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Conserved domains on  [gi|50292929|ref|XP_448897|]
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uncharacterized protein GVI51_L02695 [Nakaseomyces glabratus]

Protein Classification

YqeH domain-containing protein( domain architecture ID 10111420)

YqeH domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
83-290 4.89e-44

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


:

Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 154.34  E-value: 4.89e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929  83 CKRCSEALHNNKYNATEFKDIPFEEVEKQIPL-HSNVVHTAPILEFPFHINSQLLKNRTFN-TTMVFTKADRVFK----- 155
Cdd:cd01855   1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNdNALVVHVVDIFDFPGSLIPGLAELIGAKpVILVGNKIDLLPKdvkpn 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 156 -NKKQVQKQIPIFLdaffetylnSKATRNIVTSTLNRWNLDTLFSFLH------GTNYFVGEPNSGKSTLINALLRRLFG 228
Cdd:cd01855  81 rLKQWVKKRLKIGG---------LKIKDVILVSAKKGWGVEELIEEIKklakyrGDVYVVGATNVGKSTLINALLKSNGG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50292929 229 VKIRGNDVknfeldkqaeeelavskkfflekQLAGVSHIPNLTRTLQAYKIK-QKIIYDLPGY 290
Cdd:cd01855 152 KVQAQALV-----------------------QRLTVSPIPGTTLGLIKIPLGeGKKLYDTPGI 191
 
Name Accession Description Interval E-value
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
83-290 4.89e-44

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 154.34  E-value: 4.89e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929  83 CKRCSEALHNNKYNATEFKDIPFEEVEKQIPL-HSNVVHTAPILEFPFHINSQLLKNRTFN-TTMVFTKADRVFK----- 155
Cdd:cd01855   1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNdNALVVHVVDIFDFPGSLIPGLAELIGAKpVILVGNKIDLLPKdvkpn 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 156 -NKKQVQKQIPIFLdaffetylnSKATRNIVTSTLNRWNLDTLFSFLH------GTNYFVGEPNSGKSTLINALLRRLFG 228
Cdd:cd01855  81 rLKQWVKKRLKIGG---------LKIKDVILVSAKKGWGVEELIEEIKklakyrGDVYVVGATNVGKSTLINALLKSNGG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50292929 229 VKIRGNDVknfeldkqaeeelavskkfflekQLAGVSHIPNLTRTLQAYKIK-QKIIYDLPGY 290
Cdd:cd01855 152 KVQAQALV-----------------------QRLTVSPIPGTTLGLIKIPLGeGKKLYDTPGI 191
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
17-370 4.25e-09

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 58.40  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929    17 CNSCGVKLQNKQPGALGYytkkddnlVKKITLEdvkylifgqdiqrikemtvdtenydiklEKPLICKRCSEALHNNKYN 96
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGY--------TPKSALE----------------------------KEEVYCQRCFRLKHYNEIQ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929    97 ATEFKDIPFEEVEKQIpLHSN--VVHTAPILEFPFHINSQLLK-NRTFNTTMVFTKADRVFKNKKqVQKQIPIFLDAFFE 173
Cdd:TIGR03597  45 DVELNDDDFLNLLNSL-GDSNalIVYVVDIFDFEGSLIPELKRfVGGNPVLLVGNKIDLLPKSVN-LSKIKEWMKKRAKE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   174 tyLNSKATRNIVTSTLNRWNLDTLFSFL-HGTN----YFVGEPNSGKSTLINALLrrlfgvkirgndvknfeldkqaeee 248
Cdd:TIGR03597 123 --LGLKPVDIILVSAKKGNGIDELLDKIkKARNkkdvYVVGVTNVGKSSLINKLL------------------------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   249 lavsKKFFLEKQLAGVSHIPNltRTLQAYKIK---QKIIYDLPGYSNYNsyRIDEFIDPKWLQRfrktsIFSEKRVKKKR 325
Cdd:TIGR03597 176 ----KQNNGDKDVITTSPFPG--TTLDLIEIPlddGHSLYDTPGIINSH--QMAHYLDKKDLKY-----ITPKKEIKPKT 242
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 50292929   326 YDSivgnENGKCLTLGGIF---YLVPPPTTinqIVCYIPGELRqFHNT 370
Cdd:TIGR03597 243 YQL----NPNQTLFLGGLArfdYLKGEKTS---FTFYVSNELN-IHRT 282
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
207-289 5.13e-06

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 45.30  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   207 FVGEPNSGKSTLINALLRRlfgvkirgndvknfeldkqaeeelavskkfflekqLAGVSHIPNLTRTLQAYKIKQK---- 282
Cdd:pfam01926   4 LVGRPNVGKSTLINALTGA-----------------------------------KAIVSDYPGTTRDPNEGRLELKgkqi 48

                  ....*..
gi 50292929   283 IIYDLPG 289
Cdd:pfam01926  49 ILVDTPG 55
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
207-290 2.36e-04

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 42.37  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 207 FVGEPNSGKSTLINALLRRlfgvkirgndvknfeldkqaeeelavskkffleKQLAGVSHIPNLTRTLQAYKI-KQKIIY 285
Cdd:COG0218  28 FAGRSNVGKSSLINALTNR---------------------------------KKLARTSKTPGKTQLINFFLInDKFYLV 74

                ....*
gi 50292929 286 DLPGY 290
Cdd:COG0218  75 DLPGY 79
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
208-225 7.15e-04

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 42.02  E-value: 7.15e-04
                         10
                 ....*....|....*...
gi 50292929  208 VGEPNSGKSTLINALLRR 225
Cdd:PRK05291 221 AGRPNVGKSSLLNALLGE 238
 
Name Accession Description Interval E-value
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
83-290 4.89e-44

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 154.34  E-value: 4.89e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929  83 CKRCSEALHNNKYNATEFKDIPFEEVEKQIPL-HSNVVHTAPILEFPFHINSQLLKNRTFN-TTMVFTKADRVFK----- 155
Cdd:cd01855   1 CQRCFKLKHYNKLLDVEIPDEDFLEILSTLLNdNALVVHVVDIFDFPGSLIPGLAELIGAKpVILVGNKIDLLPKdvkpn 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 156 -NKKQVQKQIPIFLdaffetylnSKATRNIVTSTLNRWNLDTLFSFLH------GTNYFVGEPNSGKSTLINALLRRLFG 228
Cdd:cd01855  81 rLKQWVKKRLKIGG---------LKIKDVILVSAKKGWGVEELIEEIKklakyrGDVYVVGATNVGKSTLINALLKSNGG 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50292929 229 VKIRGNDVknfeldkqaeeelavskkfflekQLAGVSHIPNLTRTLQAYKIK-QKIIYDLPGY 290
Cdd:cd01855 152 KVQAQALV-----------------------QRLTVSPIPGTTLGLIKIPLGeGKKLYDTPGI 191
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
17-370 4.25e-09

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 58.40  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929    17 CNSCGVKLQNKQPGALGYytkkddnlVKKITLEdvkylifgqdiqrikemtvdtenydiklEKPLICKRCSEALHNNKYN 96
Cdd:TIGR03597   1 CIGCGAAIQTTDPKKPGY--------TPKSALE----------------------------KEEVYCQRCFRLKHYNEIQ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929    97 ATEFKDIPFEEVEKQIpLHSN--VVHTAPILEFPFHINSQLLK-NRTFNTTMVFTKADRVFKNKKqVQKQIPIFLDAFFE 173
Cdd:TIGR03597  45 DVELNDDDFLNLLNSL-GDSNalIVYVVDIFDFEGSLIPELKRfVGGNPVLLVGNKIDLLPKSVN-LSKIKEWMKKRAKE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   174 tyLNSKATRNIVTSTLNRWNLDTLFSFL-HGTN----YFVGEPNSGKSTLINALLrrlfgvkirgndvknfeldkqaeee 248
Cdd:TIGR03597 123 --LGLKPVDIILVSAKKGNGIDELLDKIkKARNkkdvYVVGVTNVGKSSLINKLL------------------------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   249 lavsKKFFLEKQLAGVSHIPNltRTLQAYKIK---QKIIYDLPGYSNYNsyRIDEFIDPKWLQRfrktsIFSEKRVKKKR 325
Cdd:TIGR03597 176 ----KQNNGDKDVITTSPFPG--TTLDLIEIPlddGHSLYDTPGIINSH--QMAHYLDKKDLKY-----ITPKKEIKPKT 242
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 50292929   326 YDSivgnENGKCLTLGGIF---YLVPPPTTinqIVCYIPGELRqFHNT 370
Cdd:TIGR03597 243 YQL----NPNQTLFLGGLArfdYLKGEKTS---FTFYVSNELN-IHRT 282
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
207-290 1.32e-06

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 48.66  E-value: 1.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 207 FVGEPNSGKSTLINALLRRlfgvkirgndvknfeldkqaeeelavskkffleKQLAGVSHIPNLTRTLQAYKIKQKIIY- 285
Cdd:cd01876   4 FAGRSNVGKSSLINALTNR---------------------------------KKLARTSKTPGRTQLINFFNVGDKFRLv 50

                ....*
gi 50292929 286 DLPGY 290
Cdd:cd01876  51 DLPGY 55
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
207-289 5.13e-06

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 45.30  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   207 FVGEPNSGKSTLINALLRRlfgvkirgndvknfeldkqaeeelavskkfflekqLAGVSHIPNLTRTLQAYKIKQK---- 282
Cdd:pfam01926   4 LVGRPNVGKSTLINALTGA-----------------------------------KAIVSDYPGTTRDPNEGRLELKgkqi 48

                  ....*..
gi 50292929   283 IIYDLPG 289
Cdd:pfam01926  49 ILVDTPG 55
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
208-225 1.43e-04

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: 42.48  E-value: 1.43e-04
                        10
                ....*....|....*...
gi 50292929 208 VGEPNSGKSTLINALLRR 225
Cdd:cd04164   9 AGKPNVGKSSLLNALAGR 26
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
207-290 2.36e-04

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 42.37  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 207 FVGEPNSGKSTLINALLRRlfgvkirgndvknfeldkqaeeelavskkffleKQLAGVSHIPNLTRTLQAYKI-KQKIIY 285
Cdd:COG0218  28 FAGRSNVGKSSLINALTNR---------------------------------KKLARTSKTPGKTQLINFFLInDKFYLV 74

                ....*
gi 50292929 286 DLPGY 290
Cdd:COG0218  75 DLPGY 79
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
146-223 2.38e-04

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 42.39  E-value: 2.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 146 VFTKADRVfkNKKQVQKQIPIFLDAFFETylnskatrnIVTSTLNRWNLDTLFSFLHG-TNYFVGepNS--GKSTLINAL 222
Cdd:cd01854  39 VLNKADLV--DDEELEELLEIYEKLGYPV---------LAVSAKTGEGLDELRELLKGkTSVLVG--QSgvGKSTLLNAL 105

                .
gi 50292929 223 L 223
Cdd:cd01854 106 L 106
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
146-223 4.46e-04

Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 42.41  E-value: 4.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 146 VFTKADRVfknkkqvqkqIPIFLDAFFETYlnskatRNI-----VTSTLNRWNLDTLFSFLHG-TNYFVGepNSG--KST 217
Cdd:COG1162 120 VLNKADLA----------DDEELEELLAIY------EALgypvlAVSAKTGEGLDELRELLKGkTSVLVG--QSGvgKST 181

                ....*.
gi 50292929 218 LINALL 223
Cdd:COG1162 182 LINALL 187
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
144-223 4.60e-04

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 40.99  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929   144 TMVFTKADRVFkNKKQVQKQIPIFLDAFFETylnskatrnIVTSTLNRWNLDTLFSFLHG-TNYFVGEPNSGKSTLINAL 222
Cdd:pfam03193  57 VIVLNKIDLLD-EEEELEELLKIYRAIGYPV---------LFVSAKTGEGIEALKELLKGkTTVLAGQSGVGKSTLLNAL 126

                  .
gi 50292929   223 L 223
Cdd:pfam03193 127 L 127
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
208-225 6.27e-04

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 42.36  E-value: 6.27e-04
                        10
                ....*....|....*...
gi 50292929 208 VGEPNSGKSTLINALLRR 225
Cdd:COG0486 219 VGRPNVGKSSLLNALLGE 236
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
208-225 7.15e-04

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 42.02  E-value: 7.15e-04
                         10
                 ....*....|....*...
gi 50292929  208 VGEPNSGKSTLINALLRR 225
Cdd:PRK05291 221 AGRPNVGKSSLLNALLGE 238
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
145-289 8.00e-04

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 40.20  E-value: 8.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 145 MVFTKAD-------RVFKNKKQVQKQIPIFLDAffetylNSKATRNIVTSTLNRWNLDTLFSFLHGTNY------FVGEP 211
Cdd:cd01856  51 IVLNKADladpaktKKWLKYFKSQGEPVLFVNA------KNGKGVKKLLKKAKKLLKENEKLKAKGLLPrplramVVGIP 124
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50292929 212 NSGKSTLINALLRrlfgvkirgndvknfeldkqaeeelavskkffleKQLAGVSHIPNLTRTLQAYKIKQKI-IYDLPG 289
Cdd:cd01856 125 NVGKSTLINRLRG----------------------------------KKVAKVGNKPGVTRGQQWIRIGPNIeLLDTPG 169
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
207-318 9.91e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.92  E-value: 9.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 207 FVGEPNSGKSTLINALLRrlfgvkirgndvknfelDKQAEeelavskkfflekqlagVSHIPNLTRTLQAYKIKQKI--- 283
Cdd:cd00880   2 IFGRPNVGKSSLLNALLG-----------------QNVGI-----------------VSPIPGTTRDPVRKEWELLPlgp 47
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 50292929 284 --IYDLPGysnynsyrIDEFIDpkwLQRFRKTSIFSE 318
Cdd:cd00880  48 vvLIDTPG--------LDEEGG---LGRERVEEARQV 73
PRK12288 PRK12288
small ribosomal subunit biogenesis GTPase RsgA;
146-236 1.91e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237039 [Multi-domain]  Cd Length: 347  Bit Score: 40.61  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929  146 VFTKADRVF-KNKKQVQKQIPIFLDAFFETYLNSKATRNivtstlnrwNLDTLFSFL-HGTNYFVGEPNSGKSTLINALL 223
Cdd:PRK12288 156 VLNKIDLLDdEGRAFVNEQLDIYRNIGYRVLMVSSHTGE---------GLEELEAALtGRISIFVGQSGVGKSSLINALL 226
                         90
                 ....*....|...
gi 50292929  224 RrlfGVKIRGNDV 236
Cdd:PRK12288 227 P---EAEILVGDV 236
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
208-225 3.01e-03

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 39.77  E-value: 3.01e-03
                          10
                  ....*....|....*...
gi 50292929   208 VGEPNSGKSTLINALLRR 225
Cdd:pfam12631 100 VGKPNVGKSSLLNALLGE 117
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
207-231 3.62e-03

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.59  E-value: 3.62e-03
                        10        20
                ....*....|....*....|....*
gi 50292929 207 FVGEPNSGKSTLINALLrrlfGVKI 231
Cdd:COG1159   8 IVGRPNVGKSTLLNALV----GQKV 28
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
207-224 4.35e-03

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 38.18  E-value: 4.35e-03
                        10
                ....*....|....*...
gi 50292929 207 FVGEPNSGKSTLINALLR 224
Cdd:cd01895   7 IIGRPNVGKSSLLNALLG 24
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
197-289 4.50e-03

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 37.75  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50292929 197 LFSFLHGTNYFVGEPNSGKSTLINALLrrlfgvkirgndvknfeldkqaeeelavsKKFFLEkqlagVSHIPNLTRTLQA 276
Cdd:cd01849  86 LKYKKGIRVGVVGLPNVGKSSFINALL-----------------------------NKFKLK-----VGSIPGTTKLQQD 131
                        90
                ....*....|....
gi 50292929 277 YKIKQKI-IYDLPG 289
Cdd:cd01849 132 VKLDKEIyLYDTPG 145
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
207-231 5.17e-03

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 37.83  E-value: 5.17e-03
                        10        20
                ....*....|....*....|....*
gi 50292929 207 FVGEPNSGKSTLINALLrrlfGVKI 231
Cdd:cd04163   8 IIGRPNVGKSTLLNALV----GQKI 28
era PRK00089
GTPase Era; Reviewed
207-231 5.70e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 38.88  E-value: 5.70e-03
                         10        20
                 ....*....|....*....|....*
gi 50292929  207 FVGEPNSGKSTLINALLrrlfGVKI 231
Cdd:PRK00089  10 IVGRPNVGKSTLLNALV----GQKI 30
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
207-223 6.91e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 38.88  E-value: 6.91e-03
                         10
                 ....*....|....*..
gi 50292929  207 FVGEPNSGKSTLINALL 223
Cdd:PRK00093 178 IIGRPNVGKSSLINALL 194
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
207-224 8.06e-03

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 37.53  E-value: 8.06e-03
                        10
                ....*....|....*...
gi 50292929 207 FVGEPNSGKSTLINALLR 224
Cdd:cd09912   5 VVGEFSAGKSTLLNALLG 22
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
207-223 8.18e-03

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.85  E-value: 8.18e-03
                        10
                ....*....|....*..
gi 50292929 207 FVGEPNSGKSTLINALL 223
Cdd:COG1160 180 IVGRPNVGKSSLINALL 196
 
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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