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Conserved domains on  [gi|755526291|ref|XP_011246578|]
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AFG3-like protein 1 isoform X1 [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];
23-613 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 762.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  23 VAAGFLYFYFRDPG---KEITWKHFVQYyLARGLVDRLEVVNKQfVRVIPVPGTtSERFVwFNIGSVDTFERNLESAQWE 99
Cdd:COG0465    3 LLLVLLFNLFSSSSssvKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGT-KTRFT-TYRVNDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 100 LGIEPTNQAAVVyttesdGSFLRSLVPTLVLVSILLYAMRRGPMGTGRggrgggLFSVGETTAKIL-KNNIDVRFADVAG 178
Cdd:COG0465   79 VTAKPPEESSWL------LSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYdEDKPKVTFDDVAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 179 CEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDM 258
Cdd:COG0465  147 VDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 259 FAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQ 338
Cdd:COG0465  227 FEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 339 IYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDAlsrkLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERV 418
Cdd:COG0465  307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEV----IARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRV 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 419 IGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPRE-QFLYTREQLFDRMCMMLGG 497
Cdd:COG0465  383 IAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGG 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 498 RVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLV 571
Cdd:COG0465  463 RAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYG-ESEGEVFLgrdigqSRNYSEETAREIDEEVRRII 541
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 755526291 572 RSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGP 613
Cdd:COG0465  542 DEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
23-613 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 762.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  23 VAAGFLYFYFRDPG---KEITWKHFVQYyLARGLVDRLEVVNKQfVRVIPVPGTtSERFVwFNIGSVDTFERNLESAQWE 99
Cdd:COG0465    3 LLLVLLFNLFSSSSssvKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGT-KTRFT-TYRVNDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 100 LGIEPTNQAAVVyttesdGSFLRSLVPTLVLVSILLYAMRRGPMGTGRggrgggLFSVGETTAKIL-KNNIDVRFADVAG 178
Cdd:COG0465   79 VTAKPPEESSWL------LSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYdEDKPKVTFDDVAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 179 CEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDM 258
Cdd:COG0465  147 VDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 259 FAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQ 338
Cdd:COG0465  227 FEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 339 IYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDAlsrkLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERV 418
Cdd:COG0465  307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEV----IARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRV 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 419 IGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPRE-QFLYTREQLFDRMCMMLGG 497
Cdd:COG0465  383 IAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGG 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 498 RVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLV 571
Cdd:COG0465  463 RAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYG-ESEGEVFLgrdigqSRNYSEETAREIDEEVRRII 541
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 755526291 572 RSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGP 613
Cdd:COG0465  542 DEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
155-612 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: 700.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  155 FSVGETTAKIL-KNNIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANV 233
Cdd:TIGR01241  35 FSFGKSKAKLLnEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  234 PFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNV 313
Cdd:TIGR01241 115 PFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  314 VVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDgslsKDALSRKLAALTPGFTGADISNVCNE 393
Cdd:TIGR01241 195 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLA----PDVDLKAVARRTPGFSGADLANLLNE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  394 AALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQ 473
Cdd:TIGR01241 271 AALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQ 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  474 YLPRE-QFLYTREQLFDRMCMMLGGRVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSF-----DFPRQG 547
Cdd:TIGR01241 351 FLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYgsdggDVFLGR 430
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526291  548 ETMVEKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLG 612
Cdd:TIGR01241 431 GFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
154-623 7.00e-166

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 489.56  E-value: 7.00e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 154 LFSVGETTAKILKN-NIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN 232
Cdd:CHL00176 162 LMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 233 VPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTN 312
Cdd:CHL00176 242 VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 313 VVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRKlaalTPGFTGADISNVCN 392
Cdd:CHL00176 322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARR----TPGFSGADLANLLN 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 393 EAALIAARHLSPSVQERHFEQAIERVIGGLEkKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYA 472
Cdd:CHL00176 398 EAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLT 476
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 473 QYLP-REQFLYTREQLFDRMCMMLGGRVAEQLFFG--QITTGAQDDLRKVTQSAYAQIVQFGMSeKLGQVSFDFPRQGET 549
Cdd:CHL00176 477 WFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDP 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 550 MV------EKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGPR-PFAEKSTY 622
Cdd:CHL00176 556 FLgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTW 635

                 .
gi 755526291 623 E 623
Cdd:CHL00176 636 K 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
171-341 4.17e-115

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: 341.90  E-value: 4.17e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 171 VRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGV 250
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 251 GPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALT 330
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 755526291 331 RPGRFDRQIYI 341
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
428-610 4.03e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 267.93  E-value: 4.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  428 VLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPREQ-FLYTREQLFDRMCMMLGGRVAEQLFFG 506
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  507 QITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGET------MVEKPYSEATAQLIDEEVRCLVRSAYNRTLE 580
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGNVflgrgmGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 755526291  581 LLTQCREQVEKVGRRLLEKEVLEKADMIEL 610
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
207-345 6.38e-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: 89.74  E-value: 6.38e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291   207 PKGAMLTGPPGTGKTLLAKATAGEANVP---FITVNGSEFLE--------------MFVGVGPARVRDMFAMARKHAPCI 269
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526291   270 LFIDEIDAIGRKRgrghlggqSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPgRFDRQIYIGPPD 345
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
23-613 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 762.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  23 VAAGFLYFYFRDPG---KEITWKHFVQYyLARGLVDRLEVVNKQfVRVIPVPGTtSERFVwFNIGSVDTFERNLESAQWE 99
Cdd:COG0465    3 LLLVLLFNLFSSSSssvKEISYSEFLQL-VEAGKVKSVTIQGDR-ITGTLKDGT-KTRFT-TYRVNDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 100 LGIEPTNQAAVVyttesdGSFLRSLVPTLVLVSILLYAMRRGPMGTGRggrgggLFSVGETTAKIL-KNNIDVRFADVAG 178
Cdd:COG0465   79 VTAKPPEESSWL------LSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYdEDKPKVTFDDVAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 179 CEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDM 258
Cdd:COG0465  147 VDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 259 FAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQ 338
Cdd:COG0465  227 FEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 339 IYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDAlsrkLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERV 418
Cdd:COG0465  307 VVVDLPDVKGREAILKVHARKKPLAPDVDLEV----IARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRV 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 419 IGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPRE-QFLYTREQLFDRMCMMLGG 497
Cdd:COG0465  383 IAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEdRYLYTKEELLDRIAVLLGG 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 498 RVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLV 571
Cdd:COG0465  463 RAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYG-ESEGEVFLgrdigqSRNYSEETAREIDEEVRRII 541
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 755526291 572 RSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGP 613
Cdd:COG0465  542 DEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
155-612 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: 700.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  155 FSVGETTAKIL-KNNIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANV 233
Cdd:TIGR01241  35 FSFGKSKAKLLnEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  234 PFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNV 313
Cdd:TIGR01241 115 PFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  314 VVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDgslsKDALSRKLAALTPGFTGADISNVCNE 393
Cdd:TIGR01241 195 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLA----PDVDLKAVARRTPGFSGADLANLLNE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  394 AALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQ 473
Cdd:TIGR01241 271 AALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQ 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  474 YLPRE-QFLYTREQLFDRMCMMLGGRVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSF-----DFPRQG 547
Cdd:TIGR01241 351 FLPEEdKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYgsdggDVFLGR 430
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526291  548 ETMVEKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLG 612
Cdd:TIGR01241 431 GFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
154-623 7.00e-166

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 489.56  E-value: 7.00e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 154 LFSVGETTAKILKN-NIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN 232
Cdd:CHL00176 162 LMNFGKSKARFQMEaDTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 233 VPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTN 312
Cdd:CHL00176 242 VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 313 VVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRKlaalTPGFTGADISNVCN 392
Cdd:CHL00176 322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARR----TPGFSGADLANLLN 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 393 EAALIAARHLSPSVQERHFEQAIERVIGGLEkKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYA 472
Cdd:CHL00176 398 EAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLT 476
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 473 QYLP-REQFLYTREQLFDRMCMMLGGRVAEQLFFG--QITTGAQDDLRKVTQSAYAQIVQFGMSeKLGQVSFDFPRQGET 549
Cdd:CHL00176 477 WFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDP 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 550 MV------EKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGPR-PFAEKSTY 622
Cdd:CHL00176 556 FLgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKTW 635

                 .
gi 755526291 623 E 623
Cdd:CHL00176 636 K 636
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
119-614 2.02e-157

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 468.36  E-value: 2.02e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 119 SFLRSLVPTLVLVSILLYAMRRGPMGTGRGGrggglFSVGETTAKIL-KNNIDVRFADVAGCEEAKLEIMEFVNFLKNPK 197
Cdd:PRK10733 101 SIFISWFPMLLLIGVWIFFMRQMQGGGGKGA-----MSFGKSKARMLtEDQIKTTFADVAGCDEAKEEVAELVEYLREPS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 198 QYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDA 277
Cdd:PRK10733 176 RFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDA 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 278 IGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHL 357
Cdd:PRK10733 256 VGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHM 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 358 RPLKLDGSLSKDALSRKlaalTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTV 437
Cdd:PRK10733 336 RRVPLAPDIDAAIIARG----TPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKEST 411
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 438 AYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPR-EQFLYTREQLFDRMCMMLGGRVAEQLFFG--QITTGAQD 514
Cdd:PRK10733 412 AYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEgDAISASRQKLESQISTLYGGRLAEEIIYGpeHVSTGASN 491
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 515 DLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGETMV------EKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQ 588
Cdd:PRK10733 492 DIKVATNLARNMVTQWGFSEKLGPLLYA-EEEGEVFLgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDI 570
                        490       500
                 ....*....|....*....|....*.
gi 755526291 589 VEKVGRRLLEKEVLEKADMIELLGPR 614
Cdd:PRK10733 571 LHAMKDALMKYETIDAPQIDDLMARR 596
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
171-341 4.17e-115

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: 341.90  E-value: 4.17e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 171 VRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGV 250
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 251 GPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALT 330
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 755526291 331 RPGRFDRQIYI 341
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
170-426 1.36e-112

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 341.60  E-value: 1.36e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 170 DVRFADVAGCEEAKLEIMEFV-NFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGqsEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 328
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 329 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDalsrKLAALTPGFTGADISNVCNEAALIAARHLSPSVQE 408
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLD----KLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307
                        250
                 ....*....|....*...
gi 755526291 409 RHFEQAIERVIGGLEKKT 426
Cdd:COG1222  308 EDLEKAIEKVKKKTETAT 325
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
170-425 8.11e-93

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 292.51  E-value: 8.11e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 170 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 249 GVGpAR-VRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDP 327
Cdd:PRK03992 207 GEG-ARlVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 328 ALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSkdalSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQ 407
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD----LEELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*...
gi 755526291 408 ERHFEQAIERVIGGLEKK 425
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
428-610 4.03e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 267.93  E-value: 4.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  428 VLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPREQ-FLYTREQLFDRMCMMLGGRVAEQLFFG 506
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELIFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  507 QITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDfPRQGET------MVEKPYSEATAQLIDEEVRCLVRSAYNRTLE 580
Cdd:pfam01434  82 EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLE-ESDGNVflgrgmGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 755526291  581 LLTQCREQVEKVGRRLLEKEVLEKADMIEL 610
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
170-419 4.33e-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: 253.18  E-value: 4.33e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  170 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 328
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  329 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRklaaLTPGFTGADISNVCNEAALIAARHLSPSVQE 408
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAK----MTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 755526291  409 RHFEQAIERVI 419
Cdd:TIGR01242 354 DDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
170-418 5.28e-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: 254.07  E-value: 5.28e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 170 DVRFADVAGCEEAKLEIMEFVN-FLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:COG0464  153 EAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYV 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHlGGQSEQEntLNQMLVEMDGFNSstNVVVLAGTNRPDILDPA 328
Cdd:COG0464  233 GETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVG-DGVGRRV--VNTLLTEMEELRS--DVVVIAATNRPDLLDPA 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 329 LTRpgRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDgslsKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQE 408
Cdd:COG0464  308 LLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD----EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTT 381
                        250
                 ....*....|
gi 755526291 409 RHFEQAIERV 418
Cdd:COG0464  382 EDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
170-424 1.34e-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: 251.36  E-value: 1.34e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  170 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHlgGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 328
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  329 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPS--- 405
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSM----PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSpak 682
                         250       260       270
                  ....*....|....*....|....*....|....
gi 755526291  406 ---------------VQERHFEQAIERVIGGLEK 424
Cdd:TIGR01243 683 eklevgeeeflkdlkVEMRHFLEALKKVKPSVSK 716
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
173-339 1.93e-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: 220.67  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 173 FADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVG 251
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 252 PARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTR 331
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                 ....*...
gi 755526291 332 PGRFDRQI 339
Cdd:cd19502  162 PGRFDRKI 169
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
173-419 1.38e-64

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 219.64  E-value: 1.38e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 173 FADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVG 251
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 252 PARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTR 331
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 332 PGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHF 411
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKM----TLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                 ....*...
gi 755526291 412 EQAIERVI 419
Cdd:PTZ00361 418 RKAKEKVL 425
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
182-341 2.11e-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: 204.44  E-value: 2.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 182 AKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAM 261
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 262 ARKHAPCILFIDEIDAIGRKRGRghLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
170-419 2.19e-62

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 212.70  E-value: 2.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 170 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 328
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 329 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQE 408
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKM----NLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILP 376
                        250
                 ....*....|.
gi 755526291 409 RHFEQAIERVI 419
Cdd:PTZ00454 377 KDFEKGYKTVV 387
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
170-464 6.03e-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: 219.78  E-value: 6.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  170 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFV 248
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKrgRGHLGGQSEQEnTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPA 328
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPK--REEVTGEVEKR-VVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  329 LTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLkldgSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPS--- 405
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNM----PLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREgki 406
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  406 ----------------VQERHFEQAIERV-------------------IGGLEKKTQVLQpsekttvayhEAghavVGWF 450
Cdd:TIGR01243 407 nfeaeeipaevlkelkVTMKDFMEALKMVepsairevlvevpnvrwsdIGGLEEVKQELR----------EA----VEWP 472
                         330
                  ....*....|....
gi 755526291  451 LEHADPLLKVSIIP 464
Cdd:TIGR01243 473 LKHPEIFEKMGIRP 486
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
173-417 4.87e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 201.27  E-value: 4.87e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 173 FADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGP 252
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 253 ARVRDMFAMARKhAPCILFIDEIDAIGRKRGRGHLGGqsEQENTLNQMLVEMDGFNSstNVVVLAGTNRPDILDPALTRp 332
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 333 gRFDRQIYIGPPDIKGRSSIFKVHLRPLKldgsLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFE 412
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFP----LPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229

                 ....*
gi 755526291 413 QAIER 417
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 ...
175-341 1.33e-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: 194.43  E-value: 1.33e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 253
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 254 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRP 332
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 755526291 333 GRFDRQIYI 341
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 ...
182-341 1.66e-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: 1.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 182 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFA 260
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 261 MARKHAPCILFIDEIDAIGRKRGRGhlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIY 340
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQS--DSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 755526291 341 I 341
Cdd:cd19511  159 V 159
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
182-341 5.43e-55

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: 184.62  E-value: 5.43e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 182 AKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFA 260
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 261 MARKHAPCILFIDEIDAIGRKRGRGhlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIY 340
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTT--GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 755526291 341 I 341
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 ...
183-341 3.54e-54

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 182.71  E-value: 3.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 183 KLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAM 261
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 262 ARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
211-342 2.67e-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: 178.94  E-value: 2.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  211 MLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlGGQ 290
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755526291  291 SEQENTLNQMLVEMDGFNSST-NVVVLAGTNRPDILDPALtrPGRFDRQIYIG 342
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 ...
175-342 1.37e-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: 175.70  E-value: 1.37e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 253
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 254 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHlgGQSEQEnTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPG 333
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 755526291 334 RFDRQIYIG 342
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 ...
187-341 2.30e-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: 2.30e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 187 MEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHA 266
Cdd:cd19530   10 MSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526291 267 PCILFIDEIDAIGRKRGRghlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
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 ...
175-339 9.48e-45

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: 157.18  E-value: 9.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNFLKNPKQ-YQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 253
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 254 RVRDMFAMARKHAPCILFIDEIDAIGRKRGrghlGGQSEQENTL-NQMLVEMDGFN----SSTNVVVLAGTNRPDILDPA 328
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE----SAQREMERRIvSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                        170
                 ....*....|.
gi 755526291 329 LTRPGRFDRQI 339
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 ...
194-340 4.59e-44

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: 4.59e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 194 KNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFID 273
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755526291 274 EIDAIGRKRGRGHLGgqsEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIY 340
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 ...
183-341 4.27e-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: 4.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 183 KLEIMEFVNF-LKNPKQYQDlGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAM 261
Cdd:cd19527    2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 262 ARKHAPCILFIDEIDAIGRKRGR-GHLGGQSEQenTLNQMLVEMDGFNSST-NVVVLAGTNRPDILDPALTRPGRFDRQI 339
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 755526291 340 YI 341
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 ...
176-341 2.54e-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: 133.63  E-value: 2.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 176 VAGCEEAKLEIMEFVNF-LKNPKQYQdLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPAR 254
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 255 VRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGFNSSTN--VVVLAGTNRPDILDPALTR 331
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 755526291 332 pgRFDRQIYI 341
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
170-341 9.19e-35

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: 129.60  E-value: 9.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 170 DVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMF 247
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 248 VGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGF-NSSTNVVVLAGTNRPDIL 325
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE----GESEASRRIkTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                        170
                 ....*....|....*.
gi 755526291 326 DPALTRpgRFDRQIYI 341
Cdd:cd19521  157 DSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
175-340 3.08e-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: 3.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEAN-----VPFITVNGSEFLEMFV 248
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 249 GVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRgrghlggQSEQENT----LNQMLVEMDGFNSSTNVVVLAGTNRPDI 324
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....*.
gi 755526291 325 LDPALTRPGRFDRQIY 340
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; ...
163-341 3.57e-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: 123.17  E-value: 3.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 163 KILKNNIDVRFADVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGS 241
Cdd:cd19525   11 EIMDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISAS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 242 EFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRgrghlgGQSEQENTL---NQMLVEMDGFNSSTN--VVVL 316
Cdd:cd19525   90 SLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR------GEGEHESSRrikTEFLVQLDGATTSSEdrILVV 163
                        170       180
                 ....*....|....*....|....*
gi 755526291 317 AGTNRPDILDPALTRpgRFDRQIYI 341
Cdd:cd19525  164 GATNRPQEIDEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
175-341 1.19e-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: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQdlGAKIP-KGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGP 252
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 253 ARVRDMFAMARKHAPCILFIDEIDAIGRKRgrghlGGQSEQENTL---NQMLVEMDGF-------NSSTNVVVLAGTNRP 322
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR-----GTSEEHEASRrvkSELLVQMDGVggasendDPSKMVMVLAATNFP 153
                        170
                 ....*....|....*....
gi 755526291 323 DILDPALTRpgRFDRQIYI 341
Cdd:cd19522  154 WDIDEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
175-335 1.94e-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: 1.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLG-AKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGP 252
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 253 ARVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlggqSEQENTL---NQMLVEMDGFNSSTN--VVVLAGTNRPDILDP 327
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDE 154
                        170
                 ....*....|
gi 755526291 328 ALTR--PGRF 335
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; ...
196-341 1.08e-29

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: 115.66  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 196 PKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANV--PFItVNGSEFLEMFVGVGPARVRDMFAMARKHAPC----- 268
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAEEEQRRlgans 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526291 269 ---ILFIDEIDAIGRKRGRGHlGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
Cdd:cd19504  103 glhIIIFDEIDAICKQRGSMA-GSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
175-341 1.98e-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: 111.48  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLGAKiPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 253
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 254 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRghlgGQSEQENTL-NQMLVEMDGF--NSSTNVVVLAGTNRPDILDPALT 330
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE----GEHEASRRLkTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 755526291 331 RpgRFDRQIYI 341
Cdd:cd19524  156 R--RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
207-343 2.29e-28

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: 111.08  E-value: 2.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 207 PKGAMLTGPPGTGKTLLAKATAGEA---NVPFITVNGSEFLEMFVG---VGPARVRDMFAMARKHAPCILFIDEIDAIGR 280
Cdd:cd00009   19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755526291 281 KrgrghlggqsEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGP 343
Cdd:cd00009   99 G----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
197-398 1.37e-26

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 113.96  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 197 KQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEID 276
Cdd:CHL00195 249 KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEID 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 277 -AIGRKRGRGHLGGQSEQENTLNQMLVEmdgfnSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKV 355
Cdd:CHL00195 329 kAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKI 403
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755526291 356 HLRPLKLDGSLSKDAlsRKLAALTPGFTGADISNVCNEAALIA 398
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 ...
197-341 4.08e-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: 93.59  E-value: 4.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 197 KQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEID 276
Cdd:cd19507   21 KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755526291 277 aigrkRGRGHLGGQSEQENT---LNQMLVEMDgfNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
Cdd:cd19507  101 -----KGFSNADSKGDSGTSsrvLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
207-345 6.38e-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: 89.74  E-value: 6.38e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291   207 PKGAMLTGPPGTGKTLLAKATAGEANVP---FITVNGSEFLE--------------MFVGVGPARVRDMFAMARKHAPCI 269
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526291   270 LFIDEIDAIGRKRgrghlggqSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPgRFDRQIYIGPPD 345
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
192-341 1.42e-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: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 192 FLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEflemfVGVGPARVRDMFAMARKHApcILF 271
Cdd:cd19510    8 FIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS--IIL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755526291 272 IDEIDA---IGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
Cdd:cd19510   81 LEDIDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
175-341 1.08e-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: 78.00  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 175 DVAGCEEAKLEIMEFVNF-LKNPKQYQDLgAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPA 253
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 254 RVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQentlNQMLVEMDGFNSST--NVVVLAGTNRPDILDPALTR 331
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQ----VELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
                        170
                 ....*....|
gi 755526291 332 pgRFDRQIYI 341
Cdd:cd19523  156 --YFSKRLLV 163
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
202-341 3.09e-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: 3.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 202 LGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFL--------------EMFVGVGPARVRDMFAMARKHAP 267
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755526291 268 CILFIDEIDAIGRKRgrghLGGQSEQENT--LNQML--VEMDGFNSST-NVVVLAGTNRPDILDPALTRPGRFDRQIYI 341
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 ...
374-413 1.29e-11

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: 59.47  E-value: 1.29e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 755526291  374 KLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQ 413
Cdd:pfam17862   6 ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK04195 PRK04195
replication factor C large subunit; Provisional
172-292 1.99e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 63.40  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 172 RFADVAGCEEAKLEIMEFV-NFLKNpkqyqdlgaKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEF-----LE 245
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755526291 246 MFVGVGpARVRDMFAMARKhapcILFIDEIDAIgrkRGRGHLGGQSE 292
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 ...
211-339 3.70e-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: 58.69  E-value: 3.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 211 MLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMfvGV-GPARVRDMFAMARK-HAPCILFIDEIDAIGRKRGRGHLg 288
Cdd:cd19512   26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEKI- 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755526291 289 gQSEQENTLNQMLVEMdGFNSSTNVVVLAgTNRPDILDPALTrpGRFDRQI 339
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 ...
206-286 5.40e-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: 58.93  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 206 IPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEM-FVGvgparvRDMFAMARKHAPCILFIDEIDAI-GRKRG 283
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIaKRGGS 118

                 ...
gi 755526291 284 RGH 286
Cdd:cd19498  119 SGP 121
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
212-275 3.92e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 59.33  E-value: 3.92e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755526291 212 LTGPPGTGKTLLAKATAGEANVPFITVNGSeflemFVGVgpARVRDMFAMARKHA----PCILFIDEI 275
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
214-275 5.65e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.91  E-value: 5.65e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526291 214 GPPGTGKTLLAKATAGEANVPFITVNGSeflemFVGVgpARVRDMFAMARKHA----PCILFIDEI 275
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
211-278 8.33e-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: 55.28  E-value: 8.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  211 MLTGPPGTGKTLLAKATAGEANV---PFITVNGSEFLE-----MFVGVGPARVR-----DMFAMARKHAPCILFIDEIDA 277
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIEK 86

                  .
gi 755526291  278 I 278
Cdd:pfam07724  87 A 87
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
207-418 4.78e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 52.54  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 207 PKGAMLTGPPGTGKTLLAKATAGEA---------NVPFITVN----GSEF------LEMFV--------GVGPARVRDMF 259
Cdd:COG1474   51 PSNVLIYGPTGTGKTAVAKYVLEELeeeaeergvDVRVVYVNcrqaSTRYrvlsriLEELGsgedipstGLSTDELFDRL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 260 --AMARKHAPCILFIDEIDAIGRKRGrghlggqseqENTLNQmLVEMDGFNSSTNVVVLAGTNRPDI---LDP-ALTRPG 333
Cdd:COG1474  131 yeALDERDGVLVVVLDEIDYLVDDEG----------DDLLYQ-LLRANEELEGARVGVIGISNDLEFlenLDPrVKSSLG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 334 ----RFDR----QIYigppDI-KGRSSI-FKvhlrplklDGSLSKDALsRKLAALTPGFTG-A----DISNVcneAALIA 398
Cdd:COG1474  200 eeeiVFPPydadELR----DIlEDRAELaFY--------DGVLSDEVI-PLIAALAAQEHGdArkaiDLLRV---AGEIA 263
                        250       260
                 ....*....|....*....|
gi 755526291 399 ARHLSPSVQERHFEQAIERV 418
Cdd:COG1474  264 EREGSDRVTEEHVREAREKI 283
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
211-335 2.02e-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: 47.67  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  211 MLTGPPGTGKTLLAKATAgEA--NVPFITVNGSEFLE-------MFVGVGPARVRD---MFAMARKHapcILFIDEIDai 278
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgplVRAAREGE---IAVLDEIN-- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  279 grkrgRGHlggqSEQENTLNQMLVE-----MDGFN----SSTNVVVLAGTNRPDI----LDPALTRpgRF 335
Cdd:pfam07728  77 -----RAN----PDVLNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
211-341 3.14e-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: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 211 MLTGPPGTGKTLLAKATAGEANV---------PFITVNGSEFLEMFVGVGPARVRDMFA-----MARKHAPCILFIDEID 276
Cdd:cd19508   56 LLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEVE 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526291 277 AIGRKRGRGHLGGQ-SEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTrpGRFDRQIYI 341
Cdd:cd19508  136 SLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
174-280 4.63e-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: 47.55  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 174 ADVAGCEEAKLEIMEF--VNFLKNpkqyqDLGAKIpkgAMLTGPPGTGKTLLAKATAGEANVPF--ITVNG-SEFLEM-- 246
Cdd:cd19500   10 ADHYGLEDVKERILEYlaVRKLKG-----SMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvRDEAEIrg 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755526291 247 ----FVGVGPARVRDMFAMARKHAPCILfIDEIDAIGR 280
Cdd:cd19500   82 hrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
185-418 5.70e-06

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 48.41  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 185 EIMEFVNFLKNpkqYQDLGakipkgaMLTGPPGTGKTLLAKATAGE-ANVPFITVNGS----EFL-----EMFVGVGPAR 254
Cdd:COG2842   38 RFAEALDEARA---LPGIG-------VVYGESGVGKTTAAREYANRnPNVIYVTASPSwtskELLeelaeELGIPAPPGT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 255 VRDMFAMARKH-APCI--LFIDEIDaigrkrgrgHLGGqseqentlnQMLVEMDGFNSSTNV-VVLAGTNRpdiLDPALT 330
Cdd:COG2842  108 IADLRDRILERlAGTGrlLIIDEAD---------HLKP---------KALEELRDIHDETGVgVVLIGMER---LPAKLK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 331 RPGRFDRQIYigppdikgrssiFKVHLRPLKLD---------GSLSKDALSRKLAALTPGFTGAdISNVCNEAALIAARH 401
Cdd:COG2842  167 RYEQLYSRIG------------FWVEFKPLSLEdvralaeawGELTDPDLLELLHRITRGNLRR-LDRTLRLAARAAKRN 233
                        250
                 ....*....|....*..
gi 755526291 402 LSPSVQERHFEQAIERV 418
Cdd:COG2842  234 GLTKITLDHVRAAALML 250
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
208-243 1.06e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.43  E-value: 1.06e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 755526291 208 KGAMLTGPPGTGKTLLAKATAGE--ANVPFITVNGSEF 243
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
179-275 2.07e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.46  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 179 CEEAKLEIMEFVNFLKNPKQyqdlgakipkgAMLTGPPGTGKT----LLAKATAGEA--NVPFITVN----GSEFLEMFV 248
Cdd:COG1401  204 REKFEETLEAFLAALKTKKN-----------VILAGPPGTGKTylarRLAEALGGEDngRIEFVQFHpswsYEDFLLGYR 272
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755526291 249 ---GVGPARVRD-MF------AMARKHAPCILFIDEI 275
Cdd:COG1401  273 pslDEGKYEPTPgIFlrfclkAEKNPDKPYVLIIDEI 309
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
16-107 2.07e-05

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 43.75  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291   16 LAVLGAGVAAGFLYFYF---RDPGKEITWKHFVQyYLARGLVDRLEVVNKQFVRVIPVPGTTSER-----FVWFNIGSVD 87
Cdd:pfam06480   3 LWLLILLVLLLLFLLFLlssSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGskfttYFIPSLPNVD 81
                          90       100
                  ....*....|....*....|
gi 755526291   88 TFERNLESAQWELGIEPTNQ 107
Cdd:pfam06480  82 SLLEKLEDALEEKGVKVSVK 101
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
211-276 3.43e-05

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.86  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 211 MLTGPPGTGKTLLAKATA-----GEANvpFITVNGSEFLEMF-----VGVGPARV----RDMFAMA-RKHAPCILFIDEI 275
Cdd:cd19499   45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVgyteGGQLTEAvRRKPYSVVLLDEI 122

                 .
gi 755526291 276 D 276
Cdd:cd19499  123 E 123
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
211-326 4.73e-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: 43.26  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 211 MLTGPPGTGKTLLAKATAGEA---NVPFITVngsEFLEMFVgvgpARVRDmfaMARKHAPCILFIDEIDAIGRKRGRGhl 287
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFI---SFLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARASQGD-- 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755526291 288 ggqsEQENTLNQMLVEMDGFNsSTNVVVLAGTNRPDILD 326
Cdd:cd01120   70 ----RSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
AAA_22 pfam13401
AAA domain;
211-326 7.19e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 43.10  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  211 MLTGPPGTGKTLLAK---ATAGEANVPFITVN------GSEFLEMFV------GVGPARVRDMFAM-----ARKHAPCIL 270
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVDlpsgtsPKDLLRALLralglpLSGRLSKEELLAAlqqllLALAVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755526291  271 FIDEIDAIgrkrgrghlggqseQENTLNQmLVEMDGFNSSTNVVVLAGTnrPDILD 326
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 ...
208-246 7.93e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 7.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 755526291  208 KGAMLTGPPGTGKTLLAKATAGE--ANVPFITVNGSEF--LEM 246
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 ...
193-281 1.15e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 44.13  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 193 LKNPKQYQDLGAKIPKGAM-LTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEM-FVG--VGPARVR----DMFAMARK 264
Cdd:cd19497   35 IRNNLKQKDDDVELEKSNIlLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKllqaADYDVERA 114
                         90
                 ....*....|....*..
gi 755526291 265 HAPcILFIDEIDAIGRK 281
Cdd:cd19497  115 QRG-IVYIDEIDKIARK 130
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
205-277 1.17e-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: 43.00  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 205 KIPKGAM--LTGPPGTGKTLLAKATAGEANVP--FITVNGSEFLEMFVGVGPARV----------RDMFAMARK--HAPC 268
Cdd:cd00267   21 TLKAGEIvaLVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100

                 ....*....
gi 755526291 269 ILFIDEIDA 277
Cdd:cd00267  101 LLLLDEPTS 109
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
211-281 1.30e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.76  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 211 MLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEM-FVGvgparvRDMFAMARK--HApC----------ILFIDEIDA 277
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVG------EDVENILLKllQA-AdydvekaqrgIVYIDEIDK 184

                 ....
gi 755526291 278 IGRK 281
Cdd:PRK05342 185 IARK 188
44 PHA02544
clamp loader, small subunit; Provisional
205-293 2.35e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.83  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 205 KIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEflemfVGVGPARVR-DMFA--MARKHAPCILFIDEIDAIGRK 281
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD-----CRIDFVRNRlTRFAstVSLTGGGKVIIIDEFDRLGLA 115
                         90
                 ....*....|..
gi 755526291 282 RGRGHLGGQSEQ 293
Cdd:PHA02544 116 DAQRHLRSFMEA 127
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
211-275 5.33e-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: 40.95  E-value: 5.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755526291  211 MLTGPPGTGKTLLAKATAGEANVPF-ITvngseflemfvgVGPA--RVRDMFAMARKHAPC-ILFIDEI 275
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIrIT------------SGPAieRPGDLAAILTNLEPGdVLFIDEI 93
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
212-280 1.59e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.27  E-value: 1.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755526291 212 LTGPPGTGKTLLAKATAGEANVPFITVNGseflemfvgvgPA--RVRDMFAM---ARKHApcILFIDEIDAIGR 280
Cdd:PRK00080  56 LYGPPGLGKTTLANIIANEMGVNIRITSG-----------PAleKPGDLAAIltnLEEGD--VLFIDEIHRLSP 116
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
212-276 2.69e-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: 40.15  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291 212 LTGPPGTGKTLLAKATAGEANVPFITVNGSE----------------FLEMFVGVGPArvrdmFAmarkhapCILFIDEI 275
Cdd:COG0714   36 LEGVPGVGKTTLAKALARALGLPFIRIQFTPdllpsdilgtyiydqqTGEFEFRPGPL-----FA-------NVLLADEI 103

                 .
gi 755526291 276 D 276
Cdd:COG0714  104 N 104
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
203-280 5.36e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.21  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526291  203 GAKIPKGA----MLTGPPGTGKTLLAKATAGEANVpfitvngseflEMFVGVGPA--RVRDMFAMA---RKHApcILFID 273
Cdd:TIGR00635  22 AAKMRQEAldhlLLYGPPGLGKTTLAHIIANEMGV-----------NLKITSGPAleKPGDLAAILtnlEEGD--VLFID 88

                  ....*..
gi 755526291  274 EIDAIGR 280
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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