NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|486175400|ref|WP_001535563|]
View 

GTPase family protein [Escherichia coli]

Protein Classification

GTPase family protein( domain architecture ID 11466459)

GTPase family protein with a Ras-like GTPase domain, similar to Escherichia coli uncharacterized proteins YkfA, YeeP and YfjP

Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11152757

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YeeP COG3596
Predicted GTPase [General function prediction only];
1-272 4.52e-74

Predicted GTPase [General function prediction only];


:

Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 228.88  E-value: 4.52e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   1 MNPS-DAIEAIEKPLSSLPYSLSRHILEHLR--KLTSHEPVIGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRF 77
Cdd:COG3596    1 MSTEvSSLTERLEALKRLPQVLRELLAEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  78 RL-SGHGHSMVITDLPGVGESRDRDAEYEAlYRDILPELDLVLWLIKADDRALSVDEYFWRHILHRGHQ-QVLFVVTQAD 155
Cdd:COG3596   81 RLeSDGLPGLVLLDTPGLGEVNERDREYRE-LRELLPEADLILWVVKADDRALATDEEFLQALRAQYPDpPVLVVLTQVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 156 KTEPCHEWDMAGIQPSPAQAQNIREKTEAVFRLF----RPVHPVVAVSARTGWELDTLVSALMTALPDHAASPLMTRLqd 231
Cdd:COG3596  160 RLEPEREWDPPYNWPSPPKEQNIRRALEAIAEQLgvpiDRVIPVSAAEDRTGYGLEELVDALAEALPEAKRSRLARLL-- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 486175400 232 elrtesvRGQAREQFTGAVDRIFDTAESVCVASVARAVWNW 272
Cdd:COG3596  238 -------RAKAIDRYTLLAAAAALLAAALLALLALLLAALA 271
 
Name Accession Description Interval E-value
YeeP COG3596
Predicted GTPase [General function prediction only];
1-272 4.52e-74

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 228.88  E-value: 4.52e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   1 MNPS-DAIEAIEKPLSSLPYSLSRHILEHLR--KLTSHEPVIGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRF 77
Cdd:COG3596    1 MSTEvSSLTERLEALKRLPQVLRELLAEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  78 RL-SGHGHSMVITDLPGVGESRDRDAEYEAlYRDILPELDLVLWLIKADDRALSVDEYFWRHILHRGHQ-QVLFVVTQAD 155
Cdd:COG3596   81 RLeSDGLPGLVLLDTPGLGEVNERDREYRE-LRELLPEADLILWVVKADDRALATDEEFLQALRAQYPDpPVLVVLTQVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 156 KTEPCHEWDMAGIQPSPAQAQNIREKTEAVFRLF----RPVHPVVAVSARTGWELDTLVSALMTALPDHAASPLMTRLqd 231
Cdd:COG3596  160 RLEPEREWDPPYNWPSPPKEQNIRRALEAIAEQLgvpiDRVIPVSAAEDRTGYGLEELVDALAEALPEAKRSRLARLL-- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 486175400 232 elrtesvRGQAREQFTGAVDRIFDTAESVCVASVARAVWNW 272
Cdd:COG3596  238 -------RAKAIDRYTLLAAAAALLAAALLALLALLLAALA 271
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
40-217 6.32e-63

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: 194.48  E-value: 6.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  40 GIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRLSGHGHSMVITDLPGVGESRDRDAEYEALYRDILPELDLVL 119
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 120 WLIKADDRALSVDEYFWRHILHRGHQQVLFVVTQADktepchewdmagiqpspaqaqnirekteavfrlfrpvhPVVAVS 199
Cdd:cd11383   81 WLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD--------------------------------------PVLAVS 122
                        170
                 ....*....|....*...
gi 486175400 200 ARTGWELDTLVSALMTAL 217
Cdd:cd11383  123 ARTGWGLDELAEALITAL 140
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
39-152 2.52e-16

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: 73.04  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   39 IGIMGKSGAGKSSLCNTLFqGEVTPVSDVHAGTREVQRFRLSGHGHSMVITDLPGVGESRDRDAEYEALYRDILpELDLV 118
Cdd:pfam01926   2 VALVGRPNVGKSTLINALT-GAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAII-EADLI 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 486175400  119 LWLIKADDRALSVDEYFwRHILHRGHQQVLFVVT 152
Cdd:pfam01926  80 LFVVDSEEGITPLDEEL-LELLRENKKPIILVLN 112
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
36-156 5.56e-06

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: 45.44  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   36 EPVIGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREV--QRFRLSGHGHSMVITDLPGVGE-SRDRDAEYEALYRdIL 112
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYvtTVIEEDGKTYKFNLLDTAGQEDyDAIRRLYYPQVER-SL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 486175400  113 PELDLVLWLIKADDRALSVDEYFWRHIlhRGHQQVLFVVTQADK 156
Cdd:TIGR00231  80 RVFDIVILVLDVEEILEKQTKEIIHHA--DSGVPIILVGNKIDL 121
era PRK00089
GTPase Era; Reviewed
39-220 5.75e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 46.58  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  39 IGIMGKSGAGKSSLCNTLFQGEVTPVSDVhagtreVQ--RFRLSG---HGHS-MVITDLPGVGESRDR------DAEYEA 106
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPK------PQttRHRIRGivtEDDAqIIFVDTPGIHKPKRAlnramnKAAWSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 107 LyRDIlpelDLVLWLIKADDRALSVDEYFWRhILHRGHQQVLFVVTQADKTEPchewdmagiqpspaqAQNIREKTEAVF 186
Cdd:PRK00089  82 L-KDV----DLVLFVVDADEKIGPGDEFILE-KLKKVKTPVILVLNKIDLVKD---------------KEELLPLLEELS 140
                        170       180       190
                 ....*....|....*....|....*....|....
gi 486175400 187 RLFrPVHPVVAVSARTGWELDTLVSALMTALPDH 220
Cdd:PRK00089 141 ELM-DFAEIVPISALKGDNVDELLDVIAKYLPEG 173
 
Name Accession Description Interval E-value
YeeP COG3596
Predicted GTPase [General function prediction only];
1-272 4.52e-74

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 228.88  E-value: 4.52e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   1 MNPS-DAIEAIEKPLSSLPYSLSRHILEHLR--KLTSHEPVIGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRF 77
Cdd:COG3596    1 MSTEvSSLTERLEALKRLPQVLRELLAEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  78 RL-SGHGHSMVITDLPGVGESRDRDAEYEAlYRDILPELDLVLWLIKADDRALSVDEYFWRHILHRGHQ-QVLFVVTQAD 155
Cdd:COG3596   81 RLeSDGLPGLVLLDTPGLGEVNERDREYRE-LRELLPEADLILWVVKADDRALATDEEFLQALRAQYPDpPVLVVLTQVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 156 KTEPCHEWDMAGIQPSPAQAQNIREKTEAVFRLF----RPVHPVVAVSARTGWELDTLVSALMTALPDHAASPLMTRLqd 231
Cdd:COG3596  160 RLEPEREWDPPYNWPSPPKEQNIRRALEAIAEQLgvpiDRVIPVSAAEDRTGYGLEELVDALAEALPEAKRSRLARLL-- 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 486175400 232 elrtesvRGQAREQFTGAVDRIFDTAESVCVASVARAVWNW 272
Cdd:COG3596  238 -------RAKAIDRYTLLAAAAALLAAALLALLALLLAALA 271
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
40-217 6.32e-63

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: 194.48  E-value: 6.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  40 GIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRLSGHGHSMVITDLPGVGESRDRDAEYEALYRDILPELDLVL 119
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 120 WLIKADDRALSVDEYFWRHILHRGHQQVLFVVTQADktepchewdmagiqpspaqaqnirekteavfrlfrpvhPVVAVS 199
Cdd:cd11383   81 WLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD--------------------------------------PVLAVS 122
                        170
                 ....*....|....*...
gi 486175400 200 ARTGWELDTLVSALMTAL 217
Cdd:cd11383  123 ARTGWGLDELAEALITAL 140
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
40-215 6.66e-31

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: 112.94  E-value: 6.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  40 GIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRLS--GHGHSMVITDLPGVGESRDRDaeYEALYRDILPELDL 117
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKEldKGKVKLVLVDTPGLDEFGGLG--REELARLLLRGADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 118 VLWLIKADDRALSVDEYFWRHILHRGHQQ-VLFVVTQADKTEPCHEWdmagiqpspaqaqnirEKTEAVFRLFRPVHPVV 196
Cdd:cd00882   79 ILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDLLEEREVE----------------ELLRLEELAKILGVPVF 142
                        170
                 ....*....|....*....
gi 486175400 197 AVSARTGWELDTLVSALMT 215
Cdd:cd00882  143 EVSAKTGEGVDELFEKLIE 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
40-213 1.99e-19

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: 82.68  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  40 GIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRL-SGHGHSMVITDLPGVGESRDRDAEYEALYRDILPELDLV 118
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWeLLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 119 LWLIKADdraLSVDEYFWRHI-LHRGHQQVLFVVTQADKTepchewdmagiqPSPAQAQNIREKTeavfRLFRPVHPVVA 197
Cdd:cd00880   81 LLVVDSD---LTPVEEEAKLGlLRERGKPVLLVLNKIDLV------------PESEEEELLRERK----LELLPDLPVIA 141
                        170
                 ....*....|....*.
gi 486175400 198 VSARTGWELDTLVSAL 213
Cdd:cd00880  142 VSALPGEGIDELRKKI 157
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
39-152 2.52e-16

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: 73.04  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   39 IGIMGKSGAGKSSLCNTLFqGEVTPVSDVHAGTREVQRFRLSGHGHSMVITDLPGVGESRDRDAEYEALYRDILpELDLV 118
Cdd:pfam01926   2 VALVGRPNVGKSTLINALT-GAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAII-EADLI 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 486175400  119 LWLIKADDRALSVDEYFwRHILHRGHQQVLFVVT 152
Cdd:pfam01926  80 LFVVDSEEGITPLDEEL-LELLRENKKPIILVLN 112
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
47-201 2.49e-13

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: 66.42  E-value: 2.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  47 AGKSSLCNTLFQGEVTPVSDVHA-GTREVQRFRLSGHghsMVITDLPGVGESRDRDAEyeaLYRDILPELDLVLWLIKAd 125
Cdd:cd09912   11 AGKSTLLNALLGEEVLPTGVTPTtAVITVLRYGLLKG---VVLVDTPGLNSTIEHHTE---ITESFLPRADAVIFVLSA- 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 486175400 126 DRALS-VDEYFWRHILHRGHQQVLFVVTQADKTEPcHEWDMagiqpspAQAQNIREKTEAVFRLFRPvhPVVAVSAR 201
Cdd:cd09912   84 DQPLTeSEREFLKEILKWSGKKIFFVLNKIDLLSE-EELEE-------VLEYSREELGVLELGGGEP--RIFPVSAK 150
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
35-213 3.48e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.16  E-value: 3.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  35 HEPVIGIMGKSGAGKSSLCNTLFQGEVTPvsDVHAGTREVQ----RFRLSGHGHSMVITDLPGVGESRdrdaEYEALYRD 110
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSL--EKYLSTNGVTidkkELKLDGLDVDLVIWDTPGQDEFR----ETRQFYAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 111 ILPELDLVLWLIKADDRALSVDEYFWRHILHR--GHQQVLFVVTQADKTEpchEWDmagIQPSPAQAQNIREKteavfrl 188
Cdd:COG1100   76 QLTGASLYLFVVDGTREETLQSLYELLESLRRlgKKSPIILVLNKIDLYD---EEE---IEDEERLKEALSED------- 142
                        170       180
                 ....*....|....*....|....*
gi 486175400 189 frPVHPVVAVSARTGWELDTLVSAL 213
Cdd:COG1100  143 --NIVEVVATSAKTGEGVEELFAAL 165
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
39-213 1.07e-12

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: 64.45  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  39 IGIMGKSGAGKSSLCNTLF-QGEVTPVSDVHAGTREVQRFRLsghGHSMVITDLPGVGE---SRDRDAEYEALYRDIL-- 112
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQLINFFNV---GDKFRLVDLPGYGYakvSKEVREKWGKLIEEYLen 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 113 -PELDLVLWLIKADDRALSVDEYFWRHILHRGhQQVLFVVTQADKTepchewdmagiqpSPAQAQNIREKTEAVFRLFRP 191
Cdd:cd01876   79 rENLKGVVLLIDARHGPTPIDLEMLEFLEELG-IPFLIVLTKADKL-------------KKSELAKVLKKIKEELNLFNI 144
                        170       180
                 ....*....|....*....|..
gi 486175400 192 VHPVVAVSARTGWELDTLVSAL 213
Cdd:cd01876  145 LPPVILFSSKKGTGIDELRALI 166
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
41-213 8.05e-10

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: 56.35  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  41 IMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRLSGHGHSMVITDLPGVgesRDRDAEYEAL----YRDILPELD 116
Cdd:cd04164    8 IAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGL---RETEDEIEKIgierAREAIEEAD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 117 LVLWLIkadDRALSVDEYFWRHILHRGHQQVLFVVTQADKtepchewdmagiqpspaqaqnireKTEAVFRLFRPVHPVV 196
Cdd:cd04164   85 LVLLVV---DASEGLDEEDLEILELPAKKPVIVVLNKSDL------------------------LSDAEGISELNGKPII 137
                        170
                 ....*....|....*..
gi 486175400 197 AVSARTGWELDTLVSAL 213
Cdd:cd04164  138 AISAKTGEGIDELKEAL 154
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
41-228 1.15e-06

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: 49.29  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  41 IMGKSGAGKSSLCNTLFQGEVTPVSDVhAG-TREVQRFRLSGHGHSMVITDLPGVGESRD----------RDAEYEAlyr 109
Cdd:COG0486  218 IVGRPNVGKSSLLNALLGEERAIVTDI-AGtTRDVIEERINIGGIPVRLIDTAGLRETEDevekigieraREAIEEA--- 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 110 dilpelDLVLWLIKADDRALSVDEYFWRHILHRghqQVLFVVTQADKTepchewdmagiqpsPAQAQNIREkteavfrlf 189
Cdd:COG0486  294 ------DLVLLLLDASEPLTEEDEEILEKLKDK---PVIVVLNKIDLP--------------SEADGELKS--------- 341
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 486175400 190 RPVHPVVAVSARTGWELDTLVSAL---MTALPDHAASPLMTR 228
Cdd:COG0486  342 LPGEPVIAISAKTGEGIDELKEAIlelVGEGALEGEGVLLTN 383
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
36-156 5.56e-06

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: 45.44  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   36 EPVIGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREV--QRFRLSGHGHSMVITDLPGVGE-SRDRDAEYEALYRdIL 112
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYvtTVIEEDGKTYKFNLLDTAGQEDyDAIRRLYYPQVER-SL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 486175400  113 PELDLVLWLIKADDRALSVDEYFWRHIlhRGHQQVLFVVTQADK 156
Cdd:TIGR00231  80 RVFDIVILVLDVEEILEKQTKEIIHHA--DSGVPIILVGNKIDL 121
era PRK00089
GTPase Era; Reviewed
39-220 5.75e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 46.58  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  39 IGIMGKSGAGKSSLCNTLFQGEVTPVSDVhagtreVQ--RFRLSG---HGHS-MVITDLPGVGESRDR------DAEYEA 106
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQKISIVSPK------PQttRHRIRGivtEDDAqIIFVDTPGIHKPKRAlnramnKAAWSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 107 LyRDIlpelDLVLWLIKADDRALSVDEYFWRhILHRGHQQVLFVVTQADKTEPchewdmagiqpspaqAQNIREKTEAVF 186
Cdd:PRK00089  82 L-KDV----DLVLFVVDADEKIGPGDEFILE-KLKKVKTPVILVLNKIDLVKD---------------KEELLPLLEELS 140
                        170       180       190
                 ....*....|....*....|....*....|....
gi 486175400 187 RLFrPVHPVVAVSARTGWELDTLVSALMTALPDH 220
Cdd:PRK00089 141 ELM-DFAEIVPISALKGDNVDELLDVIAKYLPEG 173
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
39-216 6.36e-06

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: 45.50  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  39 IGIMGKSGAGKSSLCNTLFQGEVTPVSDVhAG-TREVQRFRLSGHGHSMVITDLPGVGE--SRDRDAEYEALYR--DILP 113
Cdd:cd01895    5 IAIIGRPNVGKSSLLNALLGEERVIVSDI-AGtTRDSIDVPFEYDGQKYTLIDTAGIRKkgKVTEGIEKYSVLRtlKAIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 114 ELDLVLWLIKADDRALSVDEYFWRHILHRGhQQVLFVVTQadktepcheWDmaGIQPSPAQAQNIREKTEAVFRLFRPVh 193
Cdd:cd01895   84 RADVVLLVLDASEGITEQDLRIAGLILEEG-KALIIVVNK---------WD--LVEKDEKTMKEFEKELRRKLPFLDYA- 150
                        170       180
                 ....*....|....*....|...
gi 486175400 194 PVVAVSARTGWELDTLVSALMTA 216
Cdd:cd01895  151 PIVFISALTGQGVDKLFDAIKEV 173
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
39-214 9.86e-06

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: 44.76  E-value: 9.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  39 IGIMGKSGAGKSSLCNTLFQGEVTPVSDVhagtreVQ--RFRLSG---HGHS-MVITDLPGVGESRDRDAEY---EAlyR 109
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQKISIVSPK------PQttRNRIRGiytDDDAqIIFVDTPGIHKPKKKLGERmvkAA--W 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 110 DILPELDLVLWLIKADDRALSVDEYFwRHILHRGHQQVLFVVTQADKTEPchewdmagiqpspaqaQNIREKTEAVFRLF 189
Cdd:cd04163   78 SALKDVDLVLFVVDASEWIGEGDEFI-LELLKKSKTPVILVLNKIDLVKD----------------KEDLLPLLEKLKEL 140
                        170       180
                 ....*....|....*....|....*
gi 486175400 190 RPVHPVVAVSARTGWELDTLVSALM 214
Cdd:cd04163  141 HPFAEIFPISALKGENVDELLEYIV 165
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
39-220 1.07e-05

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 45.75  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  39 IGIMGKSGAGKSSLCNTLFqGE-VTPVSDVhagtreVQ--RFRLSG---HGHS-MVITDLPGVGESRDR------DAEYE 105
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALV-GQkVSIVSPK------PQttRHRIRGivtREDAqIVFVDTPGIHKPKRKlgrrmnKAAWS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 106 ALYrdilpELDLVLWLIKADDRALSVDEYFWRHiLHRGHQQVLFVVTQADKTEPchewdmagiqpspaqaQNIREKTEAV 185
Cdd:COG1159   79 ALE-----DVDVILFVVDATEKIGEGDEFILEL-LKKLKTPVILVINKIDLVKK----------------EELLPLLAEY 136
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 486175400 186 FRLFrPVHPVVAVSARTGWELDTLVSALMTALPDH 220
Cdd:COG1159  137 SELL-DFAEIVPISALKGDNVDELLDEIAKLLPEG 170
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
41-213 1.23e-05

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: 45.93  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   41 IMGKSGAGKSSLCNTLFQGEVTPVSDVhAG-TREVQRFRLSGHGHSMVITDLPGVgesRDRDAEYEAL----YRDILPEL 115
Cdd:pfam12631  99 IVGKPNVGKSSLLNALLGEERAIVTDI-PGtTRDVIEETINIGGIPLRLIDTAGI---RETDDEVEKIgierAREAIEEA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  116 DLVLWLIkaDDRALSVDEYFWRHILHRGHQQVLFVVTQADKTepchewdmagiqpspaqaqnirekTEAVFRLFRPVHPV 195
Cdd:pfam12631 175 DLVLLVL--DASRPLDEEDLEILELLKDKKPIIVVLNKSDLL------------------------GEIDELEELKGKPV 228
                         170
                  ....*....|....*...
gi 486175400  196 VAVSARTGWELDTLVSAL 213
Cdd:pfam12631 229 LAISAKTGEGLDELEEAI 246
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
41-228 8.12e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 43.56  E-value: 8.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  41 IMGKSGAGKSSLCNTLFQGEVTPVSDVhAG-TREVQRFRLSGHGHSMVITDLPGVGESRDrdaEYEAL----YRDILPEL 115
Cdd:PRK05291 220 IAGRPNVGKSSLLNALLGEERAIVTDI-AGtTRDVIEEHINLDGIPLRLIDTAGIRETDD---EVEKIgierSREAIEEA 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 116 DLVLWLIKADDRALSVDEYFWRHILHRghqQVLFVVTQADKTEPCHEWDMAGiqpspaqaqnirekteavfrlfrpvHPV 195
Cdd:PRK05291 296 DLVLLVLDASEPLTEEDDEILEELKDK---PVIVVLNKADLTGEIDLEEENG-------------------------KPV 347
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 486175400 196 VAVSARTGWELDTLVSAL----MTALPDHAASPLMTR 228
Cdd:PRK05291 348 IRISAKTGEGIDELREAIkelaFGGFGGNQEGVFLTN 384
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
25-96 1.33e-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: 42.00  E-value: 1.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 486175400  25 ILEHLRKLTShepviGIMGKSGAGKSSLCNTLFQGE---VTPVSDVHA-G---TREVQRFRLSGHGhsMVItDLPGVGE 96
Cdd:cd01854   79 LRELLKGKTS-----VLVGQSGVGKSTLLNALLPELvlaTGEISEKLGrGrhtTTHRELFPLPGGG--LII-DTPGFRE 149
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
37-217 2.37e-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: 41.21  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400  37 PVIGIMGKSGAGKSSLCNTLFQ--------GevTPvsdvhaG-TREVQRFRLsghGHSMVITDLPGVG---ESRDRDAEY 104
Cdd:COG0218   24 PEIAFAGRSNVGKSSLINALTNrkklartsK--TP------GkTQLINFFLI---NDKFYLVDLPGYGyakVSKAEKEKW 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400 105 EALYRDIL---PELDLVLWLI------KADDRALsvdeYFWrhiLHRGHQQVLFVVTQADKtepchewdmagiqPSPAQA 175
Cdd:COG0218   93 QKLIEDYLegrENLKGVVLLIdirhppKELDLEM----LEW---LDEAGIPFLIVLTKADK-------------LKKSEL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 486175400 176 QNIREKTEAVFRLFRPVHPVVAVSARTGWELDTLVSALMTAL 217
Cdd:COG0218  153 AKQLKAIKKALGKDPAAPEVILFSSLKKEGIDELRAAIEEWL 194
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
2-96 5.67e-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: 39.83  E-value: 5.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400    2 NPSDAIEAIEKPLSSLPY------SLSRHILEHLRK-LTSHepVIGIMGKSGAGKSSLCNTLFQGEVTPVSDV------- 67
Cdd:pfam03193  67 DEEEELEELLKIYRAIGYpvlfvsAKTGEGIEALKElLKGK--TTVLAGQSGVGKSTLLNALLPELDLRTGEIseklgrg 144
                          90       100       110
                  ....*....|....*....|....*....|
gi 486175400   68 -HAgTREVQRFRLSGHGhsmVITDLPGVGE 96
Cdd:pfam03193 145 rHT-TTHVELFPLPGGG---LLIDTPGFRE 170
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
39-99 1.33e-03

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 39.22  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 486175400  39 IGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRLSGHGHSMVITDLPGVGESRD 99
Cdd:cd01853   34 ILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRPREVSRTVDGFKLNIIDTPGLLESQD 94
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
38-65 2.19e-03

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 37.63  E-value: 2.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 486175400   38 VIGIMGKSGAGKSSLCNtLFQGEVTPVS 65
Cdd:pfam00005  13 ILALVGPNGAGKSTLLK-LIAGLLSPTE 39
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
20-94 5.51e-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: 36.59  E-value: 5.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 486175400  20 SLSRHILEHLRKLTSHEPV-IGIMGKSGAGKSSLCNTLFQGEVTPVSDVHAGTREVQRFRLSghgHSMVITDLPGV 94
Cdd:cd01849   74 KLKAEITKQKLKLKYKKGIrVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLD---KEIYLYDTPGI 146
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
29-93 7.62e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.30  E-value: 7.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486175400  29 LRKLTSHEPVIGimGKSGAGKSSLCNTLFQGEVTPVSDV----HAG---TREVQRFRLSGHGhsmVITDLPG 93
Cdd:PRK12289 167 LEQLRNKITVVA--GPSGVGKSSLINRLIPDVELRVGKVsgklGRGrhtTRHVELFELPNGG---LLADTPG 233
AAA_22 pfam13401
AAA domain;
32-150 8.52e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.78  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486175400   32 LTSHEPVIGIMGKSGAGKSSLCNTLFQgevtpvsdvhagtrevqrfRLSGHGHSMVITDLPGVGESRDrdaeyeaLYRDI 111
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLE-------------------QLPEVRDSVVFVDLPSGTSPKD-------LLRAL 54
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 486175400  112 LPELDLVLwliKADDRALSVDEYFWRHILHRGHQQVLFV 150
Cdd:pfam13401  55 LRALGLPL---SGRLSKEELLAALQQLLLALAVAVVLII 90
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH