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Conserved domains on  [gi|731159862|emb|CEK38897|]
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50S ribosome-binding GTPase family protein [[Clostridium] sordellii]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 177-327 2.88e-19

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd09912:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 180  Bit Score: 85.29  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 177 SNICEVRYfidkkGILNDFVIVDTPGLNQSLLENTNSrMLDYYNHADGIIWILDSQNVISKSSYELLEELKhnysiEKNK 256
Cdd:cd09912   35 AVITVLRY-----GLLKGVVLVDTPGLNSTIEHHTEI-TESFLPRADAVIFVLSADQPLTESEREFLKEIL-----KWSG 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 731159862 257 DNIICVVNKIDTIKNKTKD---KQKIIEKVDLLYEQNFKDIVMISARNAINGILNNDTNLIDISNIKALENSIE 327
Cdd:cd09912  104 KKIFFVLNKIDLLSEEELEevlEYSREELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLE 177
Dynamin_N super family cl47533
Dynamin family;
73-266 2.86e-11

Dynamin family;


The actual alignment was detected with superfamily member pfam00350:

Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 62.25  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862   73 GKTSLINSLIKEHFLEVRDIPNTWKLDSLVYGENKRI-----EIIYDNKISRIYNYEEGKDIIKNEEIKFKNSKNKIRYE 147
Cdd:pfam00350  10 GKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGAsegavKVEYKDGEKKFEDFSELREEIEKETEKIAGTGKGISSE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862  148 LEKYKNkekinkeelknykkiledmyiyksnicevrYFIDKKGIlndfVIVDTPGLNQSLLENTNsrMLD-YYNHADGII 226
Cdd:pfam00350  90 PIVLEI------------------------------LSPLVPGL----TLVDTPGLDSVAVGDQE--LTKeYIKPADIIL 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 731159862  227 WILDSQNVISKSSYELLEELkhnysIEKNKDNIICVVNKI 266
Cdd:pfam00350 134 AVTPANVDLSTSEALFLARE-----VDPNGKRTIGVLTKA 168
 
Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 177-327 2.88e-19

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: 85.29  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 177 SNICEVRYfidkkGILNDFVIVDTPGLNQSLLENTNSrMLDYYNHADGIIWILDSQNVISKSSYELLEELKhnysiEKNK 256
Cdd:cd09912   35 AVITVLRY-----GLLKGVVLVDTPGLNSTIEHHTEI-TESFLPRADAVIFVLSADQPLTESEREFLKEIL-----KWSG 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 731159862 257 DNIICVVNKIDTIKNKTKD---KQKIIEKVDLLYEQNFKDIVMISARNAINGILNNDTNLIDISNIKALENSIE 327
Cdd:cd09912  104 KKIFFVLNKIDLLSEEELEevlEYSREELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLE 177
era PRK00089
GTPase Era; Reviewed
 189-304 1.58e-11

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 65.07  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 189 KGILND----FVIVDTPG-------LNQSLLENTNSRMLDyynhADGIIWILDSQNVISKSSYELLEELKhnysieKNKD 257
Cdd:PRK00089  45 RGIVTEddaqIIFVDTPGihkpkraLNRAMNKAAWSSLKD----VDLVLFVVDADEKIGPGDEFILEKLK------KVKT 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 731159862 258 NIICVVNKIDTIknktKDKQKIIEKVDLLYEQ-NFKDIVMISARNAIN 304
Cdd:PRK00089 115 PVILVLNKIDLV----KDKEELLPLLEELSELmDFAEIVPISALKGDN 158
Dynamin_N pfam00350
Dynamin family;
73-266 2.86e-11

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 62.25  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862   73 GKTSLINSLIKEHFLEVRDIPNTWKLDSLVYGENKRI-----EIIYDNKISRIYNYEEGKDIIKNEEIKFKNSKNKIRYE 147
Cdd:pfam00350  10 GKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGAsegavKVEYKDGEKKFEDFSELREEIEKETEKIAGTGKGISSE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862  148 LEKYKNkekinkeelknykkiledmyiyksnicevrYFIDKKGIlndfVIVDTPGLNQSLLENTNsrMLD-YYNHADGII 226
Cdd:pfam00350  90 PIVLEI------------------------------LSPLVPGL----TLVDTPGLDSVAVGDQE--LTKeYIKPADIIL 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 731159862  227 WILDSQNVISKSSYELLEELkhnysIEKNKDNIICVVNKI 266
Cdd:pfam00350 134 AVTPANVDLSTSEALFLARE-----VDPNGKRTIGVLTKA 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
189-304 7.60e-10

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 60.00  E-value: 7.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 189 KGILND----FVIVDTPG-------LNQSLLENTNSRMLDyynhADGIIWILDSQNVISKSSYELLEELKhnysieKNKD 257
Cdd:COG1159   43 RGIVTRedaqIVFVDTPGihkpkrkLGRRMNKAAWSALED----VDVILFVVDATEKIGEGDEFILELLK------KLKT 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 731159862 258 NIICVVNKIDTIKnktkdKQKIIEKVDLLYEQ-NFKDIVMISARNAIN 304
Cdd:COG1159  113 PVILVINKIDLVK-----KEELLPLLAEYSELlDFAEIVPISALKGDN 155
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 214-304 9.61e-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: 44.78  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862  214 RMLDYYNHADGIIWILDSQNVISKSSYELLEELKhnysiekNKDNIICVVNKIDtiknktkdkqkIIEKVDLLYEQNFKD 293
Cdd:pfam12631 166 RAREAIEEADLVLLVLDASRPLDEEDLEILELLK-------DKKPIIVVLNKSD-----------LLGEIDELEELKGKP 227

                          90
                  ....*....|.
gi 731159862  294 IVMISARNAIN 304
Cdd:pfam12631 228 VLAISAKTGEG 238
 
Name Accession Description Interval E-value
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 177-327 2.88e-19

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: 85.29  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 177 SNICEVRYfidkkGILNDFVIVDTPGLNQSLLENTNSrMLDYYNHADGIIWILDSQNVISKSSYELLEELKhnysiEKNK 256
Cdd:cd09912   35 AVITVLRY-----GLLKGVVLVDTPGLNSTIEHHTEI-TESFLPRADAVIFVLSADQPLTESEREFLKEIL-----KWSG 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 731159862 257 DNIICVVNKIDTIKNKTKD---KQKIIEKVDLLYEQNFKDIVMISARNAINGILNNDTNLIDISNIKALENSIE 327
Cdd:cd09912  104 KKIFFVLNKIDLLSEEELEevlEYSREELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQSGFEELEEHLE 177
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 189-304 8.40e-12

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 63.63  E-value: 8.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 189 KGILND----FVIVDTPG-------LNQSLLENTNSRMldyyNHADGIIWILDSQNVISKSSYELLEELKhnysieKNKD 257
Cdd:cd04163   43 RGIYTDddaqIIFVDTPGihkpkkkLGERMVKAAWSAL----KDVDLVLFVVDASEWIGEGDEFILELLK------KSKT 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 731159862 258 NIICVVNKIDTIKNKtKDKQKIIEKVDLLYeqNFKDIVMISARNAIN 304
Cdd:cd04163  113 PVILVLNKIDLVKDK-EDLLPLLEKLKELH--PFAEIFPISALKGEN 156
era PRK00089
GTPase Era; Reviewed
 189-304 1.58e-11

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 65.07  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 189 KGILND----FVIVDTPG-------LNQSLLENTNSRMLDyynhADGIIWILDSQNVISKSSYELLEELKhnysieKNKD 257
Cdd:PRK00089  45 RGIVTEddaqIIFVDTPGihkpkraLNRAMNKAAWSSLKD----VDLVLFVVDADEKIGPGDEFILEKLK------KVKT 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 731159862 258 NIICVVNKIDTIknktKDKQKIIEKVDLLYEQ-NFKDIVMISARNAIN 304
Cdd:PRK00089 115 PVILVLNKIDLV----KDKEELLPLLEELSELmDFAEIVPISALKGDN 158
Dynamin_N pfam00350
Dynamin family;
73-266 2.86e-11

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 62.25  E-value: 2.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862   73 GKTSLINSLIKEHFLEVRDIPNTWKLDSLVYGENKRI-----EIIYDNKISRIYNYEEGKDIIKNEEIKFKNSKNKIRYE 147
Cdd:pfam00350  10 GKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGAsegavKVEYKDGEKKFEDFSELREEIEKETEKIAGTGKGISSE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862  148 LEKYKNkekinkeelknykkiledmyiyksnicevrYFIDKKGIlndfVIVDTPGLNQSLLENTNsrMLD-YYNHADGII 226
Cdd:pfam00350  90 PIVLEI------------------------------LSPLVPGL----TLVDTPGLDSVAVGDQE--LTKeYIKPADIIL 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 731159862  227 WILDSQNVISKSSYELLEELkhnysIEKNKDNIICVVNKI 266
Cdd:pfam00350 134 AVTPANVDLSTSEALFLARE-----VDPNGKRTIGVLTKA 168
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
189-304 7.60e-10

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 60.00  E-value: 7.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 189 KGILND----FVIVDTPG-------LNQSLLENTNSRMLDyynhADGIIWILDSQNVISKSSYELLEELKhnysieKNKD 257
Cdd:COG1159   43 RGIVTRedaqIVFVDTPGihkpkrkLGRRMNKAAWSALED----VDVILFVVDATEKIGEGDEFILELLK------KLKT 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 731159862 258 NIICVVNKIDTIKnktkdKQKIIEKVDLLYEQ-NFKDIVMISARNAIN 304
Cdd:COG1159  113 PVILVINKIDLVK-----KEELLPLLAEYSELlDFAEIVPISALKGDN 155
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 165-304 6.86e-09

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: 55.16  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 165 YKKILEDMYIYKSNICEVRYFIDKKGILNDFVIVDTPGLNQSLLENTNSRMLDYYNHADGIIWILDSQNVISkssyELLE 244
Cdd:cd00882   19 GGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGADLILLVVDSTDRES----EEDA 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 245 ELKHNYSIEKNKDNIICVVNKIDTIKNKTKDKQKIIEKVDLLYEQnfkDIVMISARNAIN 304
Cdd:cd00882   95 KLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGV---PVFEVSAKTGEG 151
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 191-299 2.73e-05

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: 44.54  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 191 ILNDFVIVDTPGL--NQSLLENTNSRMLDYYNHADGIIWILDSqnviSKSSYEllEELKHNYSIEKNKDnIICVVNKIDt 268
Cdd:cd00880   44 PLGPVVLIDTPGLdeEGGLGRERVEEARQVADRADLVLLVVDS----DLTPVE--EEAKLGLLRERGKP-VLLVLNKID- 115

                         90       100       110
                 ....*....|....*....|....*....|.
gi 731159862 269 ikNKTKDKQKIIEKVDLLYEQNFKDIVMISA 299
Cdd:cd00880  116 --LVPESEEEELLRERKLELLPDLPVIAVSA 144
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 214-304 9.61e-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: 44.78  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862  214 RMLDYYNHADGIIWILDSQNVISKSSYELLEELKhnysiekNKDNIICVVNKIDtiknktkdkqkIIEKVDLLYEQNFKD 293
Cdd:pfam12631 166 RAREAIEEADLVLLVLDASRPLDEEDLEILELLK-------DKKPIIVVLNKSD-----------LLGEIDELEELKGKP 227

                          90
                  ....*....|.
gi 731159862  294 IVMISARNAIN 304
Cdd:pfam12631 228 VLAISAKTGEG 238
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
194-301 1.21e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.05  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 194 DFVIVDTPGlnQSLLENTNSRMLDYYNHADGIIWILDSQNVIS-KSSYELLEELKHNYsiekNKDNIICVVNKIDTIKNK 272
Cdd:COG1100   54 DLVIWDTPG--QDEFRETRQFYARQLTGASLYLFVVDGTREETlQSLYELLESLRRLG----KKSPIILVLNKIDLYDEE 127

                         90       100
                 ....*....|....*....|....*....
gi 731159862 273 TKDKQKIIEkvDLLYEQNFKDIVMISARN 301
Cdd:COG1100  128 EIEDEERLK--EALSEDNIVEVVATSAKT 154
YeeP COG3596
Predicted GTPase [General function prediction only];
196-267 4.38e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 42.45  E-value: 4.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 731159862 196 VIVDTPGLNQSLLENTNSRML-DYYNHADGIIWILDSQNVISKSSYELLEELKHNYSIEKnkdnIICVVNKID 267
Cdd:COG3596   91 VLLDTPGLGEVNERDREYRELrELLPEADLILWVVKADDRALATDEEFLQALRAQYPDPP----VLVVLTQVD 159
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 181-301 7.77e-04

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 41.97  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 181 EVRYFIDkkGILndFVIVDTPGLNQS--LLEN-----TNSRMldyyNHADGIIWILDSQNVISKSSYELLEELKHnysie 253
Cdd:COG0486  253 EERINIG--GIP--VRLIDTAGLRETedEVEKigierAREAI----EEADLVLLLLDASEPLTEEDEEILEKLKD----- 319

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 731159862 254 knkDNIICVVNKIDTIKNKTKDkqkiiekvdlLYEQNFKDIVMISARN 301
Cdd:COG0486  320 ---KPVIVVLNKIDLPSEADGE----------LKSLPGEPVIAISAKT 354
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 193-304 9.00e-04

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: 40.19  E-value: 9.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 193 NDFVIVDTPG-----LNQSLLENTNSRMLDYYNHAD---GIIWILDSQNVISKSSYELLEELKHnysiekNKDNIICVVN 264
Cdd:cd01876   45 DKFRLVDLPGygyakVSKEVREKWGKLIEEYLENREnlkGVVLLIDARHGPTPIDLEMLEFLEE------LGIPFLIVLT 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 731159862 265 KIDTIKNKTKDKQKIIEKVDLLYEQNFKDIVMISARNAIN 304
Cdd:cd01876  119 KADKLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTG 158
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 194-304 3.20e-03

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 38.57  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 194 DFVIVDTPGLNQS-------LLENTNSRMldyyNHADGIIWILDSQNVISKSSYELLEELKhnysieKNKDNIICVVNKI 266
Cdd:cd01894   46 EFILIDTGGIEPDdegiskeIREQAEIAI----EEADVILFVVDGREGLTPADEEIAKYLR------KSKKPVILVVNKI 115

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 731159862 267 DTIknktKDKQKIIEkvdlLYEQNFKDIVMISARNAIN 304
Cdd:cd01894  116 DNI----KEEEEAAE----FYSLGFGEPIPISAEHGRG 145
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 186-301 7.78e-03

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


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 37.47  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731159862 186 IDKKGILndFVIVDTPGLNQSllenTNS-------RMLDYYNHADGIIWILDSQNVISKSSYELLEElkhnysieKNKDN 258
Cdd:cd04164   46 IDLGGIP--VRLIDTAGLRET----EDEiekigieRAREAIEEADLVLLVVDASEGLDEEDLEILEL--------PAKKP 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 731159862 259 IICVVNKIDtiknktkdkqkIIEKVDLLYEQNFKDIVMISARN 301
Cdd:cd04164  112 VIVVLNKSD-----------LLSDAEGISELNGKPIIAISAKT 143
 
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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