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Conserved domains on  [gi|1093537119|ref|WP_070876406|]
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endopeptidase La [Metabacillus idriensis]

Protein Classification

endopeptidase La( domain architecture ID 11422032)

endopeptidase La is an ATP-dependent serine protease that degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long; it binds to DNA in a double-stranded, site-specific manner

CATH:  1.10.8.60
EC:  3.4.21.53
Gene Ontology:  GO:0005524|GO:0016887|GO:0004176|GO:0004252|GO:0043565
MEROPS:  S16
PubMed:  34563541|9115177

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 3-774 0e+00

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


:

Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1465.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   3 KKEEKIVPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDHIIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLKLP 82
Cdd:COG0466     8 EELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  83 NGTIRVLVEGMQRGKITKYVDEGDYFAVGAASLEESTEKDAEDEALMRTLLDHFDQYIKLSKKISGETLSTVTDIDEPGR 162
Cdd:COG0466    88 DGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 163 MADIVASHLPLKLKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDK 242
Cdd:COG0466   168 LADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEK 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 243 EGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDEDH 322
Cdd:COG0466   248 DDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDH 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 323 YGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAMPG 402
Cdd:COG0466   328 YGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 403 RIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLSTIPGPLRD 482
Cdd:COG0466   408 RIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLD 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 483 RMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVSEE 562
Cdd:COG0466   488 RMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGK 567

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 563 RKKIIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAAFSF 642
Cdd:COG0466   568 KKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSY 647

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 643 IRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEKTL 722
Cdd:COG0466   648 VRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLL 727

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093537119 723 SAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHALVGENE 774
Cdd:COG0466   728 AAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPE 779
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 3-774 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1465.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   3 KKEEKIVPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDHIIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLKLP 82
Cdd:COG0466     8 EELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  83 NGTIRVLVEGMQRGKITKYVDEGDYFAVGAASLEESTEKDAEDEALMRTLLDHFDQYIKLSKKISGETLSTVTDIDEPGR 162
Cdd:COG0466    88 DGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 163 MADIVASHLPLKLKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDK 242
Cdd:COG0466   168 LADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEK 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 243 EGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDEDH 322
Cdd:COG0466   248 DDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDH 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 323 YGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAMPG 402
Cdd:COG0466   328 YGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 403 RIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLSTIPGPLRD 482
Cdd:COG0466   408 RIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLD 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 483 RMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVSEE 562
Cdd:COG0466   488 RMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGK 567

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 563 RKKIIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAAFSF 642
Cdd:COG0466   568 KKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSY 647

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 643 IRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEKTL 722
Cdd:COG0466   648 VRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLL 727

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093537119 723 SAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHALVGENE 774
Cdd:COG0466   728 AAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPE 779
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 10-769 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1091.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  10 PLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDH-IIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLKLPN---GT 85
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQpYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  86 IRVLVEGMQRGKITKYVDEGDYFAVGAASLEES--TEKDAEDEALMRTLLDHFDQYIKLSK--KISGETLSTVTDIDEPG 161
Cdd:TIGR00763  81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEpfDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 162 RMADIVASHLPLK-LKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELG 240
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 241 DKEGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDE 320
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 321 DHYGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAM 400
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 401 PGRIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLSTIPGPL 480
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 481 RDRMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVS 560
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 561 EERKK------IIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKE 634
Cdd:TIGR00763 561 QGEKKkseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 635 SAQAAFSFIRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPI 714
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1093537119 715 GGLKEKTLSAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHAL 769
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 2-769 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 937.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   2 AKKEEKI-VPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDHIIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLK 80
Cdd:PRK10787    3 PERSERIeIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  81 LPNGTIRVLVEGMQRGKITKYVDEGDYFAVGAASLEESTEKDAEDEALMRTLLDHFDQYIKLSKKISGETLSTVTDIDEP 160
Cdd:PRK10787   83 LPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 161 GRMADIVASHLPLKLKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELG 240
Cdd:PRK10787  163 ARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 241 DKEGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDE 320
Cdd:PRK10787  243 EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 321 DHYGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAM 400
Cdd:PRK10787  323 DHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSM 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 401 PGRIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLStIPGPL 480
Cdd:PRK10787  403 PGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 481 RDRMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVS 560
Cdd:PRK10787  482 LDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLL 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 561 EER-KKIIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAA 639
Cdd:PRK10787  562 DKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAA 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 640 FSFIRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKE 719
Cdd:PRK10787  642 LTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKE 721

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|
gi 1093537119 720 KTLSAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHAL 769
Cdd:PRK10787  722 KLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 311-492 2.62e-130

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: 384.60  E-value: 2.62e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 311 LKRAETILDEDHYGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIR 390
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 391 GHRRTYVGAMPGRIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATA 470
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                         170       180
                  ....*....|....*....|..
gi 1093537119 471 NNLSTIPGPLRDRMEIITIAGY 492
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 568-771 4.78e-130

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 385.05  E-value: 4.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 568 VTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAAFSFIRSRA 647
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 648 KELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEKTLSAHRA 727
Cdd:pfam05362  82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1093537119 728 GLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHALVG 771
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 9-60 2.31e-11

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 60.53  E-value: 2.31e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1093537119    9 VPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDH--IIFLTTQRDISIDE 60
Cdd:smart00464   2 LPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQpyVIVFLLQDDPTETP 55
 
Name Accession Description Interval E-value
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 3-774 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1465.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   3 KKEEKIVPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDHIIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLKLP 82
Cdd:COG0466     8 EELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLLKLP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  83 NGTIRVLVEGMQRGKITKYVDEGDYFAVGAASLEESTEKDAEDEALMRTLLDHFDQYIKLSKKISGETLSTVTDIDEPGR 162
Cdd:COG0466    88 DGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIEDPGR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 163 MADIVASHLPLKLKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDK 242
Cdd:COG0466   168 LADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELGEK 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 243 EGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDEDH 322
Cdd:COG0466   248 DDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDH 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 323 YGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAMPG 402
Cdd:COG0466   328 YGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPG 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 403 RIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLSTIPGPLRD 482
Cdd:COG0466   408 RIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLD 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 483 RMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVSEE 562
Cdd:COG0466   488 RMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGK 567

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 563 RKKIIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAAFSF 642
Cdd:COG0466   568 KKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSY 647

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 643 IRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEKTL 722
Cdd:COG0466   648 VRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLL 727

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093537119 723 SAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHALVGENE 774
Cdd:COG0466   728 AAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPE 779
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 10-769 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1091.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  10 PLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDH-IIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLKLPN---GT 85
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQpYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  86 IRVLVEGMQRGKITKYVDEGDYFAVGAASLEES--TEKDAEDEALMRTLLDHFDQYIKLSK--KISGETLSTVTDIDEPG 161
Cdd:TIGR00763  81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEpfDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 162 RMADIVASHLPLK-LKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELG 240
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 241 DKEGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDE 320
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 321 DHYGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAM 400
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 401 PGRIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLSTIPGPL 480
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 481 RDRMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVS 560
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 561 EERKK------IIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKE 634
Cdd:TIGR00763 561 QGEKKkseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 635 SAQAAFSFIRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPI 714
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1093537119 715 GGLKEKTLSAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHAL 769
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 2-769 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 937.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   2 AKKEEKI-VPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDHIIFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLK 80
Cdd:PRK10787    3 PERSERIeIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  81 LPNGTIRVLVEGMQRGKITKYVDEGDYFAVGAASLEESTEKDAEDEALMRTLLDHFDQYIKLSKKISGETLSTVTDIDEP 160
Cdd:PRK10787   83 LPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 161 GRMADIVASHLPLKLKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELG 240
Cdd:PRK10787  163 ARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 241 DKEGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDE 320
Cdd:PRK10787  243 EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 321 DHYGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAM 400
Cdd:PRK10787  323 DHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSM 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 401 PGRIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATANNLStIPGPL 480
Cdd:PRK10787  403 PGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 481 RDRMEIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLERQLAAICRKAAKQIVS 560
Cdd:PRK10787  482 LDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLLL 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 561 EER-KKIIVTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAA 639
Cdd:PRK10787  562 DKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAA 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 640 FSFIRSRAKELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKE 719
Cdd:PRK10787  642 LTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKE 721

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|
gi 1093537119 720 KTLSAHRAGLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHAL 769
Cdd:PRK10787  722 KLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 311-492 2.62e-130

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: 384.60  E-value: 2.62e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 311 LKRAETILDEDHYGLEKVKDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIR 390
Cdd:cd19500     1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 391 GHRRTYVGAMPGRIIQGMKKAGTINPVFLLDEIDKMSNDFRGDPSSALLEVLDPEQNHTFSDHYIEETYDLSKVMFIATA 470
Cdd:cd19500    81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                         170       180
                  ....*....|....*....|..
gi 1093537119 471 NNLSTIPGPLRDRMEIITIAGY 492
Cdd:cd19500   161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 568-771 4.78e-130

Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.


Pssm-ID: 428442 [Multi-domain]  Cd Length: 205  Bit Score: 385.05  E-value: 4.78e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 568 VTDKNLADYLGKNKFRYGQAELEDQIGVATGLAYTTVGGDTLSIEVSLSPGKGKLILTGKLGDVMKESAQAAFSFIRSRA 647
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 648 KELNIDEKFHELHDIHIHVPEGAVPKDGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEKTLSAHRA 727
Cdd:pfam05362  82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1093537119 728 GLTKIIMPKDNEKDIEDIPESVRNDLTFVPVSHLDEVLQHALVG 771
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 9-198 6.18e-53

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 181.77  E-value: 6.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   9 VPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDHI--IFLTTQRDISIDEPTEEDIFTVGTLTKIKQMLKLPNGTI 86
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGTY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  87 RVLVEGMQRGKITKYVD-EGDYFAVGAASLEEstEKDAEDEALMRTLLDHFDQYIKLSKKI-SGETLSTVTDIDEPGRMA 164
Cdd:pfam02190  82 KVLVEGLERVRIVELVKkEEPYLRAEVEDLPE--DSDELSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRLA 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1093537119 165 DIVASHLPLKLKEKQEVLETLDIKERLNRVIEII 198
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLELL 193
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 350-492 4.73e-31

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: 118.08  E-value: 4.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 350 LCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDeseirghrrTYVGAMPGRIIQGMKKAGTINP-VFLLDEIDKM-- 426
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALag 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093537119 427 -----SNDFRGDPSSALLEVLDPEQNHTfsdhyieetydlSKVMFIATANNLSTIPGPLRDRMEIITIAGY 492
Cdd:pfam00004  72 srgsgGDSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
 9-201 1.40e-21

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 93.02  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119   9 VPLLPLrGLLVYPTMVLHLDVgreksvqaLE---KAMMDDHiifLTTQRDI---SIDEPTEED----IFTVGTLTKIKQM 78
Cdd:COG2802     7 LPLFPL-GAVLFPGGRLPLHI--------FEpryLDMVRDC---LAGDRPFgvvLIREGREVGgpppLYDVGTLARITDF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  79 LKLPNGTIRVLVEGMQRGKITKYVDEGDYFAVGAASL---EESTEKDAEDEALMRTLLDHFDQYIKLSKkisgetLSTVT 155
Cdd:COG2802    75 EELEDGRLDITLRGVQRFRILEELQEDDPYRVAEVEWlpdEPDLPVPEELEALRERLLRLLRRYPELAG------LEADP 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1093537119 156 DIDEPGRMADIVASHLPLKLKEKQEVLETLDIKERLNRVIEIIHNE 201
Cdd:COG2802   149 DLDDPEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
601-768 2.14e-19

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 87.34  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 601 YTTVGGDTLSIEVSLS-PGKG-KLILTGKL-GDVMKESAQAAFsFIRSRakELNIDEKfheLHDIHIHVPEGAVPKDGPS 677
Cdd:COG1750    38 SGTGEGVVINITVTVTyPGSGrVYVSTSPLtGPDTQASARIAA-LVASL--LAGVDLS---SYDVYISIESDSPIVGGPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 678 AGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEKTLSAHRAGLTKIIMPKDNE----------KDIEDIPE 747
Cdd:COG1750   112 AGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAiltgyntqvgETVDLVEY 191

                         170       180
                  ....*....|....*....|.
gi 1093537119 748 SVRNDLTFVPVSHLDEVLQHA 768
Cdd:COG1750   192 GKELGVKVIEVSTIADALQYF 212
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 328-489 3.48e-19

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: 85.03  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 328 VKDRVLEYLAVQKLT------KSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESeirghrRTYVGAMP 401
Cdd:cd19481     1 LKASLREAVEAPRRGsrlrryGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 402 GRIIQGMKKAGtiNPVFLLDEIDKMSNDfRGDPS---------SALLEVLDPEQNhtfsdhyieetydLSKVMFIATANN 472
Cdd:cd19481    75 RKIFERARRLA--PCILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATNR 138

                         170       180
                  ....*....|....*....|
gi 1093537119 473 LSTI-PGPLR--DRMEIITI 489
Cdd:cd19481   139 PDLLdPALLRpgRFDEVIEF 158
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 329-487 2.97e-16

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: 76.42  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 329 KDRVLEYLAVQKLTKSLKGPILCLSGPPGVGKTSLARSVAKSLDR---NFVRISLGGVRDESEIRGHRRTYvgamPGRII 405
Cdd:cd00009     1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFGHF----LVRLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 406 QGMKKAGTiNPVFLLDEIDKMSNDFrgdpSSALLEVLdpeqnHTFSDHYIEetYDLSKVMFIATANNLSTIPGPLRDRME 485
Cdd:cd00009    77 FELAEKAK-PGVLFIDEIDSLSRGA----QNALLRVL-----ETLNDLRID--RENVRVIGATNRPLLGDLDRALYDRLD 144


                  ..
gi 1093537119 486 II 487
Cdd:cd00009   145 IR 146
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 170-566 8.74e-15

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: 76.87  E-value: 8.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 170 HLPLKLKEKQEVLETLDIKERLNRVIEIIHNEKEVLQLEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDKEGKTGEV 249
Cdd:COG0464     3 ELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 250 DILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESSVVRNYLEWLISLPWSNATVDRLDLKRAETILDEDHY----GL 325
Cdd:COG0464    83 AALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILddlgGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 326 EKVKDRVLEYLAVQKLTKSLKGPI-------LCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDEseirghrrtYVG 398
Cdd:COG0464   163 EEVKEELRELVALPLKRPELREEYglppprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------YVG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 399 AMPGRIIQGMKKA-GTINPVFLLDEIDKMSNDfRGDPS--------SALLEVLDpeqNHTFsdhyieetydlsKVMFIAT 469
Cdd:COG0464   234 ETEKNLREVFDKArGLAPCVLFIDEADALAGK-RGEVGdgvgrrvvNTLLTEME---ELRS------------DVVVIAA 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 470 ANNLSTIPGPLRDRM-EIITIAGYTEIEKIHIAKDHLLSKQLKDhglkksNLQIREsaiqniIRYHTRE-AGvrsleRQL 547
Cdd:COG0464   298 TNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDE------DVDLEE------LAEATEGlSG-----ADI 360

                         410
                  ....*....|....*....
gi 1093537119 548 AAICRKAAKQIVSEERKKI 566
Cdd:COG0464   361 RNVVRRAALQALRLGREPV 379
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 9-60 2.31e-11

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 60.53  E-value: 2.31e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1093537119    9 VPLLPLRGLLVYPTMVLHLDVGREKSVQALEKAMMDDH--IIFLTTQRDISIDE 60
Cdd:smart00464   2 LPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQpyVIVFLLQDDPTETP 55
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
675-769 4.02e-11

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 65.22  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 675 GPSAGITMATALISALTGRPVR--KEVGMTGEITLRGRVLPIGGLKEKTLSAHRAGLTKIIMPKDNEKD-IEDIPEsvrn 751
Cdd:COG3480   240 GPSAGLMFALGIYDQLTPGDLTggKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEaVGTIPT---- 315

                          90
                  ....*....|....*...
gi 1093537119 752 DLTFVPVSHLDEVLqHAL 769
Cdd:COG3480   316 GLKVVPVDTLDDAL-DAL 332
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 345-483 6.67e-11

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: 64.03  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 345 LKGPILcLSGPPGVGKTSLARSVAKSLDRNFVRIslggvrdeseirghrRTYVGAMPGRIIqgmkkaGTIN--------- 415
Cdd:COG0714    30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSDIL------GTYIydqqtgefe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 416 ----PVF----LLDEIDkmsndfRGDP--SSALLEVLdpeQNHTFSdhyIE-ETYDLSKVMF-IATANNLSTI-----PG 478
Cdd:COG0714    88 frpgPLFanvlLADEIN------RAPPktQSALLEAM---EERQVT---IPgGTYKLPEPFLvIATQNPIEQEgtyplPE 155


                  ....*
gi 1093537119 479 PLRDR 483
Cdd:COG0714   156 AQLDR 160
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
611-738 3.38e-10

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 58.23  E-value: 3.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 611 IEVSLSPGKGKLILTGKLGDVMKESAQAAFSFIRsrakelNIDEKFhELHDIHIHVPEGAVPKDGPSAGITMATALISAL 690
Cdd:pfam13541   1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALK------NSGFEF-PPKRITVNLAPADLKKEGSSFDLPIAIGILAAQ 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1093537119 691 TGRPVRKEVGMTGEITLRGRVLPIGGLKEKTLSAHRAGLTKIIMPKDN 738
Cdd:pfam13541  74 GQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
Sms COG1066
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ...
 676-769 1.80e-08

DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];


Pssm-ID: 440685 [Multi-domain]  Cd Length: 453  Bit Score: 57.37  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 676 PSAGITMATALISALTGRPVRK------EVGMTGEItlRgrvlPIGGLKEKTLSAHRAGLTKIIMPKDNEKDIEDipesv 749
Cdd:COG1066   366 PAADLAVALAIASSFRDRPLPPdtvffgEVGLTGEI--R----PVSRIEQRLKEAAKLGFKRAIVPKGNKKKLKP----- 434

                          90       100
                  ....*....|....*....|
gi 1093537119 750 rNDLTFVPVSHLDEVLQHAL 769
Cdd:COG1066   435 -KGIEIIGVSTLEEALEALF 453
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 354-584 1.88e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 57.37  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 354 GPPGVGKTSLARSVAKSLDRNFVRIS--LGGVRDeseIRghrrtyvgampgRIIQ--GMKKAGTINPVFLLDEI---DKM 426
Cdd:COG2256    56 GPPGTGKTTLARLIANATDAEFVALSavTSGVKD---IR------------EVIEeaRERRAYGRRTILFVDEIhrfNKA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 427 SNDfrgdpssALLevldpeqnhtfsdHYIEEtydlSKVMFI-ATANNLS-TIPGPLRDRMEIITIagyTEIEKIHIAKdh 504
Cdd:COG2256   121 QQD-------ALL-------------PHVED----GTITLIgATTENPSfEVNSALLSRCRVFVL---KPLSEEDLEQ-- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 505 LLSKQLKD--HGLKKSNLQIRESAIQNIIRYhtreAG--VRS----LErqLAAicrkaakqIVSEERKKIIVTDKNLADY 576
Cdd:COG2256   172 LLERALADdeRGLGGYKLELDDEALEALARL----ADgdARRalnaLE--LAV--------LSAPPDGVIEITLELVEEA 237


                  ....*...
gi 1093537119 577 LGKNKFRY 584
Cdd:COG2256   238 LQRRALRY 245
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 674-765 2.47e-08

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 57.65  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 674 DGPSAGITMATALISALTGRPVRKEVGMTGEITLRGRVLPIGGLKEK-----TLSAHRaGLTK---IIMPKDNEKDI--- 742
Cdd:COG1067   592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKiegffDVCKAR-GLTGkqgVIIPAANVKNLmlr 670

                          90       100
                  ....*....|....*....|....
gi 1093537119 743 EDIPESVRNDLTFV-PVSHLDEVL 765
Cdd:COG1067   671 DEVVEAVKAGQFHIyAVEHVDEAI 694
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 350-484 4.11e-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: 52.68  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 350 LCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGvRD--ESEIRGHRRTYVGAmPGRIIQGMKKAGTINPVFLLDEIDKMS 427
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALSNRPVFYVQLT-RDttEEDLFGRRNIDPGG-ASWVDGPLVRAAREGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093537119 428 NDFRGdpssALLEVLDPEQNHTFSDHyiEETY-DLSKVMFIATANNL----STIPGPLRDRM 484
Cdd:pfam07728  80 PDVLN----SLLSLLDERRLLLPDGG--ELVKaAPDGFRLIATMNPLdrglNELSPALRSRF 135
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 341-474 4.46e-08

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 53.72  E-value: 4.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 341 LTKSLKGPI-LCLSGPPGVGKTSLARSVAKSL---DRNFVRISLGgvrdeSEIRGHR-RTYVGAMPGriIQGMKKAGTI- 414
Cdd:cd19499    34 LSDPNRPIGsFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMS-----EYMEKHSvSRLIGAPPG--YVGYTEGGQLt 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093537119 415 -----NP--VFLLDEIDKMSNDFRGdpssALLEVLDpeqNHTFSDHYiEETYDLSKVMFIATANNLS 474
Cdd:cd19499   107 eavrrKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSNHFR 165
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 352-423 4.31e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.16  E-value: 4.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRIS--LGGVRDeseIRghrrtyvgampgRIIQGMKK--AGTINPVFLLDEI 423
Cdd:PRK13342   41 LWGPPGTGKTTLARIIAGATDAPFEALSavTSGVKD---LR------------EVIEEARQrrSAGRRTILFIDEI 101
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 346-489 1.32e-06

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: 48.52  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119  346 KGPILCLSGPPGVGKTSLARSVAKSLDRNFVR-ISLGGVRDESEIRGHRRTYVGAMPGRIIQGMKKAGTIN--------P 416
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALalarklkpD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093537119  417 VFLLDEIDKMSNDFrgdpSSALLEVLDPEQNHTFSDHYieetydlSKVMFIATANNLST-IPGPLRDRMEIITI 489
Cdd:smart00382  81 VLILDEITSLLDAE----QEALLLLLEELRLLLLLKSE-------KNLTVILTTNDEKDlGPALLRRRFDRRIV 143
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 248-424 1.77e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 50.78  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 248 EVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAESsvvrnylewlislPWSNATVDRLDLKRAETILDEDHYGLEK 327
Cdd:COG1222    19 DALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQ-------------KRLGTPRGTAVPAESPDVTFDDIGGLDE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 328 VKDRV-----LEYLAVQKLTKSLKGP---ILcLSGPPGVGKTSLARSVAKSLDRNFVRISLggvrdeSEIrghRRTYVGA 399
Cdd:COG1222    86 QIEEIreaveLPLKNPELFRKYGIEPpkgVL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG------SEL---VSKYIGE 155

                         170       180
                  ....*....|....*....|....*.
gi 1093537119 400 MPGRIIQGMKKAGTINP-VFLLDEID 424
Cdd:COG1222   156 GARNVREVFELAREKAPsIIFIDEID 181
44 PHA02544
clamp loader, small subunit; Provisional
 339-502 2.50e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 49.99  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 339 QKLTKSLKGPILCL-SGPPGVGKTSLARSVAKSLDRN--FVRISLGGVRDeseIRGHRRTYVGAMpgriiqGMKKAGTin 415
Cdd:PHA02544   34 KSIVKKGRIPNMLLhSPSPGTGKTTVAKALCNEVGAEvlFVNGSDCRIDF---VRNRLTRFASTV------SLTGGGK-- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 416 pVFLLDEIDKmsndfrgdpsSALLEVldpeQNHTFSdhYIEEtydLSK-VMFIATANNLSTIPGPLRDRMEIITIAGYTE 494
Cdd:PHA02544  103 -VIIIDEFDR----------LGLADA----QRHLRS--FMEA---YSKnCSFIITANNKNGIIEPLRSRCRVIDFGVPTK 162


                  ....*...
gi 1093537119 495 IEKIHIAK 502
Cdd:PHA02544  163 EEQIEMMK 170
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 346-477 2.51e-06

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: 48.13  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 346 KGpiLCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDEseirghrrtYVGAMPGRIIQGMKKAGTINP-VFLLDEID 424
Cdd:cd19507    32 KG--LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG---------LVGESESRLRQMIQTAEAIAPcVLWIDEIE 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1093537119 425 KM--SNDFRGD--PSSALLEvldpeqnhTFSDHYIEETydlSKVMFIATANNLSTIP 477
Cdd:cd19507   101 KGfsNADSKGDsgTSSRVLG--------TFLTWLQEKK---KPVFVVATANNVQSLP 146
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
320-591 4.34e-06

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 48.73  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 320 EDHYGLEKVKD---RVLEYLAVQKLTKSLKGP----ILcLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDEseirgh 392
Cdd:COG1223     2 DDVVGQEEAKKklkLIIKELRRRENLRKFGLWpprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 393 rrtYVG---AMPGRIIQGMKKAGTinpVFLLDEIDKMSNDfRGDPS---------SALLEVLDPEQNHtfsdhyieetyd 460
Cdd:COG1223    75 ---YLGetaRNLRKLFDFARRAPC---VIFFDEFDAIAKD-RGDQNdvgevkrvvNALLQELDGLPSG------------ 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 461 lskVMFIATANNLSTIPGPLRDRMEI---ITIAGYTEIEKIhiakdhlLSKQLKDHGLKKsnlqirESAIQNIiryhtre 537
Cdd:COG1223   136 ---SVVIAATNHPELLDSALWRRFDEvieFPLPDKEERKEI-------LELNLKKFPLPF------ELDLKKL------- 192

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1093537119 538 agVRSLE----RQLAAICRKAAKQIVSEERKKIivTDKNLADYLGKNKFRYGQAELED 591
Cdd:COG1223   193 --AKKLEglsgADIEKVLKTALKKAILEDREKV--TKEDLEEALKQRKERKKEPKKEG 246
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 207-541 8.06e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.00  E-value: 8.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 207 LEKKIGQRVKRSMERTQKEYYLREQMKAIQKELGDKEGKTGEVDILNEKIEKAGMPDHIKLTALKELERYEKVPSTSAES 286
Cdd:COG1401    74 LEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 287 SVVRNYLEwlISLPWSNATVDRLDLKRAETILDEDHYG--LEKVKDRVLEYLA------VQKLTKSLK-GPILCLSGPPG 357
Cdd:COG1401   154 VLEALEAE--LEELLAAPEDLSADALAAELSAAEELYSedLESEDDYLKDLLRekfeetLEAFLAALKtKKNVILAGPPG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 358 VGKTSLARSVAKSL----DRNFVRISlggVR----DESEIRGHR-----RTYVgAMPGRIIQGMKKA--GTINPVFL-LD 421
Cdd:COG1401   232 TGKTYLARRLAEALggedNGRIEFVQ---FHpswsYEDFLLGYRpsldeGKYE-PTPGIFLRFCLKAekNPDKPYVLiID 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 422 EIdkmsNdfRGDPSSA------LLEVLDPEQNHTFSDHYIEETYDLS---KVMFIATAN----NLSTIPGPLRDRMEIIT 488
Cdd:COG1401   308 EI----N--RANVEKYfgellsLLESDKRGEELSIELPYSGEGEEFSippNLYIIGTMNtddrSLALSDKALRRRFTFEF 381

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1093537119 489 IA-GYTEIEKIHIAKdhlLSKQLKDHgLKKSNLQIRESAIQNIIRYHTREAGVR 541
Cdd:COG1401   382 LDpDLDKLSNEEVVD---LLEELNEI-LEKRDFQIGHRALLLLDGLLSGDLDLL 431
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 352-471 1.46e-05

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 45.24  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRISLggVRDeseirghrrtyvgAMPGRIIQGM---KKAGTIN----PVF----LL 420
Cdd:pfam07726   4 LEGVPGLAKTLLVRTLARSLGLDFRRIQF--TPD-------------LLPSDITGTEvfdQKTREFEfrpgPVFanvlLA 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1093537119 421 DEIDkmsndfRGDP--SSALLEVLDpEQNHTFSDHyieeTYDLSKVMF-IATAN 471
Cdd:pfam07726  69 DEIN------RAPPktQSALLEAMQ-ERQVTIDGE----THPLPEPFFvLATQN 111
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 352-471 7.74e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 43.72  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLD---RNFVRIslggvrDESEIrgHRRTYV----GAMPGRIiqGMKKAGTI--------NP 416
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYV--GYEEGGQLteavrrkpYS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1093537119 417 VFLLDEIDKMSND-FRgdpssALLEVLDpeqNHTFSDHYiEETYDLSKVMFIATAN 471
Cdd:pfam07724  78 IVLIDEIEKAHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGN 124
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 352-440 1.00e-04

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: 43.25  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFvrISLGGVRDESEirghrrtYVGAMPGRIIQGMKKAGTINP-VFLLDEIDKMSNDF 430
Cdd:cd19529    32 LYGPPGTGKTLLAKAVATESNANF--ISVKGPELLSK-------WVGESEKAIREIFRKARQVAPcVIFFDEIDSIAPRR 102

                          90
                  ....*....|
gi 1093537119 431 RGDPSSALLE 440
Cdd:cd19529   103 GTTGDSGVTE 112
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 324-379 1.49e-04

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: 43.05  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093537119 324 GLEKVKDRVLEYLAVQ----KLTKSL-----KGPILclSGPPGVGKTSLARSVAKSLDRNFVRIS 379
Cdd:cd19503     4 GLDEQIASLKELIELPlkypELFRALglkppRGVLL--HGPPGTGKTLLARAVANEAGANFLSIS 66
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
337-443 2.49e-04

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 44.51  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 337 AVQKLTKSLKGPI-LCLSGPPGVGKTSLARSVAKSLDR---NFVRI---SLGGVRDESEIRGHRR-TYVGA----MPGRI 404
Cdd:COG3284   333 ALRRARRLADRDIpVLILGETGTGKELFARAIHAASPRadgPFVAVncaAIPEELIESELFGYEPgAFTGArrkgRPGKI 412

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1093537119 405 IQGMKkaGTInpvfLLDEIDKMSNDFRgdpsSALLEVLD 443
Cdd:COG3284   413 EQADG--GTL----FLDEIGDMPLALQ----ARLLRVLQ 441
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
339-423 3.06e-04

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 43.78  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 339 QKLTKSLK-GPILCLSGPPGVGKTSLARSVAKSLDrNFVRISLggvrDESEIRGhrrtYVGAMPGRIIQGMKKAGTINPV 417
Cdd:COG1373    11 DKLLKLLDnRKAVVITGPRQVGKTTLLKQLAKELE-NILYINL----DDPRLRA----LAEEDPDDLLEALKELYPGKTY 81


                  ....*.
gi 1093537119 418 FLLDEI 423
Cdd:COG1373    82 LFLDEI 87
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
325-490 4.62e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 43.04  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 325 LEKVKDRVLEYLAVQKLTKSLkgpiLcLSGPPGVGKTSLARSVAKSLdrnfvrisLGGVRDESEIRGH---RRTYVGAMP 401
Cdd:COG0470     1 QEEAWEQLLAAAESGRLPHAL----L-LHGPPGIGKTTLALALARDL--------LCENPEGGKACGQchsRLMAAGNHP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 402 G-------------------RIIQGMKKAGTINP--VFLLDEIDKMSNDFrgdpSSALLEVLdpeqnhtfsdhyiEETYD 460
Cdd:COG0470    68 DllelnpeeksdqigidqirELGEFLSLTPLEGGrkVVIIDEADAMNEAA----ANALLKTL-------------EEPPK 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 1093537119 461 lsKVMFIATANNLSTIPGPLRDRMEIITIA 490
Cdd:COG0470   131 --NTPFILIANDPSRLLPTIRSRCQVIRFR 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 352-436 5.24e-04

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: 41.11  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRD----ESEiRGHRRTYvgampgriiqgmKKAGTINP-VFLLDEIDKM 426
Cdd:cd19511    32 LYGPPGCGKTLLAKALASEAGLNFISVKGPELFSkyvgESE-RAVREIF------------QKARQAAPcIIFFDEIDSL 98

                          90
                  ....*....|
gi 1093537119 427 SNDfRGDPSS 436
Cdd:cd19511    99 APR-RGQSDS 107
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 324-426 5.88e-04

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: 41.26  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 324 GLEKV----KDRVL------EYLAVQKLTKSLKGpiLCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDesEIRGHR 393
Cdd:cd19520     4 GLDEVitelKELVIlplqrpELFDNSRLLQPPKG--VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD--KWYGES 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1093537119 394 RTYVGAMpgriiqgMKKAGTINP-VFLLDEIDKM 426
Cdd:cd19520    80 QKLVAAV-------FSLASKLQPsIIFIDEIDSF 106
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 352-390 7.42e-04

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: 40.85  E-value: 7.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRIS----LGGVRDESEIR 390
Cdd:cd19518    39 LHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESEEK 81
PHA02244 PHA02244
ATPase-like protein
 230-424 7.74e-04

ATPase-like protein


Pssm-ID: 107157 [Multi-domain]  Cd Length: 383  Bit Score: 42.41  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 230 EQMKAIQKELGDKEGKTGEVDILNEKIEKAGmpdhiklTALKELEryekvpstsaeSSVVRNYLEWLISLPWSNATVDRL 309
Cdd:PHA02244   19 ETTKDLADKLGEKNSNPYEQAIIDAIREKAE-------TEGKEIA-----------IDDIKKEIEDSPEEQFFELPVKIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 310 DLKRAETILDEDHYGLEKVKDRVLEYLAVQKLTKSLKGPI-LCLSGPPGVGKTSLARSVAKSLDRNFVriSLGGVRDESE 388
Cdd:PHA02244   81 LQQEGKPAGDISGIDTTKIASNPTFHYETADIAKIVNANIpVFLKGGAGSGKNHIAEQIAEALDLDFY--FMNAIMDEFE 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1093537119 389 IRGHRRTYVGAMPGRIIQGMKKAGtinpVFLLDEID 424
Cdd:PHA02244  159 LKGFIDANGKFHETPFYEAFKKGG----LFFIDEID 190
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 311-398 8.08e-04

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: 42.91  E-value: 8.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 311 LKRAETILDEdHYGLEKVKDRVLEY-----LAVQKLTKSLKGPI----LCLSGPPGVGKTSLARSVAKSLdrnfvrISLG 381
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKRQVAALksstaMALARAERGLPVAQtsnhMLFAGPPGTGKTTIARVVAKIY------CGLG 340

                          90
                  ....*....|....*..
gi 1093537119 382 GVRDESEIRGHRRTYVG 398
Cdd:TIGR03922 341 VLRKPLVREVSRADLIG 357
AAA_22 pfam13401
AAA domain;
349-430 8.34e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.02  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 349 ILCLSGPPGVGKTSLARSVAKSL---DRNFVRI---SLGGVRD-------ESEIRGHRRTYVGAMPGRIIQGMKKAGTIn 415
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVdlpSGTSPKDllrallrALGLPLSGRLSKEELLAALQQLLLALAVA- 85

                          90
                  ....*....|....*
gi 1093537119 416 PVFLLDEIDKMSNDF 430
Cdd:pfam13401  86 VVLIIDEAQHLSLEA 100
PRK13341 PRK13341
AAA family ATPase;
350-385 1.16e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 42.35  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1093537119 350 LCLSGPPGVGKTSLARSVAKSLDRNFVRIS--LGGVRD 385
Cdd:PRK13341   55 LILYGPPGVGKTTLARIIANHTRAHFSSLNavLAGVKD 92
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 323-381 1.43e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.18  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1093537119 323 YGLEKVKDRVLEYLAVqklTKSLKGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLG 381
Cdd:pfam13191   3 VGREEELEQLLDALDR---VRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
aroK PRK00131
shikimate kinase; Reviewed
 344-376 1.77e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 40.17  E-value: 1.77e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1093537119 344 SLKGPILCLSGPPGVGKTSLARSVAKSLDRNFV 376
Cdd:PRK00131    1 MLKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 352-424 1.80e-03

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: 40.01  E-value: 1.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRISlggvrdESEIrghRRTYVGAMPgRIIQGM-----KKAGTInpVFlLDEID 424
Cdd:cd19502    42 LYGPPGTGKTLLAKAVANHTDATFIRVV------GSEL---VQKYIGEGA-RLVRELfemarEKAPSI--IF-IDEID 106
COG3903 COG3903
Predicted ATPase [General function prediction only];
348-389 2.33e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 41.54  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1093537119 348 PILCLSGPPGVGKTSLARSVAKSLDRNF----VRISLGGVRDESEI 389
Cdd:COG3903   177 RLVTLTGPGGVGKTRLALEVAHRLADRFpdgvWFVDLAGVTDPALV 222
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 324-424 2.62e-03

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: 39.52  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 324 GLEKVKDRVLEYLAV----QKLT----KSLKGPILclSGPPGVGKTSLARSVAKSLDRNFVRISlGGVRDEseirghrrT 395
Cdd:cd19501     8 GCEEAKEELKEVVEFlknpEKFTklgaKIPKGVLL--VGPPGTGKTLLAKAVAGEAGVPFFSIS-GSDFVE--------M 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1093537119 396 YVGAMPGRIIQGMKKAGTINP--VFlLDEID 424
Cdd:cd19501    77 FVGVGASRVRDLFEQAKKNAPciVF-IDEID 106
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 320-383 4.43e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.98  E-value: 4.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093537119 320 EDHYGLEKVKDRVLEYLAVQKLTKSLKGPILcLSGPPGVGKTSLARSVAKSLDRNfVRISLGGV 383
Cdd:TIGR00635   4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPA 65
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 320-581 4.64e-03

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: 40.28  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 320 EDHYGLEKVKDRVLEY----LAVQKLTKSL-----KGpiLCLSGPPGVGKTSLARSVAKSLDRNFvrISLGGVRDESEir 390
Cdd:TIGR01243 453 SDIGGLEEVKQELREAvewpLKHPEIFEKMgirppKG--VLLFGPPGTGKTLLAKAVATESGANF--IAVRGPEILSK-- 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 391 ghrrtYVGAMPGRIIQGMKKAGTINP-VFLLDEIDKMSNDFRGDPSSAlleVLDPEQNHTFSDhyIEETYDLSKVMFIAT 469
Cdd:TIGR01243 527 -----WVGESEKAIREIFRKARQAAPaIIFFDEIDAIAPARGARFDTS---VTDRIVNQLLTE--MDGIQELSNVVVIAA 596

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 470 ANNLSTI-PGPLR----DRmeIITIAGYTEIEKIHIAKDHLLSKQLKDHGLKKSNLQIRESAIQNIIRYHTREAGVRSLE 544
Cdd:TIGR01243 597 TNRPDILdPALLRpgrfDR--LILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALR 674

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1093537119 545 RQLAAICRKAAKQIVSEERKKIIVTDKNLADYLGKNK 581
Cdd:TIGR01243 675 ESIGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVK 711
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 352-471 4.70e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 40.59  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRIslggvrDESEIrGHRRT---YVGAMPGRIiqGMKKAGTI------NP--VFLL 420
Cdd:PRK11034  493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYV--GFDQGGLLtdavikHPhaVLLL 563

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1093537119 421 DEIDKMSNDFrgdpSSALLEVLDpeqNHTFSDHYIEETyDLSKVMFIATAN 471
Cdd:PRK11034  564 DEIEKAHPDV----FNLLLQVMD---NGTLTDNNGRKA-DFRNVVLVMTTN 606
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 352-379 4.88e-03

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: 38.49  E-value: 4.88e-03
                          10        20
                  ....*....|....*....|....*...
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVRIS 379
Cdd:cd19509    37 LYGPPGTGKTLLARAVASESGSTFFSIS 64
Sigma54_activat pfam00158
Sigma-54 interaction domain;
348-427 5.86e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 38.15  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 348 PILcLSGPPGVGKTSLARSV-AKSL--DRNFVRISLGGVRD---ESEIRGHRR-TYVGAMPGRIiqG-MKKA--GTInpv 417
Cdd:pfam00158  24 PVL-ITGESGTGKELFARAIhQLSPraDGPFVAVNCAAIPEellESELFGHEKgAFTGADSDRK--GlFELAdgGTL--- 97

                          90
                  ....*....|
gi 1093537119 418 fLLDEIDKMS 427
Cdd:pfam00158  98 -FLDEIGELP 106
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 352-426 6.19e-03

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: 38.24  E-value: 6.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093537119 352 LSGPPGVGKTSLARSVAKSLDRNFVrislggvrdesEIRGHR--RTYVGAMPGRIIQGMKKAGTINP-VFLLDEIDKM 426
Cdd:cd19530    35 LYGPPGCGKTLLAKAVANESGANFI-----------SVKGPEllNKYVGESERAVRQVFQRARASAPcVIFFDEVDAL 101
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
350-379 7.09e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 39.34  E-value: 7.09e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1093537119 350 LCLSGPPGVGKTSLARSVAKSLDRNFVRIS 379
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITS 83
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 346-424 7.56e-03

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: 37.99  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093537119 346 KGPILCLSGPPGVGKTSLARSVAKSLDRNFVRISLGGVRDESEIRGHRRTYVGAMPGrIIQGMKK------AGTINP-VF 418
Cdd:cd00267    24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ-LSGGQRQrvalarALLLNPdLL 102


                  ....*.
gi 1093537119 419 LLDEID 424
Cdd:cd00267   103 LLDEPT 108
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 349-386 9.64e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.47  E-value: 9.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1093537119 349 ILCLSGPPGVGKTSLARSVAKSLdrNFVRISLGGVRDE 386
Cdd:cd02020     1 IIAIDGPAGSGKSTVAKLLAKKL--GLPYLDTGGIRTE 36
 
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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