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Conserved domains on  [gi|1084827076|gb|OGQ60799|]
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hypothetical protein A3J24_10305 [Deltaproteobacteria bacterium RIFCSPLOWO2_02_FULL_53_8]

Protein Classification

GTP-binding protein( domain architecture ID 10785093)

GTP-binding protein similar to YsxC/EngB, a GTPase associated with ribosome biogenesis; belongs to the large superfamily of translation factor-related (TRAFAC) GTPases

CATH:  3.40.50.300
Gene Ontology:  GO:0046872|GO:0005525
PubMed:  16333325|11916378|11489118
SCOP:  4004043

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-190 1.89e-91

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: 265.40  E-value: 1.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076   1 MKITKAEFAISASKSAVYPKDGLPEILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFG 80
Cdd:COG0218     1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  81 YANVPKKVKAGWEAMIERYVSERPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALK 160
Cdd:COG0218    81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1084827076 161 KLI----PIEHPIIFSSVTGDGKPMLSRKIQEML 190
Cdd:COG0218   161 KALgkdpAAPEVILFSSLKKEGIDELRAAIEEWL 194
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-190 1.89e-91

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: 265.40  E-value: 1.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076   1 MKITKAEFAISASKSAVYPKDGLPEILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFG 80
Cdd:COG0218     1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  81 YANVPKKVKAGWEAMIERYVSERPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALK 160
Cdd:COG0218    81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1084827076 161 KLI----PIEHPIIFSSVTGDGKPMLSRKIQEML 190
Cdd:COG0218   161 KALgkdpAAPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 6-180 2.30e-81

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 239.30  E-value: 2.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076   6 AEFAISASKSAVYPKDGLPEILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFGYANVP 85
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  86 KKVKAGWEAMIERYVSERPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALKKLIPI 165
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 1084827076 166 E----HPIIFSSVTGDGKP 180
Cdd:TIGR03598 161 DaddpSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 25-190 5.07e-69

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: 207.75  E-value: 5.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  25 EILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFGYANVPKKVKAGWEAMIERYVSERP 104
Cdd:cd01876     1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076 105 TLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALKKLI---PIEHPII-FSSVTGDGKP 180
Cdd:cd01876    81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELnlfNILPPVIlFSSKKGTGID 160

                         170
                  ....*....|
gi 1084827076 181 MLSRKIQEML 190
Cdd:cd01876   161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 25-143 5.84e-21

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: 83.05  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  25 EILLVGRSNVGKSSLINAFVNKKglAKTSSVPGKTQTINFYRINDA---FYLVDLPGFgyanvPKKVKAGWeAMIERYVS 101
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKgkqIILVDTPGL-----IEGASEGE-GLGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1084827076 102 ERPTlCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTK 143
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK04213 PRK04213
GTP-binding protein EngB;
19-102 6.64e-15

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 69.56  E-value: 6.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  19 PKDGLPEILLVGRSNVGKSSLINAFVNKKglAKTSSVPGKTQTINFYRINDaFYLVDLPGFGY-ANVPKKVKAGWEAMIE 97
Cdd:PRK04213    5 RPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIV 81


                  ....*
gi 1084827076  98 RYVSE 102
Cdd:PRK04213   82 RYIED 86
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 26-59 5.16e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 35.95  E-value: 5.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1084827076   26 ILLVGRSNVGKSSLINAFVNKK---------G---LAKTSSVPGKT 59
Cdd:smart00175   3 IILIGDSGVGKSSLLSRFTDGKfseqykstiGvdfKTKTIEVDGKR 48
 
Name Accession Description Interval E-value
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
 1-190 1.89e-91

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: 265.40  E-value: 1.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076   1 MKITKAEFAISASKSAVYPKDGLPEILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFG 80
Cdd:COG0218     1 MKIKKAEFVTSAVKLEQLPPDDLPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGKTQLINFFLINDKFYLVDLPGYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  81 YANVPKKVKAGWEAMIERYVSERPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALK 160
Cdd:COG0218    81 YAKVSKAEKEKWQKLIEDYLEGRENLKGVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKLKKSELAKQLKAIK 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1084827076 161 KLI----PIEHPIIFSSVTGDGKPMLSRKIQEML 190
Cdd:COG0218   161 KALgkdpAAPEVILFSSLKKEGIDELRAAIEEWL 194
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 6-180 2.30e-81

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 239.30  E-value: 2.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076   6 AEFAISASKSAVYPKDGLPEILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFGYANVP 85
Cdd:TIGR03598   1 AEFVKSAVKLKQLPPDDGPEIAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFEVNDGFRLVDLPGYGYAKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  86 KKVKAGWEAMIERYVSERPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALKKLIPI 165
Cdd:TIGR03598  81 KEEKEKWQKLIEEYLEKRENLKGVVLLMDIRHPLKELDLEMIEWLRERGIPVLIVLTKADKLKKSELNKQLKKIKKALKK 160

                         170
                  ....*....|....*....
gi 1084827076 166 E----HPIIFSSVTGDGKP 180
Cdd:TIGR03598 161 DaddpSVQLFSSLKKTGID 179
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 25-190 5.07e-69

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: 207.75  E-value: 5.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  25 EILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGFGYANVPKKVKAGWEAMIERYVSERP 104
Cdd:cd01876     1 EVAFAGRSNVGKSSLINALTNRKKLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAKVSKEVREKWGKLIEEYLENRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076 105 TLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALKKLI---PIEHPII-FSSVTGDGKP 180
Cdd:cd01876    81 NLKGVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELnlfNILPPVIlFSSKKGTGID 160

                         170
                  ....*....|
gi 1084827076 181 MLSRKIQEML 190
Cdd:cd01876   161 ELRALIAEWL 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 25-143 5.84e-21

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: 83.05  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  25 EILLVGRSNVGKSSLINAFVNKKglAKTSSVPGKTQTINFYRINDA---FYLVDLPGFgyanvPKKVKAGWeAMIERYVS 101
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK--AIVSDYPGTTRDPNEGRLELKgkqIILVDTPGL-----IEGASEGE-GLGRAFLA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1084827076 102 ERPTlCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTK 143
Cdd:pfam01926  73 IIEA-DLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 27-178 5.84e-19

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 79.42  E-value: 5.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  27 LLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRI-----NDAFYLVDLPGFGYANVPkkvkagWEAMIERYVS 101
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGE-VGEVSDVPGTTRDPDVYVKeldkgKVKLVLVDTPGLDEFGGL------GREELARLLL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084827076 102 ERPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALKKLIPIEHPII-FSSVTGDG 178
Cdd:cd00882    74 RGADLILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFeVSAKTGEG 151
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 28-190 1.91e-18

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: 78.06  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRI----NDAFYLVDLPGFGYANVPKkvkagwEAMIERYVSER 103
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQN-VGIVSPIPGTTRDPVRKEWellpLGPVVLIDTPGLDEEGGLG------RERVEEARQVA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076 104 PTLCGAMVILDPRRDPGDVEERVYsWLLGECIPHATVFTKADKLSKNELSSRLA-ALKKLIPIEHPIIFSSVTGDGKPML 182
Cdd:cd00880    75 DRADLVLLVVDSDLTPVEEEAKLG-LLRERGKPVLLVLNKIDLVPESEEEELLReRKLELLPDLPVIAVSALPGEGIDEL 153


                  ....*...
gi 1084827076 183 SRKIQEML 190
Cdd:cd00880   154 RKKIAELL 161
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
28-192 6.25e-16

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 73.87  E-value: 6.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVP-------------GKTQTInfyrindafyLVDLPGFgyaNVPKK------V 88
Cdd:COG1159     8 IVGRPNVGKSTLLNALVGQK-VSIVSPKPqttrhrirgivtrEDAQIV----------FVDTPGI---HKPKRklgrrmN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  89 KAGWEAMIEryvserptlcgAMVIL---DPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNELSSRLAALKKLIPI 165
Cdd:COG1159    74 KAAWSALED-----------VDVILfvvDATEKIGEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDF 142

                         170       180
                  ....*....|....*....|....*...
gi 1084827076 166 EHPIIFSSVTGDGKPMLSRKIQEML-EG 192
Cdd:COG1159   143 AEIVPISALKGDNVDELLDEIAKLLpEG 170
PRK04213 PRK04213
GTP-binding protein EngB;
19-102 6.64e-15

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 69.56  E-value: 6.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  19 PKDGLPEILLVGRSNVGKSSLINAFVNKKglAKTSSVPGKTQTINFYRINDaFYLVDLPGFGY-ANVPKKVKAGWEAMIE 97
Cdd:PRK04213    5 RPDRKPEIVFVGRSNVGKSTLVRELTGKK--VRVGKRPGVTRKPNHYDWGD-FILTDLPGFGFmSGVPKEVQEKIKDEIV 81


                  ....*
gi 1084827076  98 RYVSE 102
Cdd:PRK04213   82 RYIED 86
era PRK00089
GTPase Era; Reviewed
 28-192 1.86e-14

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 69.69  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTinfyRI------NDA-FYLVDLPGFgyaNVPKK------VKAGWEA 94
Cdd:PRK00089   10 IVGRPNVGKSTLLNALVGQK-ISIVSPKPQTTRH----RIrgivteDDAqIIFVDTPGI---HKPKRalnramNKAAWSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  95 MIEryvserptlcgAMVIL---DPRRDPGDVEERVYSWLLGECIPHATVFTKADKL-SKNELSSRLAALKKLIPIEHPII 170
Cdd:PRK00089   82 LKD-----------VDLVLfvvDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVkDKEELLPLLEELSELMDFAEIVP 150

                         170       180
                  ....*....|....*....|...
gi 1084827076 171 FSSVTGDGKPMLSRKIQEML-EG 192
Cdd:PRK00089  151 ISALKGDNVDELLDVIAKYLpEG 173
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 28-190 5.87e-13

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: 63.63  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVP-------------GKTQTInfyrindafyLVDLPGFgyanVPKKVKAGwEA 94
Cdd:cd04163     8 IIGRPNVGKSTLLNALVGQK-ISIVSPKPqttrnrirgiytdDDAQII----------FVDTPGI----HKPKKKLG-ER 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  95 MIeRYVSErpTLCGAMVIL---DPRRDPGDVEERVYSWLLGECIPHATVFTKADKLS-KNELSSRLAALKKLIPIEHPII 170
Cdd:cd04163    72 MV-KAAWS--ALKDVDLVLfvvDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKdKEDLLPLLEKLKELHPFAEIFP 148

                         170       180
                  ....*....|....*....|
gi 1084827076 171 FSSVTGDGKPMLSRKIQEML 190
Cdd:cd04163   149 ISALKGENVDELLEYIVEYL 168
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 1-78 1.22e-12

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: 62.93  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076   1 MKITKAEFAISASKSAVYPKDGLPE---ILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRINDAFYLVDLP 77
Cdd:cd01856    90 KKLLKKAKKLLKENEKLKAKGLLPRplrAMVVGIPNVGKSTLINRLRGKK-VAKVGNKPGVTRGQQWIRIGPNIELLDTP 168


                  .
gi 1084827076  78 G 78
Cdd:cd01856   169 G 169
YeeP COG3596
Predicted GTPase [General function prediction only];
24-148 4.88e-11

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 60.16  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  24 PEILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRIN----DAFYLVDLPGFGYANVPKKvkagWEAMIERY 99
Cdd:COG3596    40 PVIALVGKTGAGKSSLINALFGAE-VAEVGVGRPCTREIQRYRLEsdglPGLVLLDTPGLGEVNERDR----EYRELREL 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084827076 100 VserPTLCGAMVILDPRRDPGDVEERVYSWLLGECIPHATVF--TKADKLS 148
Cdd:COG3596   115 L---PEADLILWVVKADDRALATDEEFLQALRAQYPDPPVLVvlTQVDRLE 162
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
26-192 1.22e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 57.68  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKK-GLAKTSSVPGKTQTINFYRINDA---FYLVDLPGfgyanvpkkvkagweamIERYVS 101
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIfSLEKYLSTNGVTIDKKELKLDGLdvdLVIWDTPG-----------------QDEFRE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076 102 ERPTL-------CGAMVILDPRRDPGDVEErvYSWL-----LGECIPHATVFTKADKLSKNELSS--RLAALKKLIPIEH 167
Cdd:COG1100    69 TRQFYarqltgaSLYLFVVDGTREETLQSL--YELLeslrrLGKKSPIILVLNKIDLYDEEEIEDeeRLKEALSEDNIVE 146

                         170       180
                  ....*....|....*....|....*
gi 1084827076 168 PIIFSSVTGDGKPMLSRKIQEMLEG 192
Cdd:COG1100   147 VVATSAKTGEGVEELFAALAEILRG 171
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
 28-78 1.20e-09

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 54.16  E-value: 1.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVPGKT---QTINfyrINDAFYLVDLPG 78
Cdd:cd01857    87 LVGYPNVGKSSLINALVGSK-KVSVSSTPGKTkhfQTIF---LEPGITLCDCPG 136
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 26-79 6.32e-09

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: 53.04  E-value: 6.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084827076  26 ILLVGRSNVGKSSLINA----------FVNKKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGF 79
Cdd:cd01855   128 VYVVGATNVGKSTLINAllksnggkvqAQALVQRLTVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
10-78 1.00e-08

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 53.57  E-value: 1.00e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084827076  10 ISASKSAVYPKDGLPE---ILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRINDAFYLVDLPG 78
Cdd:COG1161    97 IEAIRELAPEKGIKRRpirVMIVGIPNVGKSTLINRLAGKK-VAKTGNKPGVTKGQQWIKLDDGLELLDTPG 167
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
 26-78 2.55e-08

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 52.13  E-value: 2.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRINDAFYLVDLPG 78
Cdd:TIGR03596 121 AMIVGIPNVGKSTLINRLAGKK-VAKVGNRPGVTKGQQWIKLSDNLELLDTPG 172
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 20-192 9.12e-08

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: 50.83  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  20 KDGLPeILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKT-----QTINFYRIndAFYLVDlpgfgyanvpkkvKAGW-- 92
Cdd:COG0486   211 REGIK-VVIVGRPNVGKSSLLNALLGEE-RAIVTDIAGTTrdvieERINIGGI--PVRLID-------------TAGLre 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  93 -----EAM-IERYVSErptLCGAMVIL---DPRRDPGDVEERVYSWLLGecIPHATVFTKADklskneLSSRLAALKKLI 163
Cdd:COG0486   274 tedevEKIgIERAREA---IEEADLVLlllDASEPLTEEDEEILEKLKD--KPVIVVLNKID------LPSEADGELKSL 342

                         170       180
                  ....*....|....*....|....*....
gi 1084827076 164 PIEHPIIFSSVTGDGKPMLSRKIQEMLEG 192
Cdd:COG0486   343 PGEPVIAISAKTGEGIDELKEAILELVGE 371
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 28-78 1.38e-07

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 48.85  E-value: 1.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKGlAKTSSVPGK---TQTINFYRINDAFYLVDLPG 78
Cdd:cd01859   104 VVGYPKVGKSSIINALKGRHS-ASTSPIPGSpgyTKGIQLVRIDSKIYLIDTPG 156
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 1-79 6.71e-07

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: 46.61  E-value: 6.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084827076   1 MKITKAEFAISASKSAVYPKDGlpEILLVGRSNVGKSSLINAFVNKKGLaKTSSVPGKTQTINFYRINDAFYLVDLPGF 79
Cdd:cd01849    71 GILKLKAEITKQKLKLKYKKGI--RVGVVGLPNVGKSSFINALLNKFKL-KVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
 29-79 1.96e-06

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: 46.84  E-value: 1.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1084827076  29 VGRSNVGKSSLINAFVN----KKGLAKTSSVPGKTQTINFYRINDAFYLVDLPGF 79
Cdd:TIGR03597 160 VGVTNVGKSSLINKLLKqnngDKDVITTSPFPGTTLDLIEIPLDDGHSLYDTPGI 214
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
 28-78 3.23e-06

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 44.98  E-value: 3.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRINDAFYLVDLPG 78
Cdd:cd01858   107 FIGYPNVGKSSVINTLRSKK-VCKVAPIPGETKVWQYITLMKRIYLIDCPG 156
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 20-59 5.51e-06

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: 44.41  E-value: 5.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1084827076  20 KDGLpEILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKT 59
Cdd:cd04164     1 REGI-KVVIAGKPNVGKSSLLNALAGRD-RAIVSDIAGTT 38
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 26-78 2.01e-05

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 42.82  E-value: 2.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKglAKTSSVPGKT---QTINFYRINDAFYLVDLPG 78
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGAN--QHVGNWPGVTvekKEGKFKYKGYEIEIVDLPG 56
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 26-173 2.42e-05

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: 42.80  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKGLAkTSSVPGKTQ---TINFYRINDAFYLVDLPGfgyanVPKKVKAGWEamIERYVSE 102
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALLGEERVI-VSDIAGTTRdsiDVPFEYDGQKYTLIDTAG-----IRKKGKVTEG--IEKYSVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076 103 RpTLcGAM-------VILDPRRDPGDVEERVYSWLLGECIPHATVFTKADKLSKNElsSRLAALKKLI-----PIEH-PI 169
Cdd:cd01895    77 R-TL-KAIeradvvlLVLDASEGITEQDLRIAGLILEEGKALIIVVNKWDLVEKDE--KTMKEFEKELrrklpFLDYaPI 152


                  ....
gi 1084827076 170 IFSS 173
Cdd:cd01895   153 VFIS 156
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 28-79 3.72e-05

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first 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: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 42.04  E-value: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRI---NDAFYLVDLPGF 79
Cdd:cd01894     2 IVGRPNVGKSTLFNRLTGRR-DAIVSDTPGVTRDRKYGEAewgGREFILIDTGGI 55
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
19-59 4.08e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 43.09  E-value: 4.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1084827076  19 PKDGLPEILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKT 59
Cdd:COG1160   171 EEDDPIKIAIVGRPNVGKSSLINALLGEE-RVIVSDIAGTT 210
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 28-79 5.20e-05

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: 5.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKGLaKTSSVPGKTQ-------TINFYRINDAFYLVDLPGF 79
Cdd:cd01854    90 LVGQSGVGKSTLLNALLPELVL-ATGEISEKLGrgrhtttHRELFPLPGGGLIIDTPGF 147
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 26-80 6.84e-05

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: 41.76  E-value: 6.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKGLaKTSSVPgKTQTINF--YRINDAFYLVDLPGFG 80
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEEVL-PTGVTP-TTAVITVlrYGLLKGVVLVDTPGLN 57
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 23-79 7.76e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 42.34  E-value: 7.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084827076  23 LPEILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINfY---RIND-AFYLVDLPGF 79
Cdd:PRK00093    1 KPVVAIVGRPNVGKSTLFNRLTGKR-DAIVADTPGVTRDRI-YgeaEWLGrEFILIDTGGI 59
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 26-130 8.35e-05

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 40.18  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKGLAKTSSVPGktqtINFYRINdaFYLVDLPGfgyanvpKKVK------AGWE---AMI 96
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIG----VDFKTKT--VLENDDNG-------KKIKlniwdtAGQErfrSLH 68

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1084827076  97 ERYVSERptlCGAMVILDPRRDpgdveERVYSWL 130
Cdd:pfam08477  69 PFYYRGA---AAALLVYDSRTF-----SNLKYWL 94
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 26-79 1.07e-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: 1.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKGLaKTSSVPGK-------TQTINFYRINDAFYLVDLPGF 79
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLPELDL-RTGEISEKlgrgrhtTTHVELFPLPGGGLLIDTPGF 168
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 28-78 1.32e-04

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 40.52  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKglAKTSSVPGKT--QTINFYRIND-AFYLVDLPG 78
Cdd:cd01879     2 LVGNPNVGKTTLFNALTGAR--QKVGNWPGVTveKKEGEFKLGGkEIEIVDLPG 53
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
10-192 1.41e-04

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 41.63  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  10 ISASKSAVYPKDGLPeILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKT-----QTINfyrIND-AFYLVDlpgfgyan 83
Cdd:PRK05291  203 LASARQGEILREGLK-VVIAGRPNVGKSSLLNALLGEE-RAIVTDIAGTTrdvieEHIN---LDGiPLRLID-------- 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  84 vpkkvKAGW-------EAM-IERYVSErptLCGAMVIL---DPRRDPGDVEERVysWLLGECIPHATVFTKADKLSKNEL 152
Cdd:PRK05291  270 -----TAGIretddevEKIgIERSREA---IEEADLVLlvlDASEPLTEEDDEI--LEELKDKPVIVVLNKADLTGEIDL 339

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1084827076 153 SsrlaalkkLIPIEHPIIFSSVTGDGKPMLSRKIQEMLEG 192
Cdd:PRK05291  340 E--------EENGKPVIRISAKTGEGIDELREAIKELAFG 371
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 26-78 1.90e-04

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: 40.05  E-value: 1.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKGlAKTSSVPGKTQTINFYRI-----NDAFYLVDLPG 78
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKG-SITEYYPGTTRNYVTTVIeedgkTYKFNLLDTAG 60
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
23-79 2.33e-04

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 40.78  E-value: 2.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  23 LPEILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFY--RIND-AFYLVDLPGF 79
Cdd:COG1160     2 SPVVAIVGRPNVGKSTLFNRLTGRR-DAIVDDTPGVTRDRIYGeaEWGGrEFTLIDTGGI 60
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 28-59 2.60e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.80  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1084827076  28 LVGRSNVGKSSLINAFVNKKGLAkTSSVPGKT 59
Cdd:PRK00093  178 IIGRPNVGKSSLINALLGEERVI-VSDIAGTT 208
PRK00098 PRK00098
GTPase RsgA; Reviewed
 27-79 2.88e-04

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.57  E-value: 2.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  27 LLVGRSNVGKSSLINAFVNKKgLAKTSSVP-----GK--TQTINFYRINDAFYLVDLPGF 79
Cdd:PRK00098  168 VLAGQSGVGKSTLLNALAPDL-ELKTGEISealgrGKhtTTHVELYDLPGGGLLIDTPGF 226
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
 29-78 4.98e-04

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 39.10  E-value: 4.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1084827076  29 VGRSNVGKSSLINAFVNKKGLAkTSSVPGKTQTINFYRINDAFYLVDLPG 78
Cdd:cd04178   122 VGYPNVGKSSVINSLKRSRACN-VGATPGVTKSMQEVHLDKHVKLLDSPG 170
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
26-79 5.53e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 39.71  E-value: 5.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKGLaktssvpgKTQTIN--------------FYRINDAFYLVDLPGF 79
Cdd:COG1162   169 SVLVGQSGVGKSTLINALLPDADL--------ATGEISeklgrgrhttthaeLYPLPGGGWLIDTPGF 228
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
 26-47 5.78e-04

Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 38.80  E-value: 5.78e-04
                          10        20
                  ....*....|....*....|..
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKK 47
Cdd:cd01862     3 VIILGDSGVGKTSLMNQYVNKK 24
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 27-146 6.44e-04

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They 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. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 38.48  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827076  27 LLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKTQTINFYRIN---DAFYLVDLPGFGYANVPKKVkagWEAMIERYVser 103
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTE-VAAVGDRRPTTRAAQAYVWQtggDGLVLLDLPGVGERGRRDRE---YEELYRRLL--- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1084827076 104 PTLCGAMVILDPrRDPGD--VEERVYSWLLGECIPHATVFTKADK 146
Cdd:cd11383    74 PEADLVLWLLDA-DDRALaaDHDFYLLPLAGHDAPLLFVLNQVDP 117
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 20-59 6.53e-04

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: 39.39  E-value: 6.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1084827076  20 KDGLpEILLVGRSNVGKSSLINAFVNKKgLAKTSSVPGKT 59
Cdd:pfam12631  92 REGI-KVVIVGKPNVGKSSLLNALLGEE-RAIVTDIPGTT 129
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 15-41 1.49e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 38.62  E-value: 1.49e-03
                          10        20
                  ....*....|....*....|....*..
gi 1084827076  15 SAVYPKDGLPEILLVGRSNVGKSSLIN 41
Cdd:PRK09518  442 SGFLTPSGLRRVALVGRPNVGKSSLLN 468
obgE PRK12298
GTPase CgtA; Reviewed
 140-191 3.75e-03

GTPase CgtA; Reviewed


Pssm-ID: 237047 [Multi-domain]  Cd Length: 390  Bit Score: 37.15  E-value: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084827076 140 VFTKADKLSKNELSSRLAALKKLIPIEHPIIF-SSVTGDGKPMLSRKIQEMLE 191
Cdd:PRK12298  281 VFNKIDLLDEEEAEERAKAIVEALGWEGPVYLiSAASGLGVKELCWDLMTFIE 333
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
26-78 4.41e-03

Fe2+ transporter FeoB [Inorganic ion transport and metabolism];


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 37.02  E-value: 4.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKKglAKTSSVPGKT--QTINFYRINDA-FYLVDLPG 78
Cdd:COG0370     6 IALVGNPNVGKTTLFNALTGSR--QKVGNWPGVTveKKEGKFKLKGKeIELVDLPG 59
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 26-59 5.16e-03

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 35.95  E-value: 5.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1084827076   26 ILLVGRSNVGKSSLINAFVNKK---------G---LAKTSSVPGKT 59
Cdd:smart00175   3 IILIGDSGVGKSSLLSRFTDGKfseqykstiGvdfKTKTIEVDGKR 48
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 26-47 5.43e-03

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 35.89  E-value: 5.43e-03
                          10        20
                  ....*....|....*....|..
gi 1084827076  26 ILLVGRSNVGKSSLINAFVNKK 47
Cdd:cd00154     3 IVLIGDSGVGKTSLLLRFVDNK 24
 
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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