---PFITVNGSEFLE-----MFVGVGPARVR-----DMFAMARKHAPCILFIDEIDA 403
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIEK 86

                  .
gi 66792806   404 I 404
Cdd:pfam07724  87 A 87
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
338-401 5.02e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 59.33  E-value: 5.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66792806  338 LTGPPGTGKTLLAKATAGEANVPFITVNGSeflemFVGVgpARVRDMFAMARKHA----PCILFIDEI 401
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
340-401 5.63e-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: 5.63e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66792806 340 GPPGTGKTLLAKATAGEANVPFITVNGSeflemFVGVgpARVRDMFAMARKHA----PCILFIDEI 401
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
333-544 7.31e-08

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 55.24  E-value: 7.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 333 PKGAMLTGPPGTGKTLLAKATAGEA---------NVPFITVN----GSEF------LEMFV--------GVGPARVRDMF 385
Cdd:COG1474  51 PSNVLIYGPTGTGKTAVAKYVLEELeeeaeergvDVRVVYVNcrqaSTRYrvlsriLEELGsgedipstGLSTDELFDRL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 386 --AMARKHAPCILFIDEIDAIGRKRGrghlggqseqENTLNQmLVEMDGFNSSTNVVVLAGTNRPDI---LDP-ALTRPG 459
Cdd:COG1474 131 yeALDERDGVLVVVLDEIDYLVDDEG----------DDLLYQ-LLRANEELEGARVGVIGISNDLEFlenLDPrVKSSLG 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 460 ----RFDR----QIYigppDI-KGRSSI-FKvhlrplklDGSLSKDALsRKLAALTPGFTG-A----DISNVcneAALIA 524
Cdd:COG1474 200 eeeiVFPPydadELR----DIlEDRAELaFY--------DGVLSDEVI-PLIAALAAQEHGdArkaiDLLRV---AGEIA 263
                       250       260
                ....*....|....*....|
gi 66792806 525 ARHLSPSVQERHFEQAIERV 544
Cdd:COG1474 264 EREGSDRVTEEHVREAREKI 283
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
337-461 1.42e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 48.06  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   337 MLTGPPGTGKTLLAKATAgEA--NVPFITVNGSEFLE-------MFVGVGPARVRD---MFAMARKHapcILFIDEIDai 404
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgplVRAAREGE---IAVLDEIN-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   405 grkrgRGHlggqSEQENTLNQMLVE-----MDGFN----SSTNVVVLAGTNRPDI----LDPALTRpgRF 461
Cdd:pfam07728  77 -----RAN----PDVLNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
300-406 3.51e-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: 47.94  E-value: 3.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 300 ADVAGCEEAKLEIMEF--VNFLKNpkqyqDLGAKIpkgAMLTGPPGTGKTLLAKATAGEANVPF--ITVNG-SEFLEM-- 372
Cdd:cd19500  10 ADHYGLEDVKERILEYlaVRKLKG-----SMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvRDEAEIrg 81
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 66792806 373 ----FVGVGPARVRDMFAMARKHAPCILfIDEIDAIGR 406
Cdd:cd19500  82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
337-467 3.86e-06

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: 48.21  E-value: 3.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 337 MLTGPPGTGKTLLAKATAGEANV---------PFITVNGSEFLEMFVGVGPARVRDMFA-----MARKHAPCILFIDEID 402
Cdd:cd19508  56 LLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEVE 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66792806 403 AIGRKRGRGHLGGQ-SEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTrpGRFDRQIYI 467
Cdd:cd19508 136 SLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
334-369 8.01e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 49.20  E-value: 8.01e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 66792806 334 KGAMLTGPPGTGKTLLAKATAGE--ANVPFITVNGSEF 369
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
305-401 8.40e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.00  E-value: 8.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 305 CEEAKLEIMEFVNFLKNPKQyqdlgakipkgAMLTGPPGTGKT----LLAKATAGEA--NVPFITVN----GSEFLEMFV 374
Cdd:COG1401 204 REKFEETLEAFLAALKTKKN-----------VILAGPPGTGKTylarRLAEALGGEDngRIEFVQFHpswsYEDFLLGYR 272
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 66792806 375 ---GVGPARVRD-MF------AMARKHAPCILFIDEI 401
Cdd:COG1401 273 pslDEGKYEPTPgIFlrfclkAEKNPDKPYVLIIDEI 309
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
142-233 9.91e-06

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: 44.90  E-value: 9.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   142 LAVLGAGVAAGFLYFYF---RDPGKEITWKHFVQyYLARGLVDRLEVVNKQFVRVIPVPGTTSER-----FVWFNIGSVD 213
Cdd:pfam06480   3 LWLLILLVLLLLFLLFLlssSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGskfttYFIPSLPNVD 81
                          90       100
                  ....*....|....*....|
gi 66792806   214 TFERNLESAQWELGIEPTNQ 233
Cdd:pfam06480  82 SLLEKLEDALEEKGVKVSVK 101
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
337-452 1.88e-05

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: 44.80  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 337 MLTGPPGTGKTLLAKATAGEA---NVPFITVngsEFLEMFVgvgpARVRDmfaMARKHAPCILFIDEIDAIGRKRGRGhl 413
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFI---SFLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARASQGD-- 69
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 66792806 414 ggqsEQENTLNQMLVEMDGFNsSTNVVVLAGTNRPDILD 452
Cdd:cd01120  70 ----RSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
337-402 2.45e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 45.63  E-value: 2.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 337 MLTGPPGTGKTLLAKATA-----GEANvpFITVNGSEFLEMF-----VGVGPARV----RDMFAMA-RKHAPCILFIDEI 401
Cdd:cd19499  45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122

                .
gi 66792806 402 D 402
Cdd:cd19499 123 E 123
AAA_22 pfam13401
AAA domain;
337-452 3.96e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 43.87  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   337 MLTGPPGTGKTLLAK---ATAGEANVPFITVN------GSEFLEMFV------GVGPARVRDMFAM-----ARKHAPCIL 396
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVDlpsgtsPKDLLRALLralglpLSGRLSKEELLAAlqqllLALAVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 66792806   397 FIDEIDAIgrkrgrghlggqseQENTLNQmLVEMDGFNSSTNVVVLAGTnrPDILD 452
Cdd:pfam13401  89 IIDEAQHL--------------SLEALEE-LRDLLNLSSKLLQLILVGT--PELRE 127
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
334-372 6.01e-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: 46.15  E-value: 6.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 66792806   334 KGAMLTGPPGTGKTLLAKATAGE--ANVPFITVNGSEF--LEM 372
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVysLEM 93
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
319-407 7.81e-05

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 44.90  E-value: 7.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 319 LKNPKQYQDLGAKIPKGAM-LTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEM-FVG--VGPARVR----DMFAMARK 390
Cdd:cd19497  35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKllqaADYDVERA 114
                        90
                ....*....|....*..
gi 66792806 391 HAPcILFIDEIDAIGRK 407
Cdd:cd19497 115 QRG-IVYIDEIDKIARK 130
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
337-407 9.47e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.53  E-value: 9.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  337 MLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEM-FVGvgparvRDMFAMARK--HApC----------ILFIDEIDA 403
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVG------EDVENILLKllQA-AdydvekaqrgIVYIDEIDK 184

                 ....
gi 66792806  404 IGRK 407
Cdd:PRK05342 185 IARK 188
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
331-403 1.01e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 43.39  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 331 KIPKGAM--LTGPPGTGKTLLAKATAGEANVP--FITVNGSEFLEMFVGVGPARV----------RDMFAMARK--HAPC 394
Cdd:cd00267  21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                ....*....
gi 66792806 395 ILFIDEIDA 403
Cdd:cd00267 101 LLLLDEPTS 109
44 PHA02544
clamp loader, small subunit; Provisional
331-419 2.92e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.83  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806  331 KIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEflemfVGVGPARVR-DMFA--MARKHAPCILFIDEIDAIGRK 407
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD-----CRIDFVRNRlTRFAstVSLTGGGKVIIIDEFDRLGLA 115
                         90
                 ....*....|..
gi 66792806  408 RGRGHLGGQSEQ 419
Cdd:PHA02544 116 DAQRHLRSFMEA 127
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
337-401 5.27e-04

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 41.33  E-value: 5.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66792806   337 MLTGPPGTGKTLLAKATAGEANVPF-ITvngseflemfvgVGPA--RVRDMFAMARKHAPC-ILFIDEI 401
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIrIT------------SGPAieRPGDLAAILTNLEPGdVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
338-406 1.21e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 1.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66792806  338 LTGPPGTGKTLLAKATAGEANVPFITVNGseflemfvgvgPA--RVRDMFAM---ARKHApcILFIDEIDAIGR 406
Cdd:PRK00080  56 LYGPPGLGKTTLANIIANEMGVNIRITSG-----------PAleKPGDLAAIltnLEEGD--VLFIDEIHRLSP 116
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
338-402 2.08e-03

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.92  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806 338 LTGPPGTGKTLLAKATAGEANVPFITVNGSE----------------FLEMFVGVGPArvrdmFAmarkhapCILFIDEI 401
Cdd:COG0714  36 LEGVPGVGKTTLAKALARALGLPFIRIQFTPdllpsdilgtyiydqqTGEFEFRPGPL-----FA-------NVLLADEI 103

                .
gi 66792806 402 D 402
Cdd:COG0714 104 N 104
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
329-406 3.84e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.98  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792806   329 GAKIPKGA----MLTGPPGTGKTLLAKATAGEANVpfitvngseflEMFVGVGPA--RVRDMFAMA---RKHApcILFID 399
Cdd:TIGR00635  22 AAKMRQEAldhlLLYGPPGLGKTTLAHIIANEMGV-----------NLKITSGPAleKPGDLAAILtnlEEGD--VLFID 88

                  ....*..
gi 66792806   400 EIDAIGR 406
Cdd:TIGR00635  89 EIHRLSP 95
 
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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