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Conserved domains on  [gi|90111737|ref|NP_418766|]
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5-methylcytosine-specific restriction enzyme subunit McrB [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

PRK11331 family protein( domain architecture ID 11485318)

PRK11331 family protein

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
 1-459 0e+00

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


:

Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 968.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80
Cdd:PRK11331   1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSGKSVIP 160
Cdd:PRK11331  81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGLDYTRFASMLDNIINDYKLIFNSGKSVIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  161 PMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYED 240
Cdd:PRK11331 161 PMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYED 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  241 FIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF 320
Cdd:PRK11331 241 FIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYVFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  321 YVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILG 400
Cdd:PRK11331 321 YVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILG 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111737  401 KGFRIGHSYFCCGLEDGTSPDTQWLNEIVMTDIAPLLEEYFFDDPYKQQKWTNKLLGDS 459
Cdd:PRK11331 401 KGFRIGHSYFCCGLEDGTSPDTQWLKEIVMTDIAPLLEEYFFDDPYKQQIWADKLLGDS 459
 
Name Accession Description Interval E-value
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
 1-459 0e+00

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 968.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80
Cdd:PRK11331   1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSGKSVIP 160
Cdd:PRK11331  81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGLDYTRFASMLDNIINDYKLIFNSGKSVIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  161 PMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYED 240
Cdd:PRK11331 161 PMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYED 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  241 FIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF 320
Cdd:PRK11331 241 FIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYVFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  321 YVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILG 400
Cdd:PRK11331 321 YVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILG 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111737  401 KGFRIGHSYFCCGLEDGTSPDTQWLNEIVMTDIAPLLEEYFFDDPYKQQKWTNKLLGDS 459
Cdd:PRK11331 401 KGFRIGHSYFCCGLEDGTSPDTQWLKEIVMTDIAPLLEEYFFDDPYKQQIWADKLLGDS 459
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1-411 2.86e-89

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 280.12  E-value: 2.86e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80
Cdd:COG1401  47 AERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERS 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYpkKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSgksvip 160
Cdd:COG1401 127 DALEALERARLLLELADLEERAALETEVLEALE--AELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDY------ 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 161 pmsktesycLEDALNDLFipETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKaPQRVNMVQFHQSYSYED 240
Cdd:COG1401 199 ---------LKDLLREKF--EETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGGED-NGRIEFVQFHPSWSYED 266

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 241 FIQGYRPNGV--GFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDeE 318
Cdd:COG1401 267 FLLGYRPSLDegKYEPTPGIFLRFCLKAEKNPDKPYVLIIDEINRANVEKYFGELLSLLESDKRGEELSIELPYSGEG-E 345

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 319 RFYVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDtpQFRNfllnkkaepsfvESLCQKMNELNQEISKEati 398
Cdd:COG1401 346 EFSIPPNLYIIGTMNTDDRSLALSDKALRRRFTFEFLDPDLD--KLSN------------EEVVDLLEELNEILEKR--- 408

                       410
                ....*....|...
gi 90111737 399 lgkGFRIGHSYFC 411
Cdd:COG1401 409 ---DFQIGHRALL 418
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 196-350 7.90e-38

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: 134.34  E-value: 7.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   196 NIILQGPPGVGKTFVARRLAYLLTGekapQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQqakeqpeKKYI 275
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSN----RPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAR-------EGEI 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111737   276 FIIDEINRANlSKVFGEVMMLMEHDKRGENWSVPLTYSENDeerfyvpeNVYIIGLMNTADRSLAVVDYALRRRF 350
Cdd:pfam07728  70 AVLDEINRAN-PDVLNSLLSLLDERRLLLPDGGELVKAAPD--------GFRLIATMNPLDRGLNELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 188-353 2.51e-14

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: 70.25  E-value: 2.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 188 LKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPqrVNMVQFHqsysyeDFIQGYRpngvgFRRKDGIFYNFCQQAK 267
Cdd:cd00009  13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP--FLYLNAS------DLLEGLV-----VAELFGHFLVRLLFEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 268 EQPEKKYIFIIDEINRANLSKVFGEVMMLMEHdkrgenwsvpltysendEERFYVPENVYIIGLmnTADRSLAVVDYALR 347
Cdd:cd00009  80 AEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----------------NDLRIDRENVRVIGA--TNRPLLGDLDRALY 140


                ....*.
gi 90111737 348 RRFSFI 353
Cdd:cd00009 141 DRLDIR 146
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 194-353 3.24e-10

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: 58.15  E-value: 3.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    194 KKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKk 273
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    274 yIFIIDEINRANLSKVFGEVMMLMEhdkrgenwsvpltysENDEERFYVPENVYIIGLMNTADRSLAVvdyALRRRFSFI 353
Cdd:smart00382  81 -VLILDEITSLLDAEQEALLLLLEE---------------LRLLLLLKSEKNLTVILTTNDEKDLGPA---LLRRRFDRR 141
 
Name Accession Description Interval E-value
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
 1-459 0e+00

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 968.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80
Cdd:PRK11331   1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSGKSVIP 160
Cdd:PRK11331  81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYPKKYGQSYYACSQKVSQGLDYTRFASMLDNIINDYKLIFNSGKSVIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  161 PMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYED 240
Cdd:PRK11331 161 PMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYED 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  241 FIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF 320
Cdd:PRK11331 241 FIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKKYVFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDEERF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  321 YVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILG 400
Cdd:PRK11331 321 YVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDTPQFRNFLLNKKAEPSFVESLCQKMNELNQEISKEATILG 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111737  401 KGFRIGHSYFCCGLEDGTSPDTQWLNEIVMTDIAPLLEEYFFDDPYKQQKWTNKLLGDS 459
Cdd:PRK11331 401 KGFRIGHSYFCCGLEDGTSPDTQWLKEIVMTDIAPLLEEYFFDDPYKQQIWADKLLGDS 459
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1-411 2.86e-89

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 280.12  E-value: 2.86e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   1 MESIQPWIEKFIKQAQQQRSQSTKDYPTSYRNLRVKLSFGYGNFTSIPWFAFLGEGQEASNGIYPVILYYKDFDELVLAY 80
Cdd:COG1401  47 AERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERS 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737  81 GISDTNEPHAQWQFSSDIPKTIAEYFQATSGVYpkKYGQSYYACSQKVSQGIDYTRFASMLDNIINDYKLIFNSgksvip 160
Cdd:COG1401 127 DALEALERARLLLELADLEERAALETEVLEALE--AELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDY------ 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 161 pmsktesycLEDALNDLFipETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKaPQRVNMVQFHQSYSYED 240
Cdd:COG1401 199 ---------LKDLLREKF--EETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGGED-NGRIEFVQFHPSWSYED 266

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 241 FIQGYRPNGV--GFRRKDGIFYNFCQQAKEQPEKKYIFIIDEINRANLSKVFGEVMMLMEHDKRGENWSVPLTYSENDeE 318
Cdd:COG1401 267 FLLGYRPSLDegKYEPTPGIFLRFCLKAEKNPDKPYVLIIDEINRANVEKYFGELLSLLESDKRGEELSIELPYSGEG-E 345

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 319 RFYVPENVYIIGLMNTADRSLAVVDYALRRRFSFIDIEPGFDtpQFRNfllnkkaepsfvESLCQKMNELNQEISKEati 398
Cdd:COG1401 346 EFSIPPNLYIIGTMNTDDRSLALSDKALRRRFTFEFLDPDLD--KLSN------------EEVVDLLEELNEILEKR--- 408

                       410
                ....*....|...
gi 90111737 399 lgkGFRIGHSYFC 411
Cdd:COG1401 409 ---DFQIGHRALL 418
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 196-350 7.90e-38

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: 134.34  E-value: 7.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   196 NIILQGPPGVGKTFVARRLAYLLTGekapQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQqakeqpeKKYI 275
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSN----RPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAR-------EGEI 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111737   276 FIIDEINRANlSKVFGEVMMLMEHDKRGENWSVPLTYSENDeerfyvpeNVYIIGLMNTADRSLAVVDYALRRRF 350
Cdd:pfam07728  70 AVLDEINRAN-PDVLNSLLSLLDERRLLLPDGGELVKAAPD--------GFRLIATMNPLDRGLNELSPALRSRF 135
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 188-353 2.51e-14

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: 70.25  E-value: 2.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 188 LKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKAPqrVNMVQFHqsysyeDFIQGYRpngvgFRRKDGIFYNFCQQAK 267
Cdd:cd00009  13 ALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP--FLYLNAS------DLLEGLV-----VAELFGHFLVRLLFEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 268 EQPEKKYIFIIDEINRANLSKVFGEVMMLMEHdkrgenwsvpltysendEERFYVPENVYIIGLmnTADRSLAVVDYALR 347
Cdd:cd00009  80 AEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----------------NDLRIDRENVRVIGA--TNRPLLGDLDRALY 140


                ....*.
gi 90111737 348 RRFSFI 353
Cdd:cd00009 141 DRLDIR 146
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 194-353 3.24e-10

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: 58.15  E-value: 3.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    194 KKNIILQGPPGVGKTFVARRLAYLLTGEKAPQRVNMVQFHQSYSYEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQPEKk 273
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737    274 yIFIIDEINRANLSKVFGEVMMLMEhdkrgenwsvpltysENDEERFYVPENVYIIGLMNTADRSLAVvdyALRRRFSFI 353
Cdd:smart00382  81 -VLILDEITSLLDAEQEALLLLLEE---------------LRLLLLLKSEKNLTVILTTNDEKDLGPA---LLRRRFDRR 141
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
174-398 1.95e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 47.11  E-value: 1.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 174 LNDLFIPETTIETI--LKRLTI----KKNIILQGPPGVGKTFVARRLAYLLTGEKAPQ------RVNMVQFHQSYSYEDF 241
Cdd:COG5635 154 LDDLYVPLNLLERIesLKRLELleakKKRLLILGEPGSGKTTLLRYLALELAERYLDAedpipiLIELRDLAEEASLEDL 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 242 IQGYrpngvgFRRKDGIFYNFCQQAKEQpeKKYIFIID---EI-NRANLSKVFGEVMMLMEHdkrgenwsvpltysende 317
Cdd:COG5635 234 LAEA------LEKRGGEPEDALERLLRN--GRLLLLLDgldEVpDEADRDEVLNQLRRFLER------------------ 287

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 318 erfyVPENVYIIglmnTAdRSLAVVDYALrRRFSFIDIEPgFDTPQFRNFLLNK-KAEPSFVESLCQKMNElNQEISKEA 396
Cdd:COG5635 288 ----YPKARVII----TS-RPEGYDSSEL-EGFEVLELAP-LSDEQIEEFLKKWfEATERKAERLLEALEE-NPELRELA 355


                ..
gi 90111737 397 TI 398
Cdd:COG5635 356 RN 357
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 197-353 2.69e-05

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: 43.74  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   197 IILQGPPGVGKTFVARRLAYLLtgekapqRVNMVQFHQSysyeDFIQGYRpnGVGFRRKDGIFynfcQQAKEQPEKkyIF 276
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKEL-------GAPFIEISGS----ELVSKYV--GESEKRLRELF----EAAKKLAPC--VI 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111737   277 IIDEINRANLSKVFGEvmmlMEHDKRGENwsvpLTYSENDEERfYVPENVYIIGLMNTADRslavVDYALRRRFSFI 353
Cdd:pfam00004  62 FIDEIDALAGSRGSGG----DSESRRVVN----QLLTELDGFT-SSNSKVIVIAATNRPDK----LDPALLGRFDRI 125
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 193-350 3.01e-05

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: 44.53  E-value: 3.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 193 IKKNIILQGPPGVGKTFVARRLAylltGEkapqrVNMVQFHQSYSyeDFIQGYRpnGVGFRRKDGIFynfcQQAKEQPeK 272
Cdd:cd19501  36 IPKGVLLVGPPGTGKTLLAKAVA----GE-----AGVPFFSISGS--DFVEMFV--GVGASRVRDLF----EQAKKNA-P 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 273 KYIFI--IDEINRANLSKVFGevmmlmEHDKRGENWSVPLTysENDEerFYVPENVYIIGLMNTADrslaVVDYALRR-- 348
Cdd:cd19501  98 CIVFIdeIDAVGRKRGAGLGG------GHDEREQTLNQLLV--EMDG--FESNTGVIVIAATNRPD----VLDPALLRpg 163


                ..
gi 90111737 349 RF 350
Cdd:cd19501 164 RF 165
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 195-224 7.15e-05

ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 45.04  E-value: 7.15e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 90111737 195 KNIILQGPPGVGKTFVARRLAYLLtgeKAP 224
Cdd:COG1220  51 KNILMIGPTGVGKTEIARRLAKLA---NAP 77
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 177-228 8.76e-05

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 43.25  E-value: 8.76e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111737 177 LFIPEttietILKRLTIK--KNIILQGPPGVGKTFVARRLAYLLTGeKAPQRVN 228
Cdd:cd19504  21 VFPPE-----IVEQLGCKhvKGILLYGPPGTGKTLMARQIGKMLNA-REPKIVN 68
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
195-224 1.54e-04

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 43.91  E-value: 1.54e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 90111737  195 KNIILQGPPGVGKTFVARRLAYLLtgeKAP 224
Cdd:PRK05201  51 KNILMIGPTGVGKTEIARRLAKLA---NAP 77
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 188-224 2.13e-04

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 41.98  E-value: 2.13e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 90111737 188 LKRLTIKKNIILQGPPGVGKTFVARRLAYLLtgeKAP 224
Cdd:cd19498  40 LRDEVTPKNILMIGPTGVGKTEIARRLAKLA---GAP 73
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 177-215 2.28e-04

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: 41.50  E-value: 2.28e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 90111737 177 LFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLA 215
Cdd:cd19481   9 VEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALA 47
clpC CHL00095
Clp protease ATP binding subunit
 187-225 4.40e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 42.74  E-value: 4.40e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 90111737  187 ILKRLTiKKNIILQGPPGVGKTFVARRLAYLLTGEKAPQ 225
Cdd:CHL00095 194 ILGRRT-KNNPILIGEPGVGKTAIAEGLAQRIVNRDVPD 231
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 187-350 5.86e-04

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 41.92  E-value: 5.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 187 ILKRLTIK--KNIILQGPPGVGKTFVARRLAylltGE-KAP-QRVnmvqfhqsySYEDFIQGYRpnGVGFRRKDGIFynf 262
Cdd:COG1222 103 LFRKYGIEppKGVLLYGPPGTGKTLLAKAVA----GElGAPfIRV---------RGSELVSKYI--GEGARNVREVF--- 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 263 cQQAKEqpEKKYIFIIDEI-----NRANLSKVfGEVMMLMehdkrgenwSVPLTYSENDEERfyvpENVYIIGLMNTADr 337
Cdd:COG1222 165 -ELARE--KAPSIIFIDEIdaiaaRRTDDGTS-GEVQRTV---------NQLLAELDGFESR----GDVLIIAATNRPD- 226

                       170
                ....*....|....*
gi 90111737 338 slaVVDYALRR--RF 350
Cdd:COG1222 227 ---LLDPALLRpgRF 238
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 196-218 1.11e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 41.18  E-value: 1.11e-03
                        10        20
                ....*....|....*....|...
gi 90111737 196 NIILQGPPGVGKTFVARRLAYLL 218
Cdd:COG0606 213 NLLMIGPPGSGKTMLARRLPGIL 235
AAA_22 pfam13401
AAA domain;
194-281 1.27e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737   194 KKNIILQGPPGVGKTFVARRLAYLLTGEKApqRVNMVQFHQSYS----YEDFIQGYRPNGVGFRRKDGIFYNFCQQAKEQ 269
Cdd:pfam13401   5 AGILVLTGESGTGKTTLLRRLLEQLPEVRD--SVVFVDLPSGTSpkdlLRALLRALGLPLSGRLSKEELLAALQQLLLAL 82

                          90
                  ....*....|..
gi 90111737   270 PeKKYIFIIDEI 281
Cdd:pfam13401  83 A-VAVVLIIDEA 93
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
194-211 1.69e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 1.69e-03
                        10
                ....*....|....*...
gi 90111737 194 KKNIILQGPPGVGKTFVA 211
Cdd:COG1484  99 GENLILLGPPGTGKTHLA 116
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 196-218 1.80e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.44  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|...
gi 90111737   196 NIILQGPPGVGKTFVARRLAYLL 218
Cdd:pfam01078  24 NLLMIGPPGSGKTMLAKRLPGIL 46
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
171-282 2.79e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 39.83  E-value: 2.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 171 EDALNDLFIPET------TIETILKRL--TIKK----NIILQGPPGVGKTFVARRLAYLLTgEKAPQRVNMVQFH----Q 234
Cdd:COG1474  16 REVLSPDYVPDRlphreeEIEELASALrpALRGerpsNVLIYGPTGTGKTAVAKYVLEELE-EEAEERGVDVRVVyvncR 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 90111737 235 SYS---------YEDFIQGYRPN--GVGFRRKDGIFYNfcqqAKEQPEKKYIFIIDEIN 282
Cdd:COG1474  95 QAStryrvlsriLEELGSGEDIPstGLSTDELFDRLYE----ALDERDGVLVVVLDEID 149
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 198-218 4.01e-03

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 38.29  E-value: 4.01e-03
                        10        20
                ....*....|....*....|.
gi 90111737 198 ILQGPPGVGKTFVARRLAYLL 218
Cdd:cd17936  20 LIQGPPGTGKTFLGVKLVRAL 40
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 196-237 5.40e-03

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: 37.56  E-value: 5.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 90111737   196 NIILQGPPGVGKTFVARRLAYLLTG-EKAPQRVNMVQFHQSYS 237
Cdd:pfam07724   5 SFLFLGPTGVGKTELAKALAELLFGdERALIRIDMSEYMEEHS 47
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 184-281 6.54e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 37.15  E-value: 6.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111737 184 IETILKRltikKNIILQGPPGVGKTFVARRLAYLL------------TGeKAPQRVNMVQFHQSYSYEDFIqGYRPNGVG 251
Cdd:cd17933   6 VRLVLRN----RVSVLTGGAGTGKTTTLKALLAALeaegkrvvlaapTG-KAAKRLSESTGIEASTIHRLL-GINPGGGG 79

                        90       100       110
                ....*....|....*....|....*....|
gi 90111737 252 FRRKdgifynfcqqaKEQPEKKYIFIIDEI 281
Cdd:cd17933  80 FYYN-----------EENPLDADLLIVDEA 98
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 170-218 6.67e-03

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: 38.74  E-value: 6.67e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111737 170 LEDALNDLFIPETTIETILKR---------------LTIKKNIILQGPPGVGKTFVARRLAYLL 218
Cdd:COG0464 152 REAILDDLGGLEEVKEELRELvalplkrpelreeygLPPPRGLLLYGPPGTGKTLLARALAGEL 215
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 194-218 8.95e-03

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 37.96  E-value: 8.95e-03
                        10        20
                ....*....|....*....|....*
gi 90111737 194 KKNIILQGPPGVGKTFVARRLAYLL 218
Cdd:cd19497  50 KSNILLIGPTGSGKTLLAQTLAKIL 74
aroK PRK00131
shikimate kinase; Reviewed
 194-218 9.30e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.09  E-value: 9.30e-03
                         10        20
                 ....*....|....*....|....*
gi 90111737  194 KKNIILQGPPGVGKTFVARRLAYLL 218
Cdd:PRK00131   4 GPNIVLIGFMGAGKSTIGRLLAKRL 28
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 189-215 9.88e-03

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: 36.88  E-value: 9.88e-03
                        10        20
                ....*....|....*....|....*....
gi 90111737 189 KRLTIK--KNIILQGPPGVGKTFVARRLA 215
Cdd:cd19511  20 KRLGIRppKGVLLYGPPGCGKTLLAKALA 48
 
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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