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Conserved domains on  [gi|523412962|ref|WP_020748284|]
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MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Ralstonia solanacearum species complex]

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];
15-593 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1072.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  15 IALVLFTVFKQFDKPRAQ-EGVTYSQFMDDAKGGKIKRVEVQGRNLLVTPSEGSK--YTIISPGDIWMVGDLMKYGVQVT 91
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSvKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKtrFTTYRVNDPELVDLLEEKGVEVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  92 GKAEEEQGVLLSALYYLGPTLLIIVFWFYMMRQMQGGGkGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVVELVD 171
Cdd:COG0465   81 AKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGG-GGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 172 FLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVF 251
Cdd:COG0465  160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 252 IDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQ 331
Cdd:COG0465  240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 332 ILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIREEERR 411
Cdd:COG0465  320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 412 ATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLGAMSTGASN 491
Cdd:COG0465  400 ITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASN 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 492 DFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLEENREKV 569
Cdd:COG0465  480 DLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRdiGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKL 559
                        570       580
                 ....*....|....*....|....
gi 523412962 570 EAMTAALLEWETIDADQVNDIMAG 593
Cdd:COG0465  560 DALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
15-593 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1072.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  15 IALVLFTVFKQFDKPRAQ-EGVTYSQFMDDAKGGKIKRVEVQGRNLLVTPSEGSK--YTIISPGDIWMVGDLMKYGVQVT 91
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSvKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKtrFTTYRVNDPELVDLLEEKGVEVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  92 GKAEEEQGVLLSALYYLGPTLLIIVFWFYMMRQMQGGGkGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVVELVD 171
Cdd:COG0465   81 AKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGG-GGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 172 FLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVF 251
Cdd:COG0465  160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 252 IDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQ 331
Cdd:COG0465  240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 332 ILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIREEERR 411
Cdd:COG0465  320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 412 ATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLGAMSTGASN 491
Cdd:COG0465  400 ITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASN 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 492 DFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLEENREKV 569
Cdd:COG0465  480 DLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRdiGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKL 559
                        570       580
                 ....*....|....*....|....
gi 523412962 570 EAMTAALLEWETIDADQVNDIMAG 593
Cdd:COG0465  560 DALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
101-592 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: 839.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  101 LLSALYYLGPTLLIIVF-WFYMMRQMQGGGkGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVVELVDFLKDPQKF 179
Cdd:TIGR01241   2 LLGFLFSLLPPILLLVGvWFFFRRQMQGGG-GRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  180 QKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVG 259
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  260 RHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQILKVHMRK 339
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  340 VPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIREEERRATAYHESG 419
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  420 HAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLGAMSTGASNDFERATKM 499
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  500 ARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLEENREKVEAMTAALL 577
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 523412962  578 EWETIDADQVNDIMA 592
Cdd:TIGR01241 481 EKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
11-627 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 775.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  11 IWLVIALVLFTVFKQFDkPRAQEG--VTYSQFMDDAKGGKIKRVEVQGRNLLVTPSEGSKYTIISP-GDIWMVGDLMKYG 87
Cdd:PRK10733   7 LWLVIAVVLMSVFQSFG-PSESNGrkVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPvNDPKLLDNLLTKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  88 VQVTGKAEEEQGVLLSALYYLGPTLLIIVFWFYMMRQMQGGGKGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVV 167
Cdd:PRK10733  86 VKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 168 ELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAP 247
Cdd:PRK10733 166 ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 248 CIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIR 327
Cdd:PRK10733 246 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVR 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 328 GREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIRE 407
Cdd:PRK10733 326 GREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTE 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 408 EERRATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLG--AM 485
Cdd:PRK10733 406 AQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGpeHV 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 486 STGASNDFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLE 563
Cdd:PRK10733 486 STGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRsvAKAKHMSDETARIIDQEVKALIERNYNRARQLLT 565
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523412962 564 ENREKVEAMTAALLEWETIDADQVNDIMAGKPPRPPR-YGSSGGGSTPPNGGTPAGVTPGNVPAT 627
Cdd:PRK10733 566 DNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAgWEEPGASNNSDDNGTPKAPRPVDEPRT 630
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
151-321 4.94e-128

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: 373.88  E-value: 4.94e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 151 VTFADVAGCDESKEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 231 GAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALL 310
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 523412962 311 RPGRFDRQVYV 321
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
403-590 1.63e-85

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 265.23  E-value: 1.63e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  403 AVIREEERRATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFL 482
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  483 GAMSTGASNDFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKR 560
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 523412962  561 LLEENREKVEAMTAALLEWETIDADQVNDI 590
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
187-325 1.72e-22

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 93.98  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962   187 PRGVLLVGPPGTGKTLLARAIAGEAKVP---FFSISGSDFVE--------------MFVGVGAARVRDMFENAKKQAPCI 249
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523412962   250 VFIDEIDAVGRHRGagmgggndEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPgRFDRQVYVGLPD 325
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
190-225 1.68e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.53  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEA-----KVPFFSIsgSDFVE 225
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
15-593 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1072.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  15 IALVLFTVFKQFDKPRAQ-EGVTYSQFMDDAKGGKIKRVEVQGRNLLVTPSEGSK--YTIISPGDIWMVGDLMKYGVQVT 91
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSvKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKtrFTTYRVNDPELVDLLEEKGVEVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  92 GKAEEEQGVLLSALYYLGPTLLIIVFWFYMMRQMQGGGkGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVVELVD 171
Cdd:COG0465   81 AKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGG-GGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQEIVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 172 FLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVF 251
Cdd:COG0465  160 FLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 252 IDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQ 331
Cdd:COG0465  240 IDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 332 ILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIREEERR 411
Cdd:COG0465  320 ILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKK 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 412 ATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLGAMSTGASN 491
Cdd:COG0465  400 ITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASN 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 492 DFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLEENREKV 569
Cdd:COG0465  480 DLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRdiGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKL 559
                        570       580
                 ....*....|....*....|....
gi 523412962 570 EAMTAALLEWETIDADQVNDIMAG 593
Cdd:COG0465  560 DALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
101-592 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: 839.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  101 LLSALYYLGPTLLIIVF-WFYMMRQMQGGGkGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVVELVDFLKDPQKF 179
Cdd:TIGR01241   2 LLGFLFSLLPPILLLVGvWFFFRRQMQGGG-GRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  180 QKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVG 259
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  260 RHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQILKVHMRK 339
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  340 VPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIREEERRATAYHESG 419
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  420 HAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLGAMSTGASNDFERATKM 499
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  500 ARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLEENREKVEAMTAALL 577
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 523412962  578 EWETIDADQVNDIMA 592
Cdd:TIGR01241 481 EKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
11-627 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 775.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  11 IWLVIALVLFTVFKQFDkPRAQEG--VTYSQFMDDAKGGKIKRVEVQGRNLLVTPSEGSKYTIISP-GDIWMVGDLMKYG 87
Cdd:PRK10733   7 LWLVIAVVLMSVFQSFG-PSESNGrkVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIPvNDPKLLDNLLTKN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  88 VQVTGKAEEEQGVLLSALYYLGPTLLIIVFWFYMMRQMQGGGKGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVV 167
Cdd:PRK10733  86 VKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 168 ELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAP 247
Cdd:PRK10733 166 ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 248 CIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIR 327
Cdd:PRK10733 246 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVR 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 328 GREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPERKSAVIRE 407
Cdd:PRK10733 326 GREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTE 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 408 EERRATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLG--AM 485
Cdd:PRK10733 406 AQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGpeHV 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 486 STGASNDFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLE 563
Cdd:PRK10733 486 STGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRsvAKAKHMSDETARIIDQEVKALIERNYNRARQLLT 565
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523412962 564 ENREKVEAMTAALLEWETIDADQVNDIMAGKPPRPPR-YGSSGGGSTPPNGGTPAGVTPGNVPAT 627
Cdd:PRK10733 566 DNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAgWEEPGASNNSDDNGTPKAPRPVDEPRT 630
ftsH CHL00176
cell division protein; Validated
1-600 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 616.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962   1 MNNNWFQKAAIWLVIALVLFTVFKQFD-----------------KPRAQEGVTYSQFMDDAKGGKIKRVEV--QGRNLLV 61
Cdd:CHL00176   1 MKEQSKYAILISLPLIVEKFTVWDVFYyssvedglkspnnpdvvQNKASSRMTYGRFLEYLDMGWIKKVDLydNGRTAIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  62 TpsegskytIISP--GDIW-------------MVGDLMKYGVQVTGKAEEEQGVLLSAL-YYLGPTLLIIVFWFYMMR-- 123
Cdd:CHL00176  81 E--------ASSPelGNRPqrirvelpvgaseLIQKLKEANIDFDAHPPVLKSNIVTILsNLLLPLILIGVLWFFFQRss 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 124 QMQGGGKGGAFSFGKSRARLIDENNNSVTFADVAGCDESKEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLL 203
Cdd:CHL00176 153 NFKGGPGQNLMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 204 ARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVE 283
Cdd:CHL00176 233 AKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 284 MDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADL 363
Cdd:CHL00176 313 MDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADL 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 364 ANLVNEAALFAARRNKRVVDMQDFEDAKDKIYMGPErKSAVIREEERRATAYHESGHAVVAKLLPKADPVHKVTIMPRGW 443
Cdd:CHL00176 393 ANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQ 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 444 AGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFLGAMS--TGASNDFERATKMARDMVTRYGMSdSLGTMVYVDT 521
Cdd:CHL00176 472 AKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEvtTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESN 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 522 -EQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKRLLEENREKVEAMTAALLEWETIDADQVNDIMAGKPPRP 598
Cdd:CHL00176 551 nSTDPFLGRfmQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILP 630

                 ..
gi 523412962 599 PR 600
Cdd:CHL00176 631 PK 632
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
151-321 4.94e-128

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: 373.88  E-value: 4.94e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 151 VTFADVAGCDESKEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 231 GAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALL 310
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 523412962 311 RPGRFDRQVYV 321
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
150-394 1.21e-117

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 353.16  E-value: 1.21e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 150 SVTFADVAGCDESKEEVVELV-DFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 229 GVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGndEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKA 308
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 309 LLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFE 388
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLE 311

                 ....*.
gi 523412962 389 DAKDKI 394
Cdd:COG1222  312 KAIEKV 317
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
150-409 1.15e-102

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 317.16  E-value: 1.15e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 150 SVTFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 229 GVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKA 308
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 309 LLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFE 388
Cdd:PRK03992 287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFL 366
                        250       260
                 ....*....|....*....|.
gi 523412962 389 DAKDKIyMGPERKSAVIREEE 409
Cdd:PRK03992 367 KAIEKV-MGKEEKDSMEEPGV 386
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
144-394 6.18e-86

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: 272.83  E-value: 6.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  144 IDENNNsVTFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSD 222
Cdd:TIGR01242 113 VEERPN-VSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  223 FVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRA 302
Cdd:TIGR01242 192 LVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRP 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  303 DVLDKALLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVV 382
Cdd:TIGR01242 272 DILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYV 351
                         250
                  ....*....|..
gi 523412962  383 DMQDFEDAKDKI 394
Cdd:TIGR01242 352 TMDDFIKAVEKV 363
Peptidase_M41 pfam01434
Peptidase family M41;
403-590 1.63e-85

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 265.23  E-value: 1.63e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  403 AVIREEERRATAYHESGHAVVAKLLPKADPVHKVTIMPRGWAGGLTWQLPEHDKHYAYKDTMLEEIAILFGGRAAEEVFL 482
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  483 GAMSTGASNDFERATKMARDMVTRYGMSDSLGTMVYVDTEQDGFFGR--MSSKTVSEATQQKVDSEIRRIVDEQYTLAKR 560
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 523412962  561 LLEENREKVEAMTAALLEWETIDADQVNDI 590
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
153-390 3.65e-82

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: 264.08  E-value: 3.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 153 FADVAGCDESKEEVVELVD-FLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVG 231
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 232 AARVRDMFENAKKQAPCIVFIDEIDAVGRHRGaGMGGGNDEREqtLNQMLVEMDGFEanSGVIVIAATNRADVLDKALLR 311
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELR--SDVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962 312 pgRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDA 390
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEA 387
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
150-415 4.05e-74

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: 252.14  E-value: 4.05e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  150 SVTFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  229 GVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEReqTLNQMLVEMDGFEANSGVIVIAATNRADVLDKA 308
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  309 LLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARR----------- 377
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigspakekle 686
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 523412962  378 -------NKRVVDMQDFEDAKDKIymGPERKSAVIREEERRATAY 415
Cdd:TIGR01243 687 vgeeeflKDLKVEMRHFLEALKKV--KPSVSKEDMLRYERLAKEL 729
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
152-321 2.19e-65

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: 212.20  E-value: 2.19e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 152 TFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 231 GAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALL 310
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 523412962 311 RPGRFDRQVYV 321
Cdd:cd19502  161 RPGRFDRKIEF 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
150-415 4.32e-65

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 219.25  E-value: 4.32e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 150 SVTFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFV 228
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 229 GVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKA 308
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 309 LLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFE 388
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFE 380
                        250       260
                 ....*....|....*....|....*..
gi 523412962 389 DAkdkiymgperKSAVIREEERRATAY 415
Cdd:PTZ00454 381 KG----------YKTVVRKTDRDYDFY 397
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
163-321 1.17e-64

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: 209.45  E-value: 1.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 163 KEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENA 242
Cdd:cd19481    2 KASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962 243 KKQAPCIVFIDEIDAVGRHRGAgmGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19481   82 RRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
153-394 4.87e-64

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 211.28  E-value: 4.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 153 FADVAGCDESKEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGA 232
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 233 ARVRDMFENAkKQAPCIVFIDEIDAVGRHRGAGMGGGndEREQTLNQMLVEMDGFeaNSGVIVIAATNRADVLDKALLRp 312
Cdd:COG1223   81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 313 gRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDAKD 392
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 ..
gi 523412962 393 KI 394
Cdd:COG1223  234 QR 235
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
151-377 5.11e-64

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: 224.40  E-value: 5.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  151 VTFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVG 229
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  230 VGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGggnDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKAL 309
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523412962  310 LRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARR 377
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
163-321 8.65e-61

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: 199.43  E-value: 8.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 163 KEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19511    2 KRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 242 AKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEReqTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19511   82 ARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
152-394 8.99e-61

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 208.86  E-value: 8.99e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 152 TFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 231 GAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALL 310
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 311 RPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFEDA 390
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                 ....
gi 523412962 391 KDKI 394
Cdd:PTZ00361 421 KEKV 424
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
190-323 8.50e-57

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: 187.80  E-value: 8.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGagmGGG 269
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 523412962  270 NDEREQTLNQMLVEMDGFEAN-SGVIVIAATNRADVLDKALLrpGRFDRQVYVGL 323
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
155-321 4.45e-56

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: 187.11  E-value: 4.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 234 RVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGmGGGNDEReqTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPG 313
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*...
gi 523412962 314 RFDRQVYV 321
Cdd:cd19503  158 RFDREVEI 165
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
163-321 2.78e-55

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: 185.02  E-value: 2.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 163 KEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 242 AKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
163-321 2.16e-53

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: 180.00  E-value: 2.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 163 KEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19529    2 KQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 242 AKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEReqTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19529   82 ARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
155-322 2.64e-50

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: 171.85  E-value: 2.64e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 234 RVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGggnDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPG 313
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHG---EVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 523412962 314 RFDRQVYVG 322
Cdd:cd19519  158 RFDREIDIG 166
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
155-319 4.51e-49

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: 168.74  E-value: 4.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVVELVDFLKDPQK-FQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 234 RVRDMFENAKKQAPCIVFIDEIDAVGRHRgagMGGGNDEREQTLNQMLVEMDGFEANS----GVIVIAATNRADVLDKAL 309
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR---ESAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 523412962 310 LRPGRFDRQV 319
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
173-321 4.19e-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: 165.74  E-value: 4.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 173 LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFI 252
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962 253 DEIDAVGRHRGagmGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19530   96 DEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
164-320 4.09e-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: 4.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 164 EEVVELVDflKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAK 243
Cdd:cd19526    6 EETIEWPS--KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQ 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 244 KQAPCIVFIDEIDAVGRHRGAGMGGGNDereQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVY 320
Cdd:cd19526   84 SAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
163-321 2.44e-42

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: 149.97  E-value: 2.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 163 KEEVVELVDF-LKDPQKFQKlGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFEN 241
Cdd:cd19527    2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 242 AKKQAPCIVFIDEIDAVGRHRGA-GMGGGNDEReqTLNQMLVEMDGFE-ANSGVIVIAATNRADVLDKALLRPGRFDRQV 319
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 523412962 320 YV 321
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 ...
156-321 2.00e-40

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: 144.80  E-value: 2.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 156 VAGCDESKEEVVELVDF-LKDPQKFqKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAAR 234
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 235 VRDMFENAKKQAPCIVFIDEIDAVGRHRGAgmggGNDEREQTL-NQMLVEMDGFEA--NSGVIVIAATNRADVLDKALLR 311
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVLNkpEDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 523412962 312 pgRFDRQVYV 321
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
150-321 4.85e-37

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 135.76  E-value: 4.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 150 SVTFADVAGCDESKEEVVELVDF-LKDPQKFQklGGRIP-RGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMF 227
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 228 VGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMgggNDEREQTLNQMLVEMDGFEANS-GVIVIAATNRADVLD 306
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGE---SEASRRIKTELLVQMNGVGNDSqGVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 523412962 307 KALLRpgRFDRQVYV 321
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
155-320 2.37e-35

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: 131.09  E-value: 2.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVVELVDF-LKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIA-----GEAKVPFFSISGSDFVEMFV 228
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 229 GVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAgmgggndEREQT----LNQMLVEMDGFEANSGVIVIAATNRADV 304
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....*.
gi 523412962 305 LDKALLRPGRFDRQVY 320
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; ...
144-321 4.69e-33

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: 125.10  E-value: 4.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 144 IDENNNSVTFADVAGCDESKEEVVELVDF-LKDPQKFQKLGGRiPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSD 222
Cdd:cd19525   12 IMDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 223 FVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMgggNDEREQTLNQMLVEMDGFEANSG--VIVIAATN 300
Cdd:cd19525   91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE---HESSRRIKTEFLVQLDGATTSSEdrILVVGATN 167
                        170       180
                 ....*....|....*....|.
gi 523412962 301 RADVLDKALLRpgRFDRQVYV 321
Cdd:cd19525  168 RPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
155-321 7.53e-32

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: 121.11  E-value: 7.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVVELVDFLKD-PQKFQKLGgRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLrPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 234 RVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMgggNDEREQTLNQMLVEMDGFEANSG--VIVIAATNRADVLDKALLR 311
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGE---HEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 523412962 312 pgRFDRQVYV 321
Cdd:cd19524  157 --RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
185-323 1.23e-30

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: 117.25  E-value: 1.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 185 RIPRGVLLVGPPGTGKTLLARAIAGEA---KVPFFSISGSDFVEMFVG---VGAARVRDMFENAKKQAPCIVFIDEIDAV 258
Cdd:cd00009   17 PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSL 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523412962 259 GRhrgagmgggnDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGL 323
Cdd:cd00009   97 SR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
155-315 1.46e-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: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVVELVDF-LKDPQKFQKlgGRI---PRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDN--SRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 231 GAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGmgggndEREQTL---NQMLVEMDGF--EANSGVIVIAATNRADVL 305
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLstDGNCRVIVMGATNRPQDL 152
                        170
                 ....*....|..
gi 523412962 306 DKALLR--PGRF 315
Cdd:cd19520  153 DEAILRrmPKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
176-321 1.64e-30

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 117.98  E-value: 1.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 176 PQKFQKLGGRIPRGVLLVGPPGTGKTLLARAI-----AGEAKVpffsISGSDFVEMFVGVGAARVRDMFENAKKQAPC-- 248
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962 249 ------IVFIDEIDAVGRHRGAgMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGS-MAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
155-321 3.00e-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: 117.01  E-value: 3.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESK---EEVVELVDFLkdPQKFQklGGRIP-RGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGV 230
Cdd:cd19522    1 DIADLEEAKkllEEAVVLPMWM--PEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 231 GAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAgmGGGNDEREQTLNQMLVEMDGF-------EANSGVIVIAATNRAD 303
Cdd:cd19522   77 SEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPW 154
                        170
                 ....*....|....*...
gi 523412962 304 VLDKALLRpgRFDRQVYV 321
Cdd:cd19522  155 DIDEALRR--RLEKRIYI 170
ycf46 CHL00195
Ycf46; Provisional
150-386 1.41e-29

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 122.44  E-value: 1.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 150 SVTFADVAGCDESKeevvelvDFLKD-----PQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSIsgsDFV 224
Cdd:CHL00195 224 NEKISDIGGLDNLK-------DWLKKrstsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVG 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 225 EMF---VGVGAARVRDMFENAKKQAPCIVFIDEID-AVGRHRGAGMGGgndereqTLNQMLVEMDGF--EANSGVIVIAA 298
Cdd:CHL00195 294 KLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLATFITWlsEKKSPVFVVAT 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 299 TNRADVLDKALLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIG--NDVDASVLARGTPGFSGADLANLVNEaALFAAR 376
Cdd:CHL00195 367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIE-AMYIAF 445
                        250
                 ....*....|
gi 523412962 377 RNKRVVDMQD 386
Cdd:CHL00195 446 YEKREFTTDD 455
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
187-325 1.72e-22

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 93.98  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962   187 PRGVLLVGPPGTGKTLLARAIAGEAKVP---FFSISGSDFVE--------------MFVGVGAARVRDMFENAKKQAPCI 249
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523412962   250 VFIDEIDAVGRHRGagmgggndEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPgRFDRQVYVGLPD 325
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
186-321 3.67e-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: 3.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 186 IPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEID-AVGRHRGA 264
Cdd:cd19507   30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSK 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 265 GMGGGNderEQTLNQMLVEMDgfEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19507  110 GDSGTS---SRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
168-321 2.33e-21

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 90.87  E-value: 2.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 168 ELVDFLKDPQKFQKLGgrIP--RGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDfvemfVGVGAARVRDMFENAKKQ 245
Cdd:cd19510    4 DLKDFIKNEDWYNDRG--IPyrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962 246 ApcIVFIDEIDAV---GRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYV 321
Cdd:cd19510   77 S--IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
155-321 1.25e-19

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: 86.09  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 155 DVAGCDESKEEVV-ELVDFLKDPQKFQKLGgRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAA 233
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 234 RVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNdeREQTlnQMLVEMDGF--EANSGVIVIAATNRADVLDKALLR 311
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
                        170
                 ....*....|
gi 523412962 312 pgRFDRQVYV 321
Cdd:cd19523  156 --YFSKRLLV 163
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
345-389 9.75e-14

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: 65.64  E-value: 9.75e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 523412962  345 DVDASVLARGTPGFSGADLANLVNEAALFAARRNKRVVDMQDFED 389
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
190-262 1.39e-11

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 66.65  E-value: 1.39e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFvemfvgvGAARVRDMFENAKKQA----PCIVFIDEIdavgrHR 262
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDEI-----HR 103
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
190-262 1.65e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 66.62  E-value: 1.65e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISGsdfvemfVGVGAARVRDMFENAKKQA----PCIVFIDEIdavgrHR 262
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI-----HR 116
PRK04195 PRK04195
replication factor C large subunit; Provisional
152-268 7.96e-11

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 64.56  E-value: 7.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 152 TFADVAGCDESKEEVVELVDflkdpqKFQKlgGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDF-----VEM 226
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE------SWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 523412962 227 FVGvGAARVRDMFENAKKqapcIVFIDEIDavGRHRGAGMGG 268
Cdd:PRK04195  84 VAG-EAATSGSLFGARRK----LILLDEVD--GIHGNEDRGG 118
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
181-317 8.47e-11

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 60.85  E-value: 8.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 181 KLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFV--------------EMFVGVGAARVRDMFENAKKQA 246
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523412962 247 PCIVFIDEIDAVGRHRGAGMGGGNdeREQTLNQMLVEM-DGFEANS--GVIVIAATNRADVLDKALLRPGRFDR 317
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEED--PKLLLGLLLNYLsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
188-319 1.36e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 57.15  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 188 RGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGvGAARVRDMFENAKK-QAPCIVFIDEIDAVGRHRgAGM 266
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-STE 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 523412962 267 GGGNDEReQTLNQMLVEMDgfEANSGVIVIAATNRADVLDKALlrPGRFDRQV 319
Cdd:cd19512  101 KISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
186-271 2.85e-09

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 57.00  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 186 IPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEM-FVGVGA-ARVRDMFENakkqapcIVFIDEIDAVGrhrG 263
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIA---K 114

                 ....*...
gi 523412962 264 AGMGGGND 271
Cdd:cd19498  115 RGGSSGPD 122
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
11-95 3.51e-09

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: 54.53  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962   11 IWLVIALVLFTVFKQFDKPRAQEG--VTYSQFMDDAKGGKIKRVEVQGRNLLVTP------SEGSKYTIISPGDIWMVGD 82
Cdd:pfam06480   3 LWLLILLVLLLLFLLFLLSSSSSTkeISYSEFLEYLEAGKVKKVVVQDDEILPTGvvegtlKDGSKFTTYFIPSLPNVDS 82
                          90       100
                  ....*....|....*....|.
gi 523412962   83 --------LMKYGVQVTGKAE 95
Cdd:pfam06480  83 llekledaLEEKGVKVSVKPP 103
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
189-315 1.59e-08

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 53.45  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  189 GVLLVGPPGTGKTLLARAIAgEA--KVPFFSISGSDFVE-------MFVGVGAARVRD--MFENAKKqaPCIVFIDEIDA 257
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEINR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523412962  258 VGRHRGAGMGGGNDEREqtlnqmLVEMDGFE----ANSGVIVIAATNRAD----VLDKALLRpgRF 315
Cdd:pfam07728  78 ANPDVLNSLLSLLDERR------LLLPDGGElvkaAPDGFRLIATMNPLDrglnELSPALRS--RF 135
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
144-223 1.69e-08

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 57.29  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 144 IDENNNSVTFAD-VAGCDESKEE---VVELVdflkdpqKFQKLGGRiprGVLLVGPPGTGKTLLARAIAGE--AKVPFFS 217
Cdd:COG1224   27 LDENGKAKFVADgLVGQVEAREAagiVVKMI-------KEGKMAGK---GILIVGPPGTGKTALAVAIARElgEDTPFVA 96

                 ....*.
gi 523412962 218 ISGSDF 223
Cdd:COG1224   97 ISGSEI 102
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
158-319 2.91e-08

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 56.78  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  158 GCDESKEEVVELVDFLKDPQKFQKLGGRIP---RGVLLVGPPGTGKTLLARAIA------GEAKVP-FFSISGSDFVEMF 227
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  228 VGVGAARVRDMFENAKKQapcIVFIDEIDA-VGRHRGAgmggGNDEREQTLNQMLVEM--DGFEansgVIVIAATNRADv 304
Cdd:TIGR03922 360 IGESEAKTNEIIDSALGG---VLFLDEAYTlVETGYGQ----KDPFGLEAIDTLLARMenDRDR----LVVIGAGYRKD- 427
                         170       180
                  ....*....|....*....|
gi 523412962  305 LDKAL-----LRpGRFDRQV 319
Cdd:TIGR03922 428 LDKFLevnegLR-SRFTRVI 446
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
188-321 3.14e-08

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 53.99  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 188 RGVLLVGPPGTGKTLLARAIAGEAKV---------------------PFFSISGSDFVEMFvgvgaARVRDMFENakKQA 246
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDD--KDA 125
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 247 PCIVFIDEIDAVGRHRGAgMGGGNDERE--QTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLrpGRFDRQVYV 321
Cdd:cd19508  126 LVFVLIDEVESLAAARSA-SSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
166-223 3.50e-08

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: 55.78  E-value: 3.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  166 VVELVdflkdpqKFQKLGGRiprGVLLVGPPGTGKTLLARAIAGE--AKVPFFSISGSDF 223
Cdd:pfam06068  39 IVEMI-------KEGKIAGR---AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
154-263 1.11e-07

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 52.18  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 154 ADVAGCDESKEEVVElvdFLKDPQKFQKLGGRIprgVLLVGPPGTGKTLLARAIAGEAKVPFFSIS-G--SDFVEM---- 226
Cdd:cd19500   10 ADHYGLEDVKERILE---YLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghr 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 523412962 227 --FVGVGAARVRDMFENAKKQAPCIVfIDEIDAVGR-HRG 263
Cdd:cd19500   84 rtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGSsFRG 122
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
190-296 1.52e-07

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: 50.19  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAK---VPFFSISgsdFVEMFVgvgaARVRDMFENAKkqaPCIVFIDEIDAVGRHRgagm 266
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALlsdEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARAS---- 66
                         90       100       110
                 ....*....|....*....|....*....|
gi 523412962 267 ggGNDEREQTLNQMLVEMDGFEANSGVIVI 296
Cdd:cd01120   67 --QGDRSSELLEDLAKLLRAARNTGITVIA 94
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
190-262 2.94e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.74  E-value: 2.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISG------SDFVEMFVGVGAarvRDmfenakkqapcIVFIDEIdavgrHR 262
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI-----HR 113
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
190-338 3.18e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 49.40  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPFF----------------SISGSDFVEMFVGVGAArvrdmFENakkqapcIVFID 253
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGPL-----FAN-------VLLAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 254 EIDavgrhRGagmgggndeREQTLNQML-------VEMDG--FEANSGVIVIAATNRADV-----LDKALLRpgRFDRQV 319
Cdd:COG0714  102 EIN-----RA---------PPKTQSALLeameerqVTIPGgtYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKL 165
                        170
                 ....*....|....*....
gi 523412962 320 YVGLPDIRGREQILKVHMR 338
Cdd:COG0714  166 YIGYPDAEEEREILRRHTG 184
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
164-406 7.84e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 48.69  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 164 EEVVELVDFLKDPqkfqkLGGRIPRGVLLVGPPGTGKTLLARAIAGEAK-------VPF-------------FSI----- 218
Cdd:COG1474   33 EEIEELASALRPA-----LRGERPSNVLIYGPTGTGKTAVAKYVLEELEeeaeergVDVrvvyvncrqastrYRVlsril 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 219 ----SGSDFVEmfVGVGAARVRDMFENA--KKQAPCIVFIDEIDAVGRhrgagmgggnDEREQTLNQmLVEMDGFEANSG 292
Cdd:COG1474  108 eelgSGEDIPS--TGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVD----------DEGDDLLYQ-LLRANEELEGAR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 293 VIVIAATNRADVLDkallrpgRFDRQV--YVGLPDIR----GREQILKVHMRKVPIG---NDVDASVLARgtpgfsGADL 363
Cdd:COG1474  175 VGVIGISNDLEFLE-------NLDPRVksSLGEEEIVfppyDADELRDILEDRAELAfydGVLSDEVIPL------IAAL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 523412962 364 A-----------NLVNEAALFAARRNKRVVDMQDFEDAKDKIYmgPERKSAVIR 406
Cdd:COG1474  242 AaqehgdarkaiDLLRVAGEIAEREGSDRVTEEHVREAREKIE--RDRLLEVLR 293
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
190-260 1.46e-05

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 46.82  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPfFSIS-----------GSDfVEMFVG--VGAArvrdMFENAKKQAPcIVFIDEID 256
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VENILLklLQAA----DYDVERAQRG-IVYIDEID 125

                 ....
gi 523412962 257 AVGR 260
Cdd:cd19497  126 KIAR 129
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
185-255 1.65e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.84  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 185 RIPRGVLLVGPPGTGKT----LLARAIAGEAK-----VPFF-SISGSDFVEMFV---GVGAARVRD-MF----ENAKKQ- 245
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpSWSYEDFLLGYRpslDEGKYEPTPgIFlrfcLKAEKNp 298
                         90
                 ....*....|.
gi 523412962 246 -APCIVFIDEI 255
Cdd:COG1401  299 dKPYVLIIDEI 309
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
184-257 2.52e-05

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 46.51  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 184 GRIPRGVLLVGPPGTGKTLLARAIA----GEAKVP-----------FFSISGSDFVEMFVGV-----GAARVRDMFENAK 243
Cdd:COG0470   15 GRLPHALLLHGPPGIGKTTLALALArdllCENPEGgkacgqchsrlMAAGNHPDLLELNPEEksdqiGIDQIRELGEFLS 94
                         90
                 ....*....|....*...
gi 523412962 244 K---QAPC-IVFIDEIDA 257
Cdd:COG0470   95 LtplEGGRkVVIIDEADA 112
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
190-256 3.94e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.49  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962  190 VLLVGPPGTGKTLLARAIAGE---AKVPFFSISGSDFVE-----MFVGVGAARVR-----DMFENAKKQAPCIVFIDEID 256
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
190-260 8.06e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 44.98  E-value: 8.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962  190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISG------SDFVEMFVGVgaarvrdmfenakkQAPCIVFIDEIDAVGR 260
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNL--------------EEGDVLFIDEIHRLSP 95
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
190-260 1.07e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.15  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPfFSIS-----------GSDfVEMFVG--VGAArvrDMfeNAKKQAPCIVFIDEID 256
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENILLklLQAA---DY--DVEKAQRGIVYIDEID 183

                 ....
gi 523412962 257 AVGR 260
Cdd:PRK05342 184 KIAR 187
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
190-260 1.88e-04

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 44.27  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPfFSIS-----------GSDfVEMFVgvgaarVR-------DMfENAKKQapcIVF 251
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKllqaadyDV-EKAERG---IIY 179

                 ....*....
gi 523412962 252 IDEIDAVGR 260
Cdd:COG1219  180 IDEIDKIAR 188
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
190-262 1.92e-04

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 42.10  E-value: 1.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523412962  190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISG------SDFVEMFVGVGAarvRDmfenakkqapcIVFIDEIdavgrHR 262
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpaierpGDLAAILTNLEP---GD-----------VLFIDEI-----HR 95
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
182-211 2.51e-04

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 42.98  E-value: 2.51e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 523412962 182 LGGRIPRG--VLLVGPPGTGKTLLARAIAGEA 211
Cdd:COG0467   13 LGGGLPRGssTLLSGPPGTGKTTLALQFLAEG 44
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
190-209 3.29e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.49  E-value: 3.29e-04
                         10        20
                 ....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAG 209
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
44 PHA02544
clamp loader, small subunit; Provisional
175-222 3.31e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.05  E-value: 3.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 523412962 175 DPQKFQKL--GGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSD 222
Cdd:PHA02544  29 DKETFKSIvkKGRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD 78
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
190-220 5.10e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.76  E-value: 5.10e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEAKVPFFSISG 220
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
186-311 7.13e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 40.69  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 186 IPRG--VLLVGPPGTGKTLLARAIAGEAKVPFFSI--SGSDFVEMFVGVGAARVRDMFE------------NAKKQAPCI 249
Cdd:cd00267   22 LKAGeiVALVGPNGSGKSTLLRAIAGLLKPTSGEIliDGKDIAKLPLEELRRRIGYVPQlsggqrqrvalaRALLLNPDL 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523412962 250 VFIDEI----DAVGRHRgagmgggndereqtLNQMLVEMdgfeANSGVIVIAATNRADVLDKALLR 311
Cdd:cd00267  102 LLLDEPtsglDPASRER--------------LLELLREL----AEEGRTVIIVTHDPELAELAADR 149
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
188-225 9.65e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 41.30  E-value: 9.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 523412962 188 RGVLLVGPPGTGKTLLARAIAGEA-----KVPFFSIsgSDFVE 225
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLVN 140
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
185-209 1.10e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 42.10  E-value: 1.10e-03
                         10        20
                 ....*....|....*....|....*..
gi 523412962 185 RIPRG--VLLVGPPGTGKTLLARAIAG 209
Cdd:COG4178  385 SLKPGerLLITGPSGSGKSTLLRAIAG 411
PRK13341 PRK13341
AAA family ATPase;
191-262 1.11e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.96  E-value: 1.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 191 LLVGPPGTGKTLLARAIAGEAKVPFFSISGsdfvemfVGVGAARVRDMFENAKKQAP-----CIVFIDEIdavgrHR 262
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERLErhgkrTILFIDEV-----HR 120
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
190-209 1.59e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.21  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|
gi 523412962  190 VLLVGPPGTGKTLLARAIAG 209
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
182-244 1.66e-03

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 40.32  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 182 LGGRIPRG--VLLVGPPGTGKTL-----LARAIAGEAKVPFFSisgsdFVEmfvgvgaaRVRDMFENAKK 244
Cdd:cd01124   12 LGGGIPKGsvTLLTGGPGTGKTLfglqfLYAGAKNGEPGLFFT-----FEE--------SPERLLRNAKS 68
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
190-225 1.68e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.53  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 523412962 190 VLLVGPPGTGKTLLARAIAGEA-----KVPFFSIsgSDFVE 225
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
165-294 1.84e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 41.33  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 165 EVVELVDFLKDPQKFQKLGGRIprgvLLVGPPGTGKTLLARAIA---------GEAKVPFF----SISGS----DFVEMF 227
Cdd:COG5635  162 NLLERIESLKRLELLEAKKKRL----LILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrDLAEEasleDLLAEA 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523412962 228 VGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHrgagmgggnDEREQTLNQMLVEMDGFEANSGVI 294
Cdd:COG5635  238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII 295
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
190-264 2.65e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 39.61  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKT-LLARAIAGEAKVPFFSI---SGSDFVEMFVGVGAA--------RVRDMF-ENAKKQAPCIVFIdeID 256
Cdd:cd04105    3 VLLLGPSDSGKTaLFTKLTTGKVRSTVTSIepnVASFYSNSSKGKKLTlvdvpgheKLRDKLlEYLKASLKAIVFV--VD 80

                 ....*...
gi 523412962 257 AVGRHRGA 264
Cdd:cd04105   81 SATFQKNI 88
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
184-208 3.74e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.79  E-value: 3.74e-03
                         10        20
                 ....*....|....*....|....*
gi 523412962 184 GRIPRGVLLVGPPGTGKTLLARAIA 208
Cdd:COG2812   29 GRLAHAYLFTGPRGVGKTTLARILA 53
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
185-209 3.94e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 38.67  E-value: 3.94e-03
                         10        20
                 ....*....|....*....|....*..
gi 523412962 185 RIPRG--VLLVGPPGTGKTLLARAIAG 209
Cdd:cd03223   23 EIKPGdrLLITGPSGTGKSSLFRALAG 49
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
191-208 6.07e-03

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 39.62  E-value: 6.07e-03
                         10
                 ....*....|....*...
gi 523412962 191 LLVGPPGTGKTLLARAIA 208
Cdd:COG0466  356 CLVGPPGVGKTSLGKSIA 373
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
182-240 6.29e-03

RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 38.45  E-value: 6.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523412962 182 LGGRIPRGVL--LVGPPGTGKTLLARAIAGEAKVPfFSISGSDFVEMFVGVG----AARVRDMFE 240
Cdd:cd19493    4 LAGGLPLGAIteITGASGSGKTQFALTLASSAAMP-ARKGGLDGGVLYIDTEskfsAERLAEIAE 67
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
190-254 6.73e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 38.62  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523412962 190 VLLVGPPGTGKTLLARAIAGE-------AKVPFFSISGSDFVEMF-----VGVGAARVRDMF--------ENAKKQAPCI 249
Cdd:COG3267   46 VVLTGEVGTGKTTLLRRLLERlpddvkvAYIPNPQLSPAELLRAIadelgLEPKGASKADLLrqlqefllELAAAGRRVV 125

                 ....*
gi 523412962 250 VFIDE 254
Cdd:COG3267  126 LIIDE 130
 
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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