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Conserved domains on  [gi|47550801|ref|NP_999926|]
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uncharacterized protein LOC406638 [Danio rerio]

Protein Classification

GTPase IMAP family protein( domain architecture ID 10111261)

GTPase immunity-associated protein (IMAP) family protein may function as regulator of lymphocyte survival and homeostasis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 1-198 2.13e-90

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: 264.78  E-value: 2.13e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   1 MVLVGKTGSGKSASGNTLLGlgDFQFKTKMSSKSITRSSERYLAEVEGKIISVIDTPGICDTSMSEEELKKEMERCVYMS 80
Cdd:cd01852   3 LVLVGKTGNGKSATGNTILG--RKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  81 VPGPHVFLLVIRLGRLTAEEKHAVKWIQENFGQEAARYTIILFTHADQLKGEPLDEYISENN-DLKALVSQCGDRYHSFN 159
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCeALKRLLEKCGGRYVAFN 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 47550801 160 N--EDMINRSQVTELMEKIEKMVEENGGQHYTNEMYKKAQE 198
Cdd:cd01852 161 NkaKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 1-198 2.13e-90

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: 264.78  E-value: 2.13e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   1 MVLVGKTGSGKSASGNTLLGlgDFQFKTKMSSKSITRSSERYLAEVEGKIISVIDTPGICDTSMSEEELKKEMERCVYMS 80
Cdd:cd01852   3 LVLVGKTGNGKSATGNTILG--RKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  81 VPGPHVFLLVIRLGRLTAEEKHAVKWIQENFGQEAARYTIILFTHADQLKGEPLDEYISENN-DLKALVSQCGDRYHSFN 159
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCeALKRLLEKCGGRYVAFN 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 47550801 160 N--EDMINRSQVTELMEKIEKMVEENGGQHYTNEMYKKAQE 198
Cdd:cd01852 161 NkaKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 2-201 1.14e-67

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 207.08  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801     2 VLVGKTGSGKSASGNTLLGlgDFQFKTKMSSKSITRSSERYLAEVEGKIISVIDTPGICDTSMSEEELKKEMERCVYMSV 81
Cdd:pfam04548   4 VLVGKTGNGKSATGNSILG--RKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801    82 PGPHVFLLVIRLGRLTAEEKHAVKWIQENFGQEAARYTIILFTHADQLKGEPLDEYISE--NNDLKALVSQcgdryhsfN 159
Cdd:pfam04548  82 PGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgcPEFLKEVLRT--------A 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 47550801   160 NEDMINRsQVTELMEKIEKMVEENGGQHYTNEMYKKAQEKIE 201
Cdd:pfam04548 154 DGEEKEE-QVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGE 194
YeeP COG3596
Predicted GTPase [General function prediction only];
2-142 5.05e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 52.46  E-value: 5.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   2 VLVGKTGSGKSASGNTLLGlgdfqfktkmSSKSI-------TRSSERY-LAEVEGKIISVIDTPGIcDTSMSEEELKKEM 73
Cdd:COG3596  43 ALVGKTGAGKSSLINALFG----------AEVAEvgvgrpcTREIQRYrLESDGLPGLVLLDTPGL-GEVNERDREYREL 111

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  74 ERCvymsVPGPHVFLLVIR-LGRLTAEEKHAVKWIQENFGQEAaryTIILFTHADQLkgEPLDEYISENN 142
Cdd:COG3596 112 REL----LPEADLILWVVKaDDRALATDEEFLQALRAQYPDPP---VLVVLTQVDRL--EPEREWDPPYN 172
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 1-134 5.95e-07

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: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801     1 MVLvGKTGSGKSASGNTLLGLGDFQFKT-KMSSKSITRSSerylAEVEGKIISVIDTPGICDTSMSE-------EELKKE 72
Cdd:TIGR00993 122 LVL-GKSGVGKSATINSIFGEVKFSTDAfGMGTTSVQEIE----GLVQGVKIRVIDTPGLKSSASDQsknekilSSVKKF 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47550801    73 MERCvymsvPgPHVFLLVIRLGRLTAEEKHA--VKWIQENFGQEAARYTIILFTHA-----DQLKGEPL 134
Cdd:TIGR00993 197 IKKN-----P-PDIVLYVDRLDMQTRDSNDLplLRTITDVLGPSIWFNAIVTLTHAasappDGPNGTPL 259
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 1-198 2.13e-90

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: 264.78  E-value: 2.13e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   1 MVLVGKTGSGKSASGNTLLGlgDFQFKTKMSSKSITRSSERYLAEVEGKIISVIDTPGICDTSMSEEELKKEMERCVYMS 80
Cdd:cd01852   3 LVLVGKTGNGKSATGNTILG--RKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  81 VPGPHVFLLVIRLGRLTAEEKHAVKWIQENFGQEAARYTIILFTHADQLKGEPLDEYISENN-DLKALVSQCGDRYHSFN 159
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCeALKRLLEKCGGRYVAFN 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 47550801 160 N--EDMINRSQVTELMEKIEKMVEENGGQHYTNEMYKKAQE 198
Cdd:cd01852 161 NkaKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 2-201 1.14e-67

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 207.08  E-value: 1.14e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801     2 VLVGKTGSGKSASGNTLLGlgDFQFKTKMSSKSITRSSERYLAEVEGKIISVIDTPGICDTSMSEEELKKEMERCVYMSV 81
Cdd:pfam04548   4 VLVGKTGNGKSATGNSILG--RKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801    82 PGPHVFLLVIRLGRLTAEEKHAVKWIQENFGQEAARYTIILFTHADQLKGEPLDEYISE--NNDLKALVSQcgdryhsfN 159
Cdd:pfam04548  82 PGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgcPEFLKEVLRT--------A 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 47550801   160 NEDMINRsQVTELMEKIEKMVEENGGQHYTNEMYKKAQEKIE 201
Cdd:pfam04548 154 DGEEKEE-QVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGE 194
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 2-178 1.01e-10

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: 58.62  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   2 VLVGKTGSGKSASGNTLLGlGDFQFKTKMSSKSITRSSERYLAEVEGKIISVIDTPGIcdtsmsEEELKKEMERCVYMSV 81
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLG-GEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGL------DEFGGLGREELARLLL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  82 PGPHVFLLVIRLGRLTAEEKHAVKWIQENFGQEAarYTIILFTHADQLKGEPLDEYIsennDLKALVSQCGDRYHSFNNe 161
Cdd:cd00882  74 RGADLILLVVDSTDRESEEDAKLLILRRLRKEGI--PIILVGNKIDLLEEREVEELL----RLEELAKILGVPVFEVSA- 146

                       170
                ....*....|....*..
gi 47550801 162 dmINRSQVTELMEKIEK 178
Cdd:cd00882 147 --KTGEGVDELFEKLIE 161
YeeP COG3596
Predicted GTPase [General function prediction only];
2-142 5.05e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 52.46  E-value: 5.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   2 VLVGKTGSGKSASGNTLLGlgdfqfktkmSSKSI-------TRSSERY-LAEVEGKIISVIDTPGIcDTSMSEEELKKEM 73
Cdd:COG3596  43 ALVGKTGAGKSSLINALFG----------AEVAEvgvgrpcTREIQRYrLESDGLPGLVLLDTPGL-GEVNERDREYREL 111

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  74 ERCvymsVPGPHVFLLVIR-LGRLTAEEKHAVKWIQENFGQEAaryTIILFTHADQLkgEPLDEYISENN 142
Cdd:COG3596 112 REL----LPEADLILWVVKaDDRALATDEEFLQALRAQYPDPP---VLVVLTQVDRL--EPEREWDPPYN 172
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 2-136 1.74e-07

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: 50.39  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   2 VLVGKTGSGKSASGNTLLGlgdfQFKTKMSS-KSITRSSERYLAEVEGKIISVIDTPGI---CDTSMSEEELKKeMERcv 77
Cdd:cd01853  35 LVLGKTGVGKSSTINSIFG----ERKVSVSAfQSETLRPREVSRTVDGFKLNIIDTPGLlesQDQRVNRKILSI-IKR-- 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47550801  78 YMSVPGPHVFLLVIRLG--RLTAEEKHAVKWIQENFGQEAARYTIILFTHA-----DQLKGEPLDE 136
Cdd:cd01853 108 FLKKKTIDVVLYVDRLDmyRVDNLDVPLLRAITDSFGPSIWRNAIVVLTHAqssppDGPNGTPFSY 173
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 1-134 5.95e-07

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: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801     1 MVLvGKTGSGKSASGNTLLGLGDFQFKT-KMSSKSITRSSerylAEVEGKIISVIDTPGICDTSMSE-------EELKKE 72
Cdd:TIGR00993 122 LVL-GKSGVGKSATINSIFGEVKFSTDAfGMGTTSVQEIE----GLVQGVKIRVIDTPGLKSSASDQsknekilSSVKKF 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47550801    73 MERCvymsvPgPHVFLLVIRLGRLTAEEKHA--VKWIQENFGQEAARYTIILFTHA-----DQLKGEPL 134
Cdd:TIGR00993 197 IKKN-----P-PDIVLYVDRLDMQTRDSNDLplLRTITDVLGPSIWFNAIVTLTHAasappDGPNGTPL 259
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 2-180 7.05e-06

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: 44.93  E-value: 7.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   2 VLVGKTGSGKSASGNTLlgLGDFQFKTkmSSKS-ITRSSERYLAEVEGKI-ISVIDTPGICDTSMSEEELKKEMERcVYM 79
Cdd:cd00880   1 AIFGRPNVGKSSLLNAL--LGQNVGIV--SPIPgTTRDPVRKEWELLPLGpVVLIDTPGLDEEGGLGRERVEEARQ-VAD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801  80 SVpgpHVFLLVIRLGRLTAEEKHAVKWIqenfgQEAARYTIILFTHADQLKGEPLDEYISENndlkalvsqcgdRYHSFN 159
Cdd:cd00880  76 RA---DLVLLVVDSDLTPVEEEAKLGLL-----RERGKPVLLVLNKIDLVPESEEEELLRER------------KLELLP 135

                       170       180
                ....*....|....*....|....*.
gi 47550801 160 NEDMI-----NRSQVTELMEKIEKMV 180
Cdd:cd00880 136 DLPVIavsalPGEGIDELRKKIAELL 161
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 2-110 5.44e-05

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: 41.45  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801     2 VLVGKTGSGKSASGNTLLGLgdfqfKTKMSSKS-ITRSSERYLAEVEGKIISVIDTPGICDTSMSEEELKKE---MERCv 77
Cdd:pfam01926   3 ALVGRPNVGKSTLINALTGA-----KAIVSDYPgTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAflaIIEA- 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 47550801    78 ymsvpgpHVFLLVI-RLGRLTAEEKHAVKWIQEN 110
Cdd:pfam01926  77 -------DLILFVVdSEEGITPLDEELLELLREN 103
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
 1-152 3.42e-04

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


Pssm-ID: 130064  Cd Length: 313  Bit Score: 41.04  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801     1 MVLVGKTGSGKSASGNTLLG-----LGDFQ---FKTKMSSKsiTRSserylaeveGKIISVIDTPGICDTSMSEEELKKE 72
Cdd:TIGR00991  41 ILVMGKGGVGKSSTVNSIIGeriatVSAFQsegLRPMMVSR--TRA---------GFTLNIIDTPGLIEGGYINDQAVNI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801    73 MERCVY-MSVpgpHVFLLVIRLG--RLTAEEKHAVKWIQENFGQEAARYTIILFTHAdQLK---GEPLDEYISENNDLKA 146
Cdd:TIGR00991 110 IKRFLLgKTI---DVLLYVDRLDayRVDTLDGQVIRAITDSFGKDIWRKSLVVLTHA-QFSppdGLEYNDFFSKRSEALL 185


                  ....*.
gi 47550801   147 LVSQCG 152
Cdd:TIGR00991 186 RVIHSG 191
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 2-107 1.63e-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: 37.80  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550801   2 VLVGKTGSGKSASGNTLLGlgdfqfktkmSSKSI-------TRSSERYLAEVEGKIISVIDTPGICDtsmSEEELKKEME 74
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTG----------RRDAIvsdtpgvTRDRKYGEAEWGGREFILIDTGGIEP---DDEGISKEIR 67

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47550801  75 RCVYMSVPGPHVFLLVI--RLGrLTAEEKHAVKWI 107
Cdd:cd01894  68 EQAEIAIEEADVILFVVdgREG-LTPADEEIAKYL 101
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 2-59 3.02e-03

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: 37.76  E-value: 3.02e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47550801   2 VLVGKTGSGKSasgnTLLG--LGDFQFKTKMSSKSI------TRSSERYLAEVEGKIIsviDTPGI 59
Cdd:cd01854  89 VLVGQSGVGKS----TLLNalLPELVLATGEISEKLgrgrhtTTHRELFPLPGGGLII---DTPGF 147
 
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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