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Conserved domains on  [gi|2594345208|ref|WP_316928267|]
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GTPase [Providencia sp. PROV175]

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

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List of domain hits

Name Accession Description Interval E-value
YeeP COG3596
Predicted GTPase [General function prediction only];
10-243 1.14e-71

Predicted GTPase [General function prediction only];


:

Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 223.49  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  10 FLPKGAKDVFLSHLNK-LINYSPT-IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNM-TINNHTLTFIDLP 86
Cdd:COG3596    17 RLPQVLRELLAEALERlLVELPPPvIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLeSDGLPGLVLLDTP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  87 GVGESLERDKEYHQlYRNLLPELDLIIWVLKADDRAWSSDEQCYRFLTEQcgYQSERFLFVLNQADKIEPCRQWDEHNHQ 166
Cdd:COG3596    97 GLGEVNERDREYRE-LRELLPEADLILWVVKADDRALATDEEFLQALRAQ--YPDPPVLVVLTQVDRLEPEREWDPPYNW 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 167 PSLEQVANLELKQQAVITAFK-PHHPVMTVSAAE---GFQLTELAEQLIQALPAQASSGVARQLNST----YRTQSVENS 238
Cdd:COG3596   174 PSPPKEQNIRRALEAIAEQLGvPIDRVIPVSAAEdrtGYGLEELVDALAEALPEAKRSRLARLLRAKaidrYTLLAAAAA 253

                  ....*
gi 2594345208 239 ARNDF 243
Cdd:COG3596   254 LLAAA 258
 
Name Accession Description Interval E-value
YeeP COG3596
Predicted GTPase [General function prediction only];
10-243 1.14e-71

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 223.49  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  10 FLPKGAKDVFLSHLNK-LINYSPT-IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNM-TINNHTLTFIDLP 86
Cdd:COG3596    17 RLPQVLRELLAEALERlLVELPPPvIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLeSDGLPGLVLLDTP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  87 GVGESLERDKEYHQlYRNLLPELDLIIWVLKADDRAWSSDEQCYRFLTEQcgYQSERFLFVLNQADKIEPCRQWDEHNHQ 166
Cdd:COG3596    97 GLGEVNERDREYRE-LRELLPEADLILWVVKADDRALATDEEFLQALRAQ--YPDPPVLVVLTQVDRLEPEREWDPPYNW 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 167 PSLEQVANLELKQQAVITAFK-PHHPVMTVSAAE---GFQLTELAEQLIQALPAQASSGVARQLNST----YRTQSVENS 238
Cdd:COG3596   174 PSPPKEQNIRRALEAIAEQLGvPIDRVIPVSAAEdrtGYGLEELVDALAEALPEAKRSRLARLLRAKaidrYTLLAAAAA 253

                  ....*
gi 2594345208 239 ARNDF 243
Cdd:COG3596   254 LLAAA 258
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
34-214 4.60e-50

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: 161.74  E-value: 4.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  34 GLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGESLERDKEYHQLYRNLLPELDLII 113
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 114 WVLKADDRAWSSDEQCYrfLTEQCGYqSERFLFVLNQADkiepcrqwdehnhqpsleqvanlelkqqavitafkphhPVM 193
Cdd:cd11383    81 WLLDADDRALAADHDFY--LLPLAGH-DAPLLFVLNQVD--------------------------------------PVL 119
                         170       180
                  ....*....|....*....|.
gi 2594345208 194 TVSAAEGFQLTELAEQLIQAL 214
Cdd:cd11383   120 AVSARTGWGLDELAEALITAL 140
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-149 2.31e-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: 86.52  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQsALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVgesLERDKEYHQLYRNLLP--EL 109
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL---IEGASEGEGLGRAFLAiiEA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2594345208 110 DLIIWVLKADDRAWSSDEQCYRFLTEqcgyQSERFLFVLN 149
Cdd:pfam01926  77 DLILFVVDSEEGITPLDEELLELLRE----NKKPIILVLN 112
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
31-197 1.91e-10

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: 58.64  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  31 PTIGLMGKTGAGKSSLINALF-QSALSPVSNVSGCTRQAQLFNMtinNHTLTFIDLPGVG---ESLERDKEYHQLYRNLL 106
Cdd:TIGR03598  19 PEIAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQLINFFEV---NDGFRLVDLPGYGyakVSKEEKEKWQKLIEEYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 107 ---PELDLIIWV------LKADDRawssdeQCYRFLtEQCGYQserFLFVLNQADKIepcrqwdehnhqpSLEQVANLEL 177
Cdd:TIGR03598  96 ekrENLKGVVLLmdirhpLKELDL------EMIEWL-RERGIP---VLIVLTKADKL-------------KKSELNKQLK 152
                         170       180
                  ....*....|....*....|
gi 2594345208 178 KQQAVITAFKPHHPVMTVSA 197
Cdd:TIGR03598 153 KIKKALKKDADDPSVQLFSS 172
era PRK00089
GTPase Era; Reviewed
33-215 3.04e-09

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 56.59  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVgeslerDKEYHQLYRNL------- 105
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGI------HKPKRALNRAMnkaawss 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 106 LPELDLIIWVLKAdDRAWSSDEqcyRFLTEQCGYQSERFLFVLNQADKIEPcrqwdehnhqpsLEQVanleLKQQAVITA 185
Cdd:PRK00089   82 LKDVDLVLFVVDA-DEKIGPGD---EFILEKLKKVKTPVILVLNKIDLVKD------------KEEL----LPLLEELSE 141
                         170       180       190
                  ....*....|....*....|....*....|
gi 2594345208 186 FKPHHPVMTVSAAEGFQLTELAEQLIQALP 215
Cdd:PRK00089  142 LMDFAEIVPISALKGDNVDELLDVIAKYLP 171
 
Name Accession Description Interval E-value
YeeP COG3596
Predicted GTPase [General function prediction only];
10-243 1.14e-71

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 223.49  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  10 FLPKGAKDVFLSHLNK-LINYSPT-IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNM-TINNHTLTFIDLP 86
Cdd:COG3596    17 RLPQVLRELLAEALERlLVELPPPvIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLeSDGLPGLVLLDTP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  87 GVGESLERDKEYHQlYRNLLPELDLIIWVLKADDRAWSSDEQCYRFLTEQcgYQSERFLFVLNQADKIEPCRQWDEHNHQ 166
Cdd:COG3596    97 GLGEVNERDREYRE-LRELLPEADLILWVVKADDRALATDEEFLQALRAQ--YPDPPVLVVLTQVDRLEPEREWDPPYNW 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 167 PSLEQVANLELKQQAVITAFK-PHHPVMTVSAAE---GFQLTELAEQLIQALPAQASSGVARQLNST----YRTQSVENS 238
Cdd:COG3596   174 PSPPKEQNIRRALEAIAEQLGvPIDRVIPVSAAEdrtGYGLEELVDALAEALPEAKRSRLARLLRAKaidrYTLLAAAAA 253

                  ....*
gi 2594345208 239 ARNDF 243
Cdd:COG3596   254 LLAAA 258
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
34-214 4.60e-50

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: 161.74  E-value: 4.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  34 GLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGESLERDKEYHQLYRNLLPELDLII 113
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 114 WVLKADDRAWSSDEQCYrfLTEQCGYqSERFLFVLNQADkiepcrqwdehnhqpsleqvanlelkqqavitafkphhPVM 193
Cdd:cd11383    81 WLLDADDRALAADHDFY--LLPLAGH-DAPLLFVLNQVD--------------------------------------PVL 119
                         170       180
                  ....*....|....*....|.
gi 2594345208 194 TVSAAEGFQLTELAEQLIQAL 214
Cdd:cd11383   120 AVSARTGWGLDELAEALITAL 140
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
34-212 1.27e-29

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: 109.85  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  34 GLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTI--NNHTLTFIDLPGVGESLERDKEyhQLYRNLLPELDL 111
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELdkGKVKLVLVDTPGLDEFGGLGRE--ELARLLLRGADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 112 IIWVLKADDRAwsSDEQCYRFLTEQCGYQSERFLFVLNQADKIEPCRQWDEHNhqpsleqvanlelkqqAVITAFKPHHP 191
Cdd:cd00882    79 ILLVVDSTDRE--SEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLR----------------LEELAKILGVP 140
                         170       180
                  ....*....|....*....|.
gi 2594345208 192 VMTVSAAEGFQLTELAEQLIQ 212
Cdd:cd00882   141 VFEVSAKTGEGVDELFEKLIE 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
34-214 1.11e-23

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: 94.23  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  34 GLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTIN-NHTLTFIDLPGVGESLERDKEYHQLYRNLLPELDLI 112
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLpLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 113 IWVLKADDRAwSSDEQCYRFLteqcgYQSE-RFLFVLNQADKIEPcrqwDEHNhqpsleqvanlELKQQAVITAFKPHHP 191
Cdd:cd00880    81 LLVVDSDLTP-VEEEAKLGLL-----RERGkPVLLVLNKIDLVPE----SEEE-----------ELLRERKLELLPDLPV 139
                         170       180
                  ....*....|....*....|...
gi 2594345208 192 VMtVSAAEGFQLTELAEQLIQAL 214
Cdd:cd00880   140 IA-VSALPGEGIDELRKKIAELL 161
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-149 2.31e-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: 86.52  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQsALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVgesLERDKEYHQLYRNLLP--EL 109
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGL---IEGASEGEGLGRAFLAiiEA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2594345208 110 DLIIWVLKADDRAWSSDEQCYRFLTEqcgyQSERFLFVLN 149
Cdd:pfam01926  77 DLILFVVDSEEGITPLDEELLELLRE----NKKPIILVLN 112
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
33-214 1.23e-18

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: 81.02  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALF-QSALSPVSNVSGCTRQAQLFNMtinNHTLTFIDLPGVGE---SLERDKEYHQLYRNLL-- 106
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQLINFFNV---GDKFRLVDLPGYGYakvSKEVREKWGKLIEEYLen 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 107 -PELDLIIWVLKADDRAWSSDEQCYRFLtEQCGYQserFLFVLNQADKIepcrqwdehnhqpSLEQVANLELKQQAVITA 185
Cdd:cd01876    79 rENLKGVVLLIDARHGPTPIDLEMLEFL-EELGIP---FLIVLTKADKL-------------KKSELAKVLKKIKEELNL 141
                         170       180
                  ....*....|....*....|....*....
gi 2594345208 186 FKPHHPVMTVSAAEGFQLTELAEQLIQAL 214
Cdd:cd01876   142 FNILPPVILFSSKKGTGIDELRALIAEWL 170
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
32-202 1.93e-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: 67.19  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQSALSPVSNVSgCTrqaqlFNMTINNHTL----TFIDLPGVGESLERDKEyhqLYRNLLP 107
Cdd:cd09912     2 LLAVVGEFSAGKSTLLNALLGEEVLPTGVTP-TT-----AVITVLRYGLlkgvVLVDTPGLNSTIEHHTE---ITESFLP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 108 ELDLIIWVLKAdDRAWSSDEQcyRFLTEQCGYQSERFLFVLNQADKIEPcrqwDEhnhqpsLEQVANLELKQQAVITAFK 187
Cdd:cd09912    73 RADAVIFVLSA-DQPLTESER--EFLKEILKWSGKKIFFVLNKIDLLSE----EE------LEEVLEYSREELGVLELGG 139
                         170
                  ....*....|....*
gi 2594345208 188 PHHPVMTVSAAEGFQ 202
Cdd:cd09912   140 GEPRIFPVSAKEALE 154
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
33-214 3.23e-11

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: 60.55  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGESLERDKEYH-QLYRNLLPELDL 111
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQKISIVSPKPQTTRNRIRGIYTDDDAQIIFVDTPGIHKPKKKLGERMvKAAWSALKDVDL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 112 IIWVLKADDRaWSSDEqcyRFLTEQCGYQSERFLFVLNQADKIepcrqwdeHNHQPSLEQVANLELKQQavitaFKphhP 191
Cdd:cd04163    86 VLFVVDASEW-IGEGD---EFILELLKKSKTPVILVLNKIDLV--------KDKEDLLPLLEKLKELHP-----FA---E 145
                         170       180
                  ....*....|....*....|...
gi 2594345208 192 VMTVSAAEGFQLTELAEQLIQAL 214
Cdd:cd04163   146 IFPISALKGENVDELLEYIVEYL 168
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
31-197 1.91e-10

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: 58.64  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  31 PTIGLMGKTGAGKSSLINALF-QSALSPVSNVSGCTRQAQLFNMtinNHTLTFIDLPGVG---ESLERDKEYHQLYRNLL 106
Cdd:TIGR03598  19 PEIAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQLINFFEV---NDGFRLVDLPGYGyakVSKEEKEKWQKLIEEYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 107 ---PELDLIIWV------LKADDRawssdeQCYRFLtEQCGYQserFLFVLNQADKIepcrqwdehnhqpSLEQVANLEL 177
Cdd:TIGR03598  96 ekrENLKGVVLLmdirhpLKELDL------EMIEWL-RERGIP---VLIVLTKADKL-------------KKSELNKQLK 152
                         170       180
                  ....*....|....*....|
gi 2594345208 178 KQQAVITAFKPHHPVMTVSA 197
Cdd:TIGR03598 153 KIKKALKKDADDPSVQLFSS 172
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
33-215 1.40e-09

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 57.69  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVgeslerDKEYHQLYRNL------- 105
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVGQKVSIVSPKPQTTRHRIRGIVTREDAQIVFVDTPGI------HKPKRKLGRRMnkaawsa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 106 LPELDLIIWVLKAdDRAWSSDEqcyRFLTEQCGYQSERFLFVLNQADKIEPcrqwdehnhqpslEQVanleLKQQAVITA 185
Cdd:COG1159    80 LEDVDVILFVVDA-TEKIGEGD---EFILELLKKLKTPVILVINKIDLVKK-------------EEL----LPLLAEYSE 138
                         170       180       190
                  ....*....|....*....|....*....|
gi 2594345208 186 FKPHHPVMTVSAAEGFQLTELAEQLIQALP 215
Cdd:COG1159   139 LLDFAEIVPISALKGDNVDELLDEIAKLLP 168
era PRK00089
GTPase Era; Reviewed
33-215 3.04e-09

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 56.59  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVgeslerDKEYHQLYRNL------- 105
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKISIVSPKPQTTRHRIRGIVTEDDAQIIFVDTPGI------HKPKRALNRAMnkaawss 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 106 LPELDLIIWVLKAdDRAWSSDEqcyRFLTEQCGYQSERFLFVLNQADKIEPcrqwdehnhqpsLEQVanleLKQQAVITA 185
Cdd:PRK00089   82 LKDVDLVLFVVDA-DEKIGPGD---EFILEKLKKVKTPVILVLNKIDLVKD------------KEEL----LPLLEELSE 141
                         170       180       190
                  ....*....|....*....|....*....|
gi 2594345208 186 FKPHHPVMTVSAAEGFQLTELAEQLIQALP 215
Cdd:PRK00089  142 LMDFAEIVPISALKGDNVDELLDVIAKYLP 171
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
37-214 3.37e-09

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: 54.81  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  37 GKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGES--------LERDKEyhqlyrnLLPE 108
Cdd:cd04164    10 GKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGLRETedeiekigIERARE-------AIEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 109 LDLIIWVLKAdDRAWSSDEQcyRFLTEQCGyqsERFLFVLNQADkiepcrqwdehnhqpsleqvanleLKQQAVITAFKP 188
Cdd:cd04164    83 ADLVLLVVDA-SEGLDEEDL--EILELPAK---KPVIVVLNKSD------------------------LLSDAEGISELN 132
                         170       180
                  ....*....|....*....|....*.
gi 2594345208 189 HHPVMTVSAAEGFQLTELAEQLIQAL 214
Cdd:cd04164   133 GKPIIAISAKTGEGIDELKEALLELA 158
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
35-228 2.88e-08

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: 54.02  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  35 LMGKTGAGKSSLINALFQSALSPVSNVSGCTR---QAQLfnmTINNHTLTFIDLPGVGESL--------ERDKEyhqlyr 103
Cdd:pfam12631  99 IVGKPNVGKSSLLNALLGEERAIVTDIPGTTRdviEETI---NIGGIPLRLIDTAGIRETDdevekigiERARE------ 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 104 nLLPELDLIIWVLKADDRAWSSDEQCYRFLteqcgYQSERFLFVLNQADkiepcrqwdehnhqpsleqvanleLKQQAVI 183
Cdd:pfam12631 170 -AIEEADLVLLVLDASRPLDEEDLEILELL-----KDKKPIIVVLNKSD------------------------LLGEIDE 219
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2594345208 184 TAFKPHHPVMTVSAAEGFQLTELAEQLIQALPAQASSGV------ARQLNS 228
Cdd:pfam12631 220 LEELKGKPVLAISAKTGEGLDELEEAIKELFLAGEIASDgpiitnARHKEA 270
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
35-221 2.91e-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: 54.30  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  35 LMGKTGAGKSSLINALFQSALSPVSNVSGCTR---QAQLfnmTINNHTLTFIDLPGVGESL--------ERDKEyhqlyr 103
Cdd:COG0486   218 IVGRPNVGKSSLLNALLGEERAIVTDIAGTTRdviEERI---NIGGIPVRLIDTAGLRETEdevekigiERARE------ 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 104 nLLPELDLIIWVLKADDRAWSSDEQCYRFLteqcgyQSERFLFVLNQADkiepcrqwdehnhqpsLEQVANLELKQQavi 183
Cdd:COG0486   289 -AIEEADLVLLLLDASEPLTEEDEEILEKL------KDKPVIVVLNKID----------------LPSEADGELKSL--- 342
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2594345208 184 tafkPHHPVMTVSAAEGFQLTELAEQLIQALPAQASSG 221
Cdd:COG0486   343 ----PGEPVIAISAKTGEGIDELKEAILELVGEGALEG 376
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-214 1.11e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 50.75  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  28 NYSPTIGLMGKTGAGKSSLINALFQSALSPVSNVS--GCTRQAQLFNMTINNHTLTFIDLPGvgesLERDKEYHQLYRNL 105
Cdd:COG1100     1 MGEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStnGVTIDKKELKLDGLDVDLVIWDTPG----QDEFRETRQFYARQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 106 LPELDLIIWVLKAD-DRAWSSDEQCYRFLTEQcgYQSERFLFVLNQADKIEPCRQWDEHNHQPSLEQvanlelkqqavit 184
Cdd:COG1100    77 LTGASLYLFVVDGTrEETLQSLYELLESLRRL--GKKSPIILVLNKIDLYDEEEIEDEERLKEALSE------------- 141
                         170       180       190
                  ....*....|....*....|....*....|
gi 2594345208 185 afKPHHPVMTVSAAEGFQLTELAEQLIQAL 214
Cdd:COG1100   142 --DNIVEVVATSAKTGEGVEELFAALAEIL 169
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
41-89 4.41e-07

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: 49.30  E-value: 4.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2594345208  41 AGKSSLINALF-QSALSPVSNVSGCTRQAQLFNMtinNHTLTFIDLPGVG 89
Cdd:COG0218    34 VGKSSLINALTnRKKLARTSKTPGKTQLINFFLI---NDKFYLVDLPGYG 80
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
33-154 2.23e-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: 46.60  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHT--LTFIDLPGVGESLERDKEYHQLYRNLLPELD 110
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTykFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2594345208 111 LIIWVLKADDRAWSSDEQCYRFLTEQCGyqserFLFVLNQADKI 154
Cdd:TIGR00231  84 IVILVLDVEEILEKQTKEIIHHADSGVP-----IILVGNKIDLK 122
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
35-221 2.42e-06

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 48.18  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  35 LMGKTGAGKSSLINALFQSALSPVSNVSGCTR---QAQLfnmTINNHTLTFIDLPGVGESL--------ERDKEyhqlyr 103
Cdd:PRK05291  220 IAGRPNVGKSSLLNALLGEERAIVTDIAGTTRdviEEHI---NLDGIPLRLIDTAGIRETDdevekigiERSRE------ 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 104 nLLPELDLIIWVLKAdDRAWSSDEQCYRFLTEQcgyqsERFLFVLNQADKIEPcrqwDEHNHQPSLEQVAnlelkqqavi 183
Cdd:PRK05291  291 -AIEEADLVLLVLDA-SEPLTEEDDEILEELKD-----KPVIVVLNKADLTGE----IDLEEENGKPVIR---------- 349
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2594345208 184 tafkphhpvmtVSAAEGFQLTELAEQLIQALPAQASSG 221
Cdd:PRK05291  350 -----------ISAKTGEGIDELREAIKELAFGGFGGN 376
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
19-91 3.34e-06

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: 47.31  E-value: 3.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594345208  19 FLSHLNKLINYSPTIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGES 91
Cdd:cd01853    20 LEAKLKKELDFSLTILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRPREVSRTVDGFKLNIIDTPGLLES 92
Dynamin_N pfam00350
Dynamin family;
33-151 3.69e-06

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 46.07  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVsGCTR------------------------------QAQLFNMTINNHT--- 79
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRrptvlrlgespgasegavkveykdgekkfeDFSELREEIEKETeki 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  80 -----------------------LTFIDLPGVGESLERDKEyhqLYRNLLPELDLIIWVLKAdDRAWSSDEQcyRFLTEQ 136
Cdd:pfam00350  80 agtgkgissepivleilsplvpgLTLVDTPGLDSVAVGDQE---LTKEYIKPADIILAVTPA-NVDLSTSEA--LFLARE 153
                         170
                  ....*....|....*
gi 2594345208 137 CGYQSERFLFVLNQA 151
Cdd:pfam00350 154 VDPNGKRTIGVLTKA 168
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
33-94 4.33e-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: 45.89  E-value: 4.33e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPG------VGESLER 94
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgkVTEGIEK 72
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
24-88 9.50e-06

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: 44.87  E-value: 9.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2594345208  24 NKLINYSPTIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTinnHTLTFIDLPGV 88
Cdd:cd04178   110 NKGIKTSITVGVVGYPNVGKSSVINSLKRSRACNVGATPGVTKSMQEVHLD---KHVKLLDSPGV 171
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
32-90 3.20e-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: 43.93  E-value: 3.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQSALSPVSNVS-----GC--TRQAQLFNmtINNHTLtFIDLPGVGE 90
Cdd:cd01854    87 TSVLVGQSGVGKSTLLNALLPELVLATGEISeklgrGRhtTTHRELFP--LPGGGL-IIDTPGFRE 149
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
19-88 3.29e-05

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: 43.79  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  19 FLSHLNKLINYSPTIGLMGKTGAGKSSLINALFQS-----------ALSPVSNVSGCTRQAQLFNMtINNHTLtfIDLPG 87
Cdd:cd01855   114 LIEEIKKLAKYRGDVYVVGATNVGKSTLINALLKSnggkvqaqalvQRLTVSPIPGTTLGLIKIPL-GEGKKL--YDTPG 190

                  .
gi 2594345208  88 V 88
Cdd:cd01855   191 I 191
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
32-87 6.97e-05

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 42.98  E-value: 6.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594345208  32 TIGLMGKTGAGKSSLINAL-----FQSALSPvsnvSGCTRQAQLFNMTINNHTLTFIDLPG 87
Cdd:pfam04548   2 RIVLVGKTGNGKSATGNSIlgrkaFESKLRA----QGVTKTCQLVSRTWDGRIINVIDTPG 58
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
18-87 1.51e-04

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: 41.06  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594345208  18 VFLSHLNklinySPTIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQlfnmTIN-NHTLTFIDLPG 87
Cdd:cd01857    75 LFFSALN-----EATIGLVGYPNVGKSSLINALVGSKKVSVSSTPGKTKHFQ----TIFlEPGITLCDCPG 136
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
33-94 1.58e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 42.73  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPG------VGESLER 94
Cdd:PRK00093  176 IAIIGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkVTEGVEK 243
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
32-88 1.75e-04

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: 40.83  E-value: 1.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINnhtLTFIDLPGV 88
Cdd:cd01849    93 RVGVVGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDKE---IYLYDTPGI 146
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
32-88 1.93e-04

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: 41.15  E-value: 1.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  32 TIGLMGKTGAGKSSLINALF--QSAL-SPVSNVSGCTRQAQLFNMTINnhtLTFIDLPGV 88
Cdd:cd01859   101 IVGVVGYPKVGKSSIINALKgrHSAStSPIPGSPGYTKGIQLVRIDSK---IYLIDTPGV 157
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
42-88 3.76e-04

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 40.20  E-value: 3.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2594345208  42 GKSSLINALFQSALSPVSNVSGCTRQAQLFnmTINNHtLTFIDLPGV 88
Cdd:cd01856   127 GKSTLINRLRGKKVAKVGNKPGVTRGQQWI--RIGPN-IELLDTPGI 170
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
31-214 3.78e-04

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 40.52  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  31 PTIGLMGKTGAGKSSLINALFQSA----------LSPVsnvsgcTRQAQLF-NMTInnhTLT----FI-DLPgvgesler 94
Cdd:cd01878    42 PTVALVGYTNAGKSTLFNALTGADvlaedqlfatLDPT------TRRIKLPgGREV---LLTdtvgFIrDLP-------- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  95 dkeyHQL---YRNLLPEL---DLIIWVLKADDRAWssDEQ---CYRFLtEQCGYQSERFLFVLNQADKIEPCRQWDEHNH 165
Cdd:cd01878   105 ----HQLveaFRSTLEEVaeaDLLLHVVDASDPDR--EEQietVEEVL-KELGADDIPIILVLNKIDLLDDEELEERLRA 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2594345208 166 qpsleqvanlelkqqavitafkPHHPVMTVSAAEGFQLTELAEQLIQAL 214
Cdd:cd01878   178 ----------------------GRPDAVFISAKTGEGLDLLKEAIEELL 204
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
29-91 3.99e-04

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 41.86  E-value: 3.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594345208  29 YSPTIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGES 91
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFGEVKFSTDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLKSS 179
PLN03130 PLN03130
ABC transporter C family member; Provisional
20-52 4.02e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 42.03  E-value: 4.02e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2594345208   20 LSHLNKLINYSPTIGLMGKTGAGKSSLINALFQ 52
Cdd:PLN03130  1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFR 1287
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
20-51 5.33e-04

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 40.55  E-value: 5.33e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2594345208  20 LSHLNKLINYSPTIGLMGKTGAGKSSLINALF 51
Cdd:cd03244    20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALF 51
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
35-90 5.72e-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: 5.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594345208  35 LMGKTGAGKSSLINALFQSALSPVSNVSG-------CTRQAQLFNMtinNHTLTFIDLPGVGE 90
Cdd:pfam03193 111 LAGQSGVGKSTLLNALLPELDLRTGEISEklgrgrhTTTHVELFPL---PGGGLLIDTPGFRE 170
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
32-88 6.60e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 40.48  E-value: 6.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQSAL---SPVSNVSG----CTRQAQLFNmtINNHTLtFIDLPGV 88
Cdd:COG1162   168 TSVLVGQSGVGKSTLINALLPDADlatGEISEKLGrgrhTTTHAELYP--LPGGGW-LIDTPGF 228
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
34-214 8.15e-04

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 39.30  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  34 GLMGKTGAGKSSLINALfQSALSPVSNVSGCTRQAQ--LFNMtINNHTLTFIDLPGVGESLERDK-EYHQLYRNlLPELD 110
Cdd:cd01881     1 GLVGLPNVGKSTLLSAL-TSAKVEIASYPFTTLEPNvgVFEF-GDGVDIQIIDLPGLLDGASEGRgLGEQILAH-LYRSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208 111 LIIWVLKADDRAWSSDEQCYRFLTEQCGYQSER-----FLFVLNQADKiepcrqwdehnhqPSLEQVANLELKqqavitA 185
Cdd:cd01881    78 LILHVIDASEDCVGDPLEDQKTLNEEVSGSFLFlknkpEMIVANKIDM-------------ASENNLKRLKLD------K 138
                         170       180
                  ....*....|....*....|....*....
gi 2594345208 186 FKPHHPVMTVSAAEGFQLTELAEQLIQAL 214
Cdd:cd01881   139 LKRGIPVVPTSALTRLGLDRVIRTIRKLL 167
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
32-87 1.36e-03

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 39.06  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594345208  32 TIGLMGKTGAGKSSLINAL-----FQSALSPvsnvSGCTRQAQLFNMTINNHTLTFIDLPG 87
Cdd:cd01852     2 RLVLVGKTGNGKSATGNTIlgrkvFESKLSA----SGVTKTCQKESAVWDGRRVNVIDTPG 58
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
31-88 1.51e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 39.78  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2594345208  31 PTIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGV 88
Cdd:PRK09518  451 RRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGI 508
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
32-87 1.84e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 39.70  E-value: 1.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2594345208  32 TIGLMGKTGAGKSSLINALfQSALSPVSNVSGCT--RQAQLFNMTinNHTLTFIDLPG 87
Cdd:PRK09554    5 TIGLIGNPNSGKTTLFNQL-TGARQRVGNWAGVTveRKEGQFSTT--DHQVTLVDLPG 59
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
17-52 2.00e-03

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 39.54  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2594345208   17 DVFLSHLNKLINYSPTIGLMGKTGAGKSSLINALFQ 52
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFR 1334
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
33-94 2.40e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 39.24  E-value: 2.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2594345208  33 IGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPG------VGESLER 94
Cdd:COG1160   178 IAIVGRPNVGKSSLINALLGEERVIVSDIAGTTRDSIDTPFERDGKKYTLIDTAGirrkgkVDEGIEK 245
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
32-92 3.01e-03

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 38.43  E-value: 3.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQSALSPVSNVSGCT-RQAQlfNMTINNHT-----------LTFIDLPGVGESL 92
Cdd:pfam00735   5 TLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSeKIKK--TVEIKAYTveieedgvklnLTVIDTPGFGDAI 75
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
27-50 3.67e-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: 37.24  E-value: 3.67e-03
                          10        20
                  ....*....|....*....|....
gi 2594345208  27 INYSPTIGLMGKTGAGKSSLINAL 50
Cdd:pfam00005   8 LNPGEILALVGPNGAGKSTLLKLI 31
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
32-92 4.19e-03

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 37.91  E-value: 4.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2594345208  32 TIGLMGKTGAGKSSLINALFQSAL--SPVSNVSGCTR------QAQLFNMTINNHT--LTFIDLPGVGESL 92
Cdd:cd01850     6 NIMVVGESGLGKSTFINTLFGTKLypSKYPPAPGEHItktveiKISKAELEENGVKlkLTVIDTPGFGDNI 76
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
32-75 5.45e-03

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 38.02  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2594345208  32 TIGLMGKTGAGKSSLINaLFQSALSPVS--------NVSGCTRQ------------AQLFNMTI 75
Cdd:PRK13657  363 TVAIVGPTGAGKSTLIN-LLQRVFDPQSgrilidgtDIRTVTRAslrrniavvfqdAGLFNRSI 425
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
30-138 5.90e-03

GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding proteins, Nucleosides, purines and pyrimidines]


Pssm-ID: 130064  Cd Length: 313  Bit Score: 37.57  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2594345208  30 SPTIGLMGKTGAGKSSLINALFQSALSPVSNVSGCTRQAQLFNMTINNHTLTFIDLPGVGE-SLERDKEYHQLYRNLLPE 108
Cdd:TIGR00991  38 SLTILVMGKGGVGKSSTVNSIIGERIATVSAFQSEGLRPMMVSRTRAGFTLNIIDTPGLIEgGYINDQAVNIIKRFLLGK 117
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2594345208 109 -LDLIIWVLKADD-RAWSSDEQCYRFLTEQCG 138
Cdd:TIGR00991 118 tIDVLLYVDRLDAyRVDTLDGQVIRAITDSFG 149
PRK12289 PRK12289
small ribosomal subunit biogenesis GTPase RsgA;
37-73 6.18e-03

small ribosomal subunit biogenesis GTPase RsgA;


Pssm-ID: 237040 [Multi-domain]  Cd Length: 352  Bit Score: 37.69  E-value: 6.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2594345208  37 GKTGAGKSSLINALFQSALSPVSNVSG-------CTRQAQLFNM 73
Cdd:PRK12289  179 GPSGVGKSSLINRLIPDVELRVGKVSGklgrgrhTTRHVELFEL 222
COG4928 COG4928
Predicted P-loop ATPase, KAP-like [General function prediction only];
17-50 7.81e-03

Predicted P-loop ATPase, KAP-like [General function prediction only];


Pssm-ID: 443956  Cd Length: 386  Bit Score: 37.58  E-value: 7.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2594345208  17 DVFLSHLNKLINYSP-----TIGLMGKTGAGKSSLINAL 50
Cdd:COG4928    11 KKYAESLANLIKSSDadeplVIGLDGEWGSGKTSFLNLI 49
PLN03232 PLN03232
ABC transporter C family member; Provisional
20-52 8.48e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 37.65  E-value: 8.48e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2594345208   20 LSHLNKLINYSPTIGLMGKTGAGKSSLINALFQ 52
Cdd:PLN03232  1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
 
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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