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Conserved domains on  [gi|1363978819|emb|CEI71813|]
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AAA ATPase [Romboutsia hominis]

Protein Classification

ATP-binding protein( domain architecture ID 12206295)

ATP-binding protein containing an AAA (ATPases Associated with various cellular Activities) domain functions in an oligomeric complex and undergoes ATP hydrolysis-driven conformational changes, which are ultimately responsible for its function

Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17897320|18466635

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 16-154 8.46e-13

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: 65.47  E-value: 8.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819   16 TGEVPLVVGESGIGKTALAKKLAKE---NEWSLIVIDGNLLKEGEIGGLPTVESYIISNSNGQEvvkkttvyavhNKLRE 92
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE-----------LRLRL 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1363978819   93 IDEEISKGRNVLLFIDEINR-CEHTVQQELMNLILNREINGYKLHDDVKILAAMNPSSKYGSD 154
Cdd:smart00382  70 ALALARKLKPDVLILDEITSlLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
 
Name Accession Description Interval E-value
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 16-154 8.46e-13

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: 65.47  E-value: 8.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819   16 TGEVPLVVGESGIGKTALAKKLAKE---NEWSLIVIDGNLLKEGEIGGLPTVESYIISNSNGQEvvkkttvyavhNKLRE 92
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE-----------LRLRL 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1363978819   93 IDEEISKGRNVLLFIDEINR-CEHTVQQELMNLILNREINGYKLHDDVKILAAMNPSSKYGSD 154
Cdd:smart00382  70 ALALARKLKPDVLILDEITSlLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-149 3.25e-08

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: 52.15  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  20 PLVVGESGIGKTALAKKLAKE---NEWSLIVIDGNLLKEGEIGGLptvesyiisnsngqevvkkttvYAVHNKLREIDEE 96
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAE----------------------LFGHFLVRLLFEL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1363978819  97 ISKGRNVLLFIDEINRCEHTVQQELMNlILNREINGYKLHDDVKILAAMNPSS 149
Cdd:cd00009    80 AEKAKPGVLFIDEIDSLSRGAQNALLR-VLETLNDLRIDRENVRVIGATNRPL 131
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 21-146 6.54e-06

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: 45.28  E-value: 6.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNLLKEGEIGglptvesyiisnsngqevvkkttvyAVHNKLREIDEEISKG 100
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVG-------------------------ESEKRLRELFEAAKKL 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1363978819 101 RNVLLFIDEI-------NRCEHTVQQELMNLILNrEINGYK-LHDDVKILAAMN 146
Cdd:pfam00004  57 APCVIFIDEIdalagsrGSGGDSESRRVVNQLLT-ELDGFTsSNSKVIVIAATN 109
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 21-146 1.17e-05

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 46.54  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNllkegEIgglptVESYIisnsnGQ-EvvkkttvyavhNKLREIDEEISK 99
Cdd:COG1222   116 LLYGPPGTGKTLLAKAVAGELGAPFIRVRGS-----EL-----VSKYI-----GEgA-----------RNVREVFELARE 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1363978819 100 GRNVLLFIDEI--------NRCEHTVQQELMNLILNrEINGYKLHDDVKILAAMN 146
Cdd:COG1222   170 KAPSIIFIDEIdaiaarrtDDGTSGEVQRTVNQLLA-ELDGFESRGDVLIIAATN 223
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 20-117 4.34e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.52  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  20 PLVVGESGIGKTALAKKLAkeneWSLIvidgnllkEGEIgglptvesyiisnsngQEVVKKTTVYAV------------- 86
Cdd:PRK11034  210 PLLVGESGVGKTAIAEGLA----WRIV--------QGDV----------------PEVMADCTIYSLdigsllagtkyrg 261

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1363978819  87 --HNKLREIDEEISKGRNVLLFIDEInrceHTV 117
Cdd:PRK11034  262 dfEKRFKALLKQLEQDTNSILFIDEI----HTI 290
 
Name Accession Description Interval E-value
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 16-154 8.46e-13

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: 65.47  E-value: 8.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819   16 TGEVPLVVGESGIGKTALAKKLAKE---NEWSLIVIDGNLLKEGEIGGLPTVESYIISNSNGQEvvkkttvyavhNKLRE 92
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE-----------LRLRL 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1363978819   93 IDEEISKGRNVLLFIDEINR-CEHTVQQELMNLILNREINGYKLHDDVKILAAMNPSSKYGSD 154
Cdd:smart00382  70 ALALARKLKPDVLILDEITSlLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPA 132
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-149 3.25e-08

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: 52.15  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  20 PLVVGESGIGKTALAKKLAKE---NEWSLIVIDGNLLKEGEIGGLptvesyiisnsngqevvkkttvYAVHNKLREIDEE 96
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAE----------------------LFGHFLVRLLFEL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1363978819  97 ISKGRNVLLFIDEINRCEHTVQQELMNlILNREINGYKLHDDVKILAAMNPSS 149
Cdd:cd00009    80 AEKAKPGVLFIDEIDSLSRGAQNALLR-VLETLNDLRIDRENVRVIGATNRPL 131
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 21-146 1.97e-06

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: 47.28  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNLLkegeigglptVESYiisnsngqevvkkttVYAVHNKLREIDEEISKG 100
Cdd:cd19481    30 LLYGPPGTGKTLLAKALAGELGLPLIVVKLSSL----------LSKY---------------VGESEKNLRKIFERARRL 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1363978819 101 RNVLLFIDEI--------NRCEHTVQQELMNLILNrEINGYKLHDDVKILAAMN 146
Cdd:cd19481    85 APCILFIDEIdaigrkrdSSGESGELRRVLNQLLT-ELDGVNSRSKVLVIAATN 137
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 21-146 6.54e-06

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: 45.28  E-value: 6.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNLLKEGEIGglptvesyiisnsngqevvkkttvyAVHNKLREIDEEISKG 100
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVG-------------------------ESEKRLRELFEAAKKL 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1363978819 101 RNVLLFIDEI-------NRCEHTVQQELMNLILNrEINGYK-LHDDVKILAAMN 146
Cdd:pfam00004  57 APCVIFIDEIdalagsrGSGGDSESRRVVNQLLT-ELDGFTsSNSKVIVIAATN 109
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 21-146 1.17e-05

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 46.54  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNllkegEIgglptVESYIisnsnGQ-EvvkkttvyavhNKLREIDEEISK 99
Cdd:COG1222   116 LLYGPPGTGKTLLAKAVAGELGAPFIRVRGS-----EL-----VSKYI-----GEgA-----------RNVREVFELARE 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1363978819 100 GRNVLLFIDEI--------NRCEHTVQQELMNLILNrEINGYKLHDDVKILAAMN 146
Cdd:COG1222   170 KAPSIIFIDEIdaiaarrtDDGTSGEVQRTVNQLLA-ELDGFESRGDVLIIAATN 223
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 21-170 2.84e-05

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: 43.44  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAK---ENEWSLIVIDGNLLKEGEIGGlptvesyIISNSNGQEVVKKTTVYAVHNKLreideei 97
Cdd:pfam07728   3 LLVGPPGTGKTELAERLAAalsNRPVFYVQLTRDTTEEDLFGR-------RNIDPGGASWVDGPLVRAAREGE------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  98 skgrnvLLFIDEINRCEHTVQQELMNLILNREI---NGYKL----HDDVKILAAMNPSskygsdfDYQVVDMDAAQENRF 170
Cdd:pfam07728  69 ------IAVLDEINRANPDVLNSLLSLLDERRLllpDGGELvkaaPDGFRLIATMNPL-------DRGLNELSPALRSRF 135
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 21-110 2.80e-04

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: 42.59  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNLLkegeigglptVESYIisnsnGQ-EvvkkttvyavhNKLREIDEEISK 99
Cdd:COG0464   195 LLYGPPGTGKTLLARALAGELGLPLIEVDLSDL----------VSKYV-----GEtE-----------KNLREVFDKARG 248

                          90
                  ....*....|.
gi 1363978819 100 GRNVLLFIDEI 110
Cdd:COG0464   249 LAPCVLFIDEA 259
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 21-146 4.29e-04

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: 40.78  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGNLLkegeigglptVESYIisnSNGQEVVKKTTVYAvhnklREIDEEIskg 100
Cdd:cd19502    41 LLYGPPGTGKTLLAKAVANHTDATFIRVVGSEL----------VQKYI---GEGARLVRELFEMA-----REKAPSI--- 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1363978819 101 rnvlLFIDEINRC-----------EHTVQQELMNLIlnREINGYKLHDDVKILAAMN 146
Cdd:cd19502   100 ----IFIDEIDAIgakrfdsgtggDREVQRTMLELL--NQLDGFDPRGNIKVIMATN 150
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 20-117 4.34e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.52  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  20 PLVVGESGIGKTALAKKLAkeneWSLIvidgnllkEGEIgglptvesyiisnsngQEVVKKTTVYAV------------- 86
Cdd:PRK11034  210 PLLVGESGVGKTAIAEGLA----WRIV--------QGDV----------------PEVMADCTIYSLdigsllagtkyrg 261

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1363978819  87 --HNKLREIDEEISKGRNVLLFIDEInrceHTV 117
Cdd:PRK11034  262 dfEKRFKALLKQLEQDTNSILFIDEI----HTI 290
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 21-135 5.11e-04

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 41.31  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKE--NEWSLIVIDGNLLKEGEIggLPTvesyiISNSNGQEvVKKTTVYAVHNKLRE-IDEEI 97
Cdd:COG3267    47 VLTGEVGTGKTTLLRRLLERlpDDVKVAYIPNPQLSPAEL--LRA-----IADELGLE-PKGASKADLLRQLQEfLLELA 118

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1363978819  98 SKGRNVLLFIDEINRCEHTVQQELmNLILNREINGYKL 135
Cdd:COG3267   119 AAGRRVVLIIDEAQNLPPETLEEL-RLLSNLETDSRKL 155
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 21-146 1.64e-03

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 38.96  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  21 LVVGESGIGKTALAKKLAKENEWSLIVIDGnllkegeigglPTVESYIISNSngqevvkkttvyavHNKLREIDEEISKG 100
Cdd:cd19519    38 LLYGPPGTGKTLIARAVANETGAFFFLING-----------PEIMSKLAGES--------------ESNLRKAFEEAEKN 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1363978819 101 RNVLLFIDEI-----------NRCEHTVQQELMNLilnreINGYKLHDDVKILAAMN 146
Cdd:cd19519    93 APAIIFIDEIdaiapkrekthGEVERRIVSQLLTL-----MDGLKQRAHVIVMAATN 144
IPT pfam01745
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ...
 17-49 1.88e-03

Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes isopentenyladensosine 5'-monophosphate, a cytokinin that induces shoot formation on host plants infected with the Ti plasmid.


Pssm-ID: 366786  Cd Length: 232  Bit Score: 39.30  E-value: 1.88e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1363978819  17 GEVPLVVGESGIGKTALAKKLAKENEWSLIVID 49
Cdd:pfam01745   1 MGLYLIWGATCTGKTAEAIALAKETGWPVIVLD 33
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 5-60 2.01e-03

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 39.89  E-value: 2.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1363978819   5 ETLKSVDLVLATGEVPLVVGESGIGKTALAKKLAkenewslividGNLLKEGEIGG 60
Cdd:COG1123    20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALM-----------GLLPHGGRISG 64
clpC CHL00095
Clp protease ATP binding subunit
 20-110 6.26e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 38.50  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1363978819  20 PLVVGESGIGKTALAKKLAK--ENEWSLIVIDGNLLKEGEIGGLPTVESYIISNsngQEVVKKttvyavhnklreIDEEI 97
Cdd:CHL00095  203 PILIGEPGVGKTAIAEGLAQriVNRDVPDILEDKLVITLDIGLLLAGTKYRGEF---EERLKR------------IFDEI 267

                          90
                  ....*....|...
gi 1363978819  98 SKGRNVLLFIDEI 110
Cdd:CHL00095  268 QENNNIILVIDEV 280
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 7-40 7.61e-03

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 37.63  E-value: 7.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1363978819   7 LKSVDLVLATGEVPLVVGESGIGKTALAKKLAKE 40
Cdd:COG2401    46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA 79
 
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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