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Conserved domains on  [gi|15217719|ref|NP_174652|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

AIG1 domain-containing protein( domain architecture ID 10518548)

AIG1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
20-235 3.73e-104

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


:

Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 303.38  E-value: 3.73e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    20 KNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAvTPCGTGINVIDTPGLFDLSVSAEYLSQEIINCLVL 99
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSR-TWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719   100 AEDGLHAVVLVLSVRtRISQEEEATLNTLQVIFGSQIIDYLVVLFTGGDELEANNmtLDDYLSKGCPEFLKTVLrlcggr 179
Cdd:pfam04548  80 AEPGPHAVLLVLSLG-RFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDS--LDDYLSDGCPEFLKEVL------ 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15217719   180 rilfdnRTTDEGKKVKQVQELLAHVAAIEKSTSGIPFTDEMHRKIQKEAETLREQQ 235
Cdd:pfam04548 151 ------RTADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGERLREQQ 200
 
Name Accession Description Interval E-value
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
20-235 3.73e-104

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 303.38  E-value: 3.73e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    20 KNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAvTPCGTGINVIDTPGLFDLSVSAEYLSQEIINCLVL 99
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSR-TWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719   100 AEDGLHAVVLVLSVRtRISQEEEATLNTLQVIFGSQIIDYLVVLFTGGDELEANNmtLDDYLSKGCPEFLKTVLrlcggr 179
Cdd:pfam04548  80 AEPGPHAVLLVLSLG-RFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDS--LDDYLSDGCPEFLKEVL------ 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15217719   180 rilfdnRTTDEGKKVKQVQELLAHVAAIEKSTSGIPFTDEMHRKIQKEAETLREQQ 235
Cdd:pfam04548 151 ------RTADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGERLREQQ 200
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
20-226 2.48e-97

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: 285.97  E-value: 2.48e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  20 KNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAVTpCGTGINVIDTPGLFDLSVSAEYLSQEIINCLVL 99
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVW-DGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719 100 AEDGLHAVVLVLSVRtRISQEEEATLNTLQVIFGSQIIDYLVVLFTGGDELEANnmTLDDYLSKGCpEFLKTVLRLCGGR 179
Cdd:cd01852  80 SAPGPHAFLLVVPLG-RFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGG--SLEDYLEDSC-EALKRLLEKCGGR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15217719 180 RILFDNRTTDEgKKVKQVQELLAHVAAIEKSTSGIPFTDEMHRKIQK 226
Cdd:cd01852 156 YVAFNNKAKGR-EQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
21-90 1.19e-06

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: 49.95  E-value: 1.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15217719    21 NIVLVGRTGNGKSATGNSLIGKQVFrsETRATGVTMKCETCVAVTPCGTGINVIDTPGL----FDLSVSAEYLS 90
Cdd:TIGR00993 120 NILVLGKSGVGKSATINSIFGEVKF--STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLkssaSDQSKNEKILS 191
YeeP COG3596
Predicted GTPase [General function prediction only];
21-129 6.97e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 6.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  21 NIVLVGRTGNGKSATGNSLIGKQVFR-SETRATgvTMKCETCVAVTPCGTGINVIDTPGLFDlSVSAEYLSQEIINCLVL 99
Cdd:COG3596  41 VIALVGKTGAGKSSLINALFGAEVAEvGVGRPC--TREIQRYRLESDGLPGLVLLDTPGLGE-VNERDREYRELRELLPE 117
                        90       100       110
                ....*....|....*....|....*....|
gi 15217719 100 AedglHAVVLVLSVRTRISQEEEATLNTLQ 129
Cdd:COG3596 118 A----DLILWVVKADDRALATDEEFLQALR 143
 
Name Accession Description Interval E-value
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
20-235 3.73e-104

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 303.38  E-value: 3.73e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    20 KNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAvTPCGTGINVIDTPGLFDLSVSAEYLSQEIINCLVL 99
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSR-TWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719   100 AEDGLHAVVLVLSVRtRISQEEEATLNTLQVIFGSQIIDYLVVLFTGGDELEANNmtLDDYLSKGCPEFLKTVLrlcggr 179
Cdd:pfam04548  80 AEPGPHAVLLVLSLG-RFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDS--LDDYLSDGCPEFLKEVL------ 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15217719   180 rilfdnRTTDEGKKVKQVQELLAHVAAIEKSTSGIPFTDEMHRKIQKEAETLREQQ 235
Cdd:pfam04548 151 ------RTADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGERLREQQ 200
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
20-226 2.48e-97

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: 285.97  E-value: 2.48e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  20 KNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAVTpCGTGINVIDTPGLFDLSVSAEYLSQEIINCLVL 99
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVW-DGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719 100 AEDGLHAVVLVLSVRtRISQEEEATLNTLQVIFGSQIIDYLVVLFTGGDELEANnmTLDDYLSKGCpEFLKTVLRLCGGR 179
Cdd:cd01852  80 SAPGPHAFLLVVPLG-RFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGG--SLEDYLEDSC-EALKRLLEKCGGR 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15217719 180 RILFDNRTTDEgKKVKQVQELLAHVAAIEKSTSGIPFTDEMHRKIQK 226
Cdd:cd01852 156 YVAFNNKAKGR-EQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
21-145 1.56e-10

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: 60.41  E-value: 1.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  21 NIVLVGRTGNGKSATGNSLIGKQV-----FRSETraTGVTMkcetcVAVTPCGTGINVIDTPGLFD----------LSVS 85
Cdd:cd01853  33 TILVLGKTGVGKSSTINSIFGERKvsvsaFQSET--LRPRE-----VSRTVDGFKLNIIDTPGLLEsqdqrvnrkiLSII 105
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  86 AEYLSQEIINClVLAEDGLHAvvlvlsvrTRISQEEEATLNTLQVIFGSQIIDYLVVLFT 145
Cdd:cd01853 106 KRFLKKKTIDV-VLYVDRLDM--------YRVDNLDVPLLRAITDSFGPSIWRNAIVVLT 156
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
23-143 6.00e-07

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: 48.61  E-value: 6.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  23 VLVGRTGNGKSATGNSLIGKQVFRSETRaTGVTMKCETCVAVTPCGT-GINVIDTPGLFDLSVS-AEYLSQEIINclvla 100
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDV-PGTTRDPDVYVKELDKGKvKLVLVDTPGLDEFGGLgREELARLLLR----- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15217719 101 edGLHAVVLVLSVRTRISqEEEATLNTLQVIFGSQiIDYLVVL 143
Cdd:cd00882  75 --GADLILLVVDSTDRES-EEDAKLLILRRLRKEG-IPIILVG 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
23-128 7.08e-07

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: 48.40  E-value: 7.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  23 VLVGRTGNGKSATGNSLIGKQVFRSETRAtGVTMKCETCVAVTPCGTGINVIDTPGLFDLSVSAEYLSQEIINclvlAED 102
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIVSPIP-GTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQ----VAD 75
                        90       100
                ....*....|....*....|....*.
gi 15217719 103 GLHAVVLVLSVRTRISqEEEATLNTL 128
Cdd:cd00880  76 RADLVLLVVDSDLTPV-EEEAKLGLL 100
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
21-90 1.19e-06

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: 49.95  E-value: 1.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15217719    21 NIVLVGRTGNGKSATGNSLIGKQVFrsETRATGVTMKCETCVAVTPCGTGINVIDTPGL----FDLSVSAEYLS 90
Cdd:TIGR00993 120 NILVLGKSGVGKSATINSIFGEVKF--STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLkssaSDQSKNEKILS 191
YeeP COG3596
Predicted GTPase [General function prediction only];
21-129 6.97e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 6.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  21 NIVLVGRTGNGKSATGNSLIGKQVFR-SETRATgvTMKCETCVAVTPCGTGINVIDTPGLFDlSVSAEYLSQEIINCLVL 99
Cdd:COG3596  41 VIALVGKTGAGKSSLINALFGAEVAEvGVGRPC--TREIQRYRLESDGLPGLVLLDTPGLGE-VNERDREYRELRELLPE 117
                        90       100       110
                ....*....|....*....|....*....|
gi 15217719 100 AedglHAVVLVLSVRTRISQEEEATLNTLQ 129
Cdd:COG3596 118 A----DLILWVVKADDRALATDEEFLQALR 143
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
21-137 7.15e-06

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: 45.62  E-value: 7.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719  21 NIVLVGRTGNGKSATGNSLIGKQVF-RSETRATGVtmkceTCVAVTPCGTGINVIDTPGLFDLSVSAEYLSQEII-NClv 98
Cdd:cd09912   2 LLAVVGEFSAGKSTLLNALLGEEVLpTGVTPTTAV-----ITVLRYGLLKGVVLVDTPGLNSTIEHHTEITESFLpRA-- 74
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15217719  99 laedglHAVVLVLSVRTRISQEEEATLNTLQVIFGSQII 137
Cdd:cd09912  75 ------DAVIFVLSADQPLTESEREFLKEILKWSGKKIF 107
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
21-143 8.71e-06

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 44.15  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    21 NIVLVGRTGNGKSATGNSLIGKqvfRSETRAT-GVTmKCETCVAVTPCGTGINVIDTPGLFDLSVSAEYLSQEIinclvL 99
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGA---KAIVSDYpGTT-RDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAF-----L 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15217719   100 AEDGLHAVVLVLSVRTRISQEEEATLNTLQvifgSQIIDYLVVL 143
Cdd:pfam01926  72 AIIEADLILFVVDSEEGITPLDEELLELLR----ENKKPIILVL 111
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
19-78 1.25e-04

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 41.97  E-value: 1.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    19 IKNIVLVGRTGNGKSATGNSLIGKQVFRSETRATGVTMKCETCVAVTPCGTGINVIDTPG 78
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
23-91 2.12e-04

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 40.79  E-value: 2.12e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15217719  23 VLVGRTGNGKSATGNSLigkqvFRSETRATGVTMKCETcvAVTPC-----GTGINVIDTPGL-----FDLSVSAEYLSQ 91
Cdd:cd11383   1 GLMGKTGAGKSSLCNAL-----FGTEVAAVGDRRPTTR--AAQAYvwqtgGDGLVLLDLPGVgergrRDREYEELYRRL 72
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
22-172 2.40e-04

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


Pssm-ID: 130064  Cd Length: 313  Bit Score: 42.19  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    22 IVLVGRTGNGKSATGNSLIGKQVfrsetrATGVTMKCE----TCVAVTPCGTGINVIDTPGLfdlsVSAEYLSQEIINcl 97
Cdd:TIGR00991  41 ILVMGKGGVGKSSTVNSIIGERI------ATVSAFQSEglrpMMVSRTRAGFTLNIIDTPGL----IEGGYINDQAVN-- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217719    98 VLAEDGLHAVVLVLSVRTRISQEEEATLNTlQVI------FGSQIIDYLVVLFTGGDELEANNMTLDDYLSKGCPEFLKT 171
Cdd:TIGR00991 109 IIKRFLLGKTIDVLLYVDRLDAYRVDTLDG-QVIraitdsFGKDIWRKSLVVLTHAQFSPPDGLEYNDFFSKRSEALLRV 187

                  .
gi 15217719   172 V 172
Cdd:TIGR00991 188 I 188
 
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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