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Conserved domains on  [gi|495167072|ref|WP_007891869|]
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AAA family ATPase [Cronobacter sakazakii]

Protein Classification

COG3911 family protein( domain architecture ID 10008129)

COG3911 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3911 COG3911
Predicted ATPase [General function prediction only];
4-178 2.72e-93

Predicted ATPase [General function prediction only];


:

Pssm-ID: 443117  Cd Length: 180  Bit Score: 268.99  E-value: 2.72e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   4 TTRKIVITGGPGAGKSTLLASLARAGLNTSPETGRAIIQEQVSAGGVALPWLDREAFAAMMLNREKQAWYAADAMNDVVF 83
Cdd:COG3911    2 MTRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIGGDALPWTDPAAFAELMLEGRLRQYREAEALSGPVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072  84 FDRGIPDIIGYLNLCELPVPQTLHDAALRLRYDATVFIAPPWKAIFTQDAERRQTFEEAVRTWEAMKQVYTRYGYELAEI 163
Cdd:COG3911   82 FDRGIPDVLAYLRLLGLPVPEHLETAAAAFRYDRTVFILPPWPEIYTQDAERKQSFEEALRTYEALVETYRALGYELIEV 161

                        170
                 ....*....|....*
gi 495167072 164 PFATPQARADWIRAQ 178
Cdd:COG3911  162 PKGSVEERVDFILSR 176
 
Name Accession Description Interval E-value
COG3911 COG3911
Predicted ATPase [General function prediction only];
4-178 2.72e-93

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 268.99  E-value: 2.72e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   4 TTRKIVITGGPGAGKSTLLASLARAGLNTSPETGRAIIQEQVSAGGVALPWLDREAFAAMMLNREKQAWYAADAMNDVVF 83
Cdd:COG3911    2 MTRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIGGDALPWTDPAAFAELMLEGRLRQYREAEALSGPVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072  84 FDRGIPDIIGYLNLCELPVPQTLHDAALRLRYDATVFIAPPWKAIFTQDAERRQTFEEAVRTWEAMKQVYTRYGYELAEI 163
Cdd:COG3911   82 FDRGIPDVLAYLRLLGLPVPEHLETAAAAFRYDRTVFILPPWPEIYTQDAERKQSFEEALRTYEALVETYRALGYELIEV 161

                        170
                 ....*....|....*
gi 495167072 164 PFATPQARADWIRAQ 178
Cdd:COG3911  162 PKGSVEERVDFILSR 176
AAA_28 pfam13521
AAA domain;
7-171 1.17e-43

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 142.79  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072    7 KIVITGGPGAGKSTLLASLA-RAGLNTSPETGRAIIQEQVSAGGVALPW-LDREAFAAMMLNREKQAwYAADAMNDVVFF 84
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALAaRFGYPVVPEAAREILEELGADGGDALPWvEDLLAFARGVLEAQLED-EAAAAANDLLFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   85 DRGIPDIIGYLNLCELPVPQTLHDAALRLRYDAtVFIAPPWKAIfTQDAERRQTFEEAVRTWEAMKQVYTRYGYELAEIP 164
Cdd:pfam13521  80 DRGPLDTLAYSRAYGGPCPPELEAAARASRYDL-VFLLPPDPEI-VQDGERREDPEERERFHERLREALRELGIPVIIVP 157


                  ....*..
gi 495167072  165 FATPQAR 171
Cdd:pfam13521 158 RGSVEER 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 8-85 1.50e-04

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: 40.21  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495167072   8 IVITGGPGAGKSTLLASLARAglntSPETGRAIIqeQVSAGGVALPWLDREAFAAMMLNREKQAwyAADAMNDVVFFD 85
Cdd:cd00009   22 LLLYGPPGTGKTTLARAIANE----LFRPGAPFL--YLNASDLLEGLVVAELFGHFLVRLLFEL--AEKAKPGVLFID 91
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 6-85 9.53e-04

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: 38.12  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072     6 RKIVITGGPGAGKSTLLASLARA---------GLNTSPETGRAIIQEQVSAGGVALPWLDREAFAAMMLNRekqawyAAD 76
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARElgppgggviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL------ARK 76


                   ....*....
gi 495167072    77 AMNDVVFFD 85
Cdd:smart00382  77 LKPDVLILD 85
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 5-50 8.55e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 35.43  E-value: 8.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 495167072    5 TRKIVITGGPGAGKSTLLASLA---RAGLNTSPETGRAIIQEQVSAGGV 50
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnkGSITEYYPGTTRNYVTTVIEEDGK 49
 
Name Accession Description Interval E-value
COG3911 COG3911
Predicted ATPase [General function prediction only];
4-178 2.72e-93

Predicted ATPase [General function prediction only];


Pssm-ID: 443117  Cd Length: 180  Bit Score: 268.99  E-value: 2.72e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   4 TTRKIVITGGPGAGKSTLLASLARAGLNTSPETGRAIIQEQVSAGGVALPWLDREAFAAMMLNREKQAWYAADAMNDVVF 83
Cdd:COG3911    2 MTRRIVITGGPGSGKTTLLNALARRGYACVPEAGREIIREQQAIGGDALPWTDPAAFAELMLEGRLRQYREAEALSGPVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072  84 FDRGIPDIIGYLNLCELPVPQTLHDAALRLRYDATVFIAPPWKAIFTQDAERRQTFEEAVRTWEAMKQVYTRYGYELAEI 163
Cdd:COG3911   82 FDRGIPDVLAYLRLLGLPVPEHLETAAAAFRYDRTVFILPPWPEIYTQDAERKQSFEEALRTYEALVETYRALGYELIEV 161

                        170
                 ....*....|....*
gi 495167072 164 PFATPQARADWIRAQ 178
Cdd:COG3911  162 PKGSVEERVDFILSR 176
AAA_28 pfam13521
AAA domain;
7-171 1.17e-43

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 142.79  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072    7 KIVITGGPGAGKSTLLASLA-RAGLNTSPETGRAIIQEQVSAGGVALPW-LDREAFAAMMLNREKQAwYAADAMNDVVFF 84
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEALAaRFGYPVVPEAAREILEELGADGGDALPWvEDLLAFARGVLEAQLED-EAAAAANDLLFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   85 DRGIPDIIGYLNLCELPVPQTLHDAALRLRYDAtVFIAPPWKAIfTQDAERRQTFEEAVRTWEAMKQVYTRYGYELAEIP 164
Cdd:pfam13521  80 DRGPLDTLAYSRAYGGPCPPELEAAARASRYDL-VFLLPPDPEI-VQDGERREDPEERERFHERLREALRELGIPVIIVP 157


                  ....*..
gi 495167072  165 FATPQAR 171
Cdd:pfam13521 158 RGSVEER 164
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 5-154 1.04e-08

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 52.13  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   5 TRKIVITGGPGAGKSTLLASLARAgLNT--SPETGRAIIQEQVSAggvalpwLDREAFAAMM---LNREKQAwyAADAmN 79
Cdd:COG3172    8 VKKIVLLGAESTGKTTLARALAAH-YNTpwVPEYGREYLEEKGRA-------LTYDDLLAIArgqLALEDAA--AKRA-N 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072  80 DVVFFDRGIPDIIGYLNLCELPVPQTLHDAALRLRYDATVFIAP--PWkaifTQDAER-----RQTFEEAVRTW-EAMKQ 151
Cdd:COG3172   77 KLLFCDTDALTTKVYSELYFGKCPPWLEALAAQRRYDLYLLLDPdiPW----VADGLRdgpevREEFQQLLREElEERGI 152


                 ...
gi 495167072 152 VYT 154
Cdd:COG3172  153 PYV 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 8-85 1.50e-04

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: 40.21  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495167072   8 IVITGGPGAGKSTLLASLARAglntSPETGRAIIqeQVSAGGVALPWLDREAFAAMMLNREKQAwyAADAMNDVVFFD 85
Cdd:cd00009   22 LLLYGPPGTGKTTLARAIANE----LFRPGAPFL--YLNASDLLEGLVVAELFGHFLVRLLFEL--AEKAKPGVLFID 91
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 1-39 4.74e-04

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 39.96  E-value: 4.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495167072   1 MISTTRKI-VITGGPGAGKSTLLASLARA----GLN---TSPeTGRA 39
Cdd:COG0507  135 LALTTRRVsVLTGGAGTGKTTTLRALLAAlealGLRvalAAP-TGKA 180
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 6-44 7.44e-04

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 38.40  E-value: 7.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 495167072    6 RKIVITGGPGAGKSTLLASLARaglNTSPETGRAIIQEQ 44
Cdd:pfam00005  12 EILALVGPNGAGKSTLLKLIAG---LLSPTEGTILLDGQ 47
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 6-85 9.53e-04

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: 38.12  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072     6 RKIVITGGPGAGKSTLLASLARA---------GLNTSPETGRAIIQEQVSAGGVALPWLDREAFAAMMLNRekqawyAAD 76
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARElgppgggviYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL------ARK 76


                   ....*....
gi 495167072    77 AMNDVVFFD 85
Cdd:smart00382  77 LKPDVLILD 85
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
3-27 1.75e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 38.63  E-value: 1.75e-03
                         10        20
                 ....*....|....*....|....*
gi 495167072   3 STTRKIVITGGPGAGKSTLLASLAR 27
Cdd:COG5635  178 AKKKRLLILGEPGSGKTTLLRYLAL 202
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 6-47 1.84e-03

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 37.75  E-value: 1.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 495167072   6 RKIVITGGPGAGKSTLLASLARAglnTSPETGRAIIQEQVSA 47
Cdd:COG1134   53 ESVGIIGRNGAGKSTLLKLIAGI---LEPTSGRVEVNGRVSA 91
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 6-67 2.08e-03

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 36.66  E-value: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495167072   6 RKIVITGGPGAGKSTLLASLARAGLNTS--PETGRAIIQ---EQVSaGGvalpWLDREAFAAMMLNR 67
Cdd:cd03221   27 DRIGLVGRNGAGKSTLLKLIAGELEPDEgiVTWGSTVKIgyfEQLS-GG----EKMRLALAKLLLEN 88
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
6-28 2.51e-03

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 36.81  E-value: 2.51e-03
                         10        20
                 ....*....|....*....|...
gi 495167072   6 RKIVITGGPGAGKSTLLASLARA 28
Cdd:COG1618    1 MKIFITGRPGVGKTTLLLKVVEE 23
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 7-88 3.07e-03

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 36.82  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495167072   7 KIVITGGPGAGKSTLLASLA-RAGLNTSPETGraiiqEQVSAGGVALPWL--DREAFAA-----MMLNREKQ--AWYAAD 76
Cdd:cd01673    1 VIVVEGNIGAGKSTLAKELAeHLGYEVVPEPV-----EPDVEGNPFLEKFyeDPKRWAFpfqlyFLLSRLKQykDALEHL 75

                         90
                 ....*....|..
gi 495167072  77 AMNDVVFFDRGI 88
Cdd:cd01673   76 STGQGVILERSI 87
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 8-39 3.15e-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: 36.38  E-value: 3.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 495167072   8 IVITGGPGAGKSTLLASLARAGLNTSPE------TGRA 39
Cdd:cd17933   15 SVLTGGAGTGKTTTLKALLAALEAEGKRvvlaapTGKA 52
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 7-47 4.89e-03

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 36.36  E-value: 4.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495167072   7 KIVITGGPGAGKSTLLASLARAglnTSPETGRAIIQEQVSA 47
Cdd:cd03220   50 RIGLIGRNGAGKSTLLRLLAGI---YPPDSGTVTVRGRVSS 87
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 8-28 5.39e-03

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 36.68  E-value: 5.39e-03
                         10        20
                 ....*....|....*....|.
gi 495167072   8 IVITGGPGAGKSTLLASLARA 28
Cdd:COG4962  185 ILVSGGTGSGKTTLLNALSGF 205
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 7-50 5.85e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 35.55  E-value: 5.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495167072   7 KIVITGGPGAGKSTLLASLAR---------AGlntspeTGRAIIQEQVSAGGV 50
Cdd:cd04164    5 KVVIAGKPNVGKSSLLNALAGrdraivsdiAG------TTRDVIEEEIDLGGI 51
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
 7-25 6.11e-03

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 35.96  E-value: 6.11e-03
                         10
                 ....*....|....*....
gi 495167072   7 KIVITGGPGAGKSTLLASL 25
Cdd:COG2229   14 KIVYAGPFGAGKTTFVRSI 32
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 2-57 6.78e-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: 35.68  E-value: 6.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495167072   2 ISTTRKIVITGGPGAGKSTLLASLARAglnTSPETGRAIIQEQVSAGGVALPWLDR 57
Cdd:cd00267   22 LKAGEIVALVGPNGSGKSTLLRAIAGL---LKPTSGEILIDGKDIAKLPLEELRRR 74
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
 10-40 6.93e-03

GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441309  Cd Length: 317  Bit Score: 36.21  E-value: 6.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 495167072  10 ITGGPGAGKSTLLASLAR----AGLN--------TSPETGRAI 40
Cdd:COG1703   53 ITGVPGAGKSTLIDALGLrlreRGKRvavlavdpSSPFTGGAI 95
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 5-50 8.55e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 35.43  E-value: 8.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 495167072    5 TRKIVITGGPGAGKSTLLASLA---RAGLNTSPETGRAIIQEQVSAGGV 50
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnkGSITEYYPGTTRNYVTTVIEEDGK 49
 
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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