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Conserved domains on  [gi|23397516|ref|NP_694968|]
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GTPase IMAP family member 7 [Homo sapiens]

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 ...
 9-211 6.25e-110

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: 316.78  E-value: 6.25e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   9 LRIVLVGKTGSGKSATANTILGEEIFDSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEISRCIISS 88
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516  89 CPGPHAIVLVLLLGRYTEEEQKTVALIKAVFGKSAMKHMVILFTRKEELEGQSFHDFIADADVGLKSIVKECGNRCCAFS 168
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23397516 169 NskKTSKAEKESQVQELVELIEKMVQCNEGAYFSDDIYKDTEE 211
Cdd:cd01852 161 N--KAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 9-211 6.25e-110

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: 316.78  E-value: 6.25e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   9 LRIVLVGKTGSGKSATANTILGEEIFDSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEISRCIISS 88
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516  89 CPGPHAIVLVLLLGRYTEEEQKTVALIKAVFGKSAMKHMVILFTRKEELEGQSFHDFIADADVGLKSIVKECGNRCCAFS 168
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23397516 169 NskKTSKAEKESQVQELVELIEKMVQCNEGAYFSDDIYKDTEE 211
Cdd:cd01852 161 N--KAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 9-215 2.39e-96

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 282.57  E-value: 2.39e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516     9 LRIVLVGKTGSGKSATANTILGEEIFDSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEISRCIISS 88
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516    89 CPGPHAIVLVLLLGRYTEEEQKTVALIKAVFGKSAMKHMVILFTRKEELEGQSFHDFIADAD-VGLKSIVKEcgnrccaf 167
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDGCpEFLKEVLRT-------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 23397516   168 snskkTSKAEKESQVQELVELIEKMVQCNEGAYFSDDIYKDTEERLKQ 215
Cdd:pfam04548 153 -----ADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGER 195
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 6-132 1.20e-09

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: 59.20  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516     6 DRSLRIVLVGKTGSGKSATANTILGEEIFdSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEIS--R 83
Cdd:TIGR00993 116 DFSLNILVLGKSGVGKSATINSIFGEVKF-STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLKSSASDQSKNEKILSsvK 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23397516    84 CIISSCPgPHAIVLVLLLGRYTEEEQKTVAL--IKAVFGKSAMKHMVILFT 132
Cdd:TIGR00993 195 KFIKKNP-PDIVLYVDRLDMQTRDSNDLPLLrtITDVLGPSIWFNAIVTLT 244
YeeP COG3596
Predicted GTPase [General function prediction only];
5-99 2.50e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.39  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   5 EDRSLRIVLVGKTGSGKSATANTILGEEIfdSRI-AAQAVTKNCQKASREWQGRDLLV-VDTPGLFDTKESlDTTCKEIS 82
Cdd:COG3596  36 ELPPPVIALVGKTGAGKSSLINALFGAEV--AEVgVGRPCTREIQRYRLESDGLPGLVlLDTPGLGEVNER-DREYRELR 112

                        90
                ....*....|....*..
gi 23397516  83 RCIisscPGPHAIVLVL 99
Cdd:COG3596 113 ELL----PEADLILWVV 125
PRK01889 PRK01889
GTPase RsgA; Reviewed
 11-89 3.21e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.84  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   11 IVLVGKTGSGKSATANTILGEEifdsRIAAQAVTKNCQK-----ASREW----QGRdlLVVDTPG-----LFDTKESLDT 76
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEE----VQKTGAVREDDSKgrhttTHRELhplpSGG--LLIDTPGmrelqLWDAEDGVEE 271

                         90
                 ....*....|....*..
gi 23397516   77 TCKEI----SRCIISSC 89
Cdd:PRK01889 272 TFSDIeelaAQCRFRDC 288
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 9-211 6.25e-110

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: 316.78  E-value: 6.25e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   9 LRIVLVGKTGSGKSATANTILGEEIFDSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEISRCIISS 88
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516  89 CPGPHAIVLVLLLGRYTEEEQKTVALIKAVFGKSAMKHMVILFTRKEELEGQSFHDFIADADVGLKSIVKECGNRCCAFS 168
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23397516 169 NskKTSKAEKESQVQELVELIEKMVQCNEGAYFSDDIYKDTEE 211
Cdd:cd01852 161 N--KAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 9-215 2.39e-96

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 282.57  E-value: 2.39e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516     9 LRIVLVGKTGSGKSATANTILGEEIFDSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEISRCIISS 88
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516    89 CPGPHAIVLVLLLGRYTEEEQKTVALIKAVFGKSAMKHMVILFTRKEELEGQSFHDFIADAD-VGLKSIVKEcgnrccaf 167
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDGCpEFLKEVLRT-------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 23397516   168 snskkTSKAEKESQVQELVELIEKMVQCNEGAYFSDDIYKDTEERLKQ 215
Cdd:pfam04548 153 -----ADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGER 195
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 6-132 1.48e-13

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: 68.88  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   6 DRSLRIVLVGKTGSGKSATANTILGEEIfdSRIAA-QAVTKNCQKASREWQGRDLLVVDTPGLFD-TKESLDTTCKEISR 83
Cdd:cd01853  29 DFSLTILVLGKTGVGKSSTINSIFGERK--VSVSAfQSETLRPREVSRTVDGFKLNIIDTPGLLEsQDQRVNRKILSIIK 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 23397516  84 CIISSCPgPHAIVLVLLLGRYTEE--EQKTVALIKAVFGKSAMKHMVILFT 132
Cdd:cd01853 107 RFLKKKT-IDVVLYVDRLDMYRVDnlDVPLLRAITDSFGPSIWRNAIVVLT 156
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 6-132 1.20e-09

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: 59.20  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516     6 DRSLRIVLVGKTGSGKSATANTILGEEIFdSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFDTKESLDTTCKEIS--R 83
Cdd:TIGR00993 116 DFSLNILVLGKSGVGKSATINSIFGEVKF-STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLKSSASDQSKNEKILSsvK 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23397516    84 CIISSCPgPHAIVLVLLLGRYTEEEQKTVAL--IKAVFGKSAMKHMVILFT 132
Cdd:TIGR00993 195 KFIKKNP-PDIVLYVDRLDMQTRDSNDLPLLrtITDVLGPSIWFNAIVTLT 244
YeeP COG3596
Predicted GTPase [General function prediction only];
5-99 2.50e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.39  E-value: 2.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   5 EDRSLRIVLVGKTGSGKSATANTILGEEIfdSRI-AAQAVTKNCQKASREWQGRDLLV-VDTPGLFDTKESlDTTCKEIS 82
Cdd:COG3596  36 ELPPPVIALVGKTGAGKSSLINALFGAEV--AEVgVGRPCTREIQRYRLESDGLPGLVlLDTPGLGEVNER-DREYRELR 112

                        90
                ....*....|....*..
gi 23397516  83 RCIisscPGPHAIVLVL 99
Cdd:COG3596 113 ELL----PEADLILWVV 125
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 10-133 7.60e-08

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: 49.93  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516    10 RIVLVGKTGSGKSATANTILGEeifDSRIAAQA-VTKNCQKASREWQGRDLLVVDTPGLFD---TKESLDTTCKEISRCi 85
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGA---KAIVSDYPgTTRDPNEGRLELKGKQIILVDTPGLIEgasEGEGLGRAFLAIIEA- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 23397516    86 isscpgpHAIVLVL-LLGRYTEEEQKtvaLIKavFGKSAMKHMVILFTR 133
Cdd:pfam01926  77 -------DLILFVVdSEEGITPLDEE---LLE--LLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 12-189 4.94e-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: 4.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516  12 VLVGKTGSGKSATANTILGEEIFDSRIAAQaVTKNCQKASREWQ--GRDLLVVDTPGLFDTKESLDttckeiSRCIISSC 89
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPG-TTRDPDVYVKELDkgKVKLVLVDTPGLDEFGGLGR------EELARLLL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516  90 PGPHAIVLVL-LLGRYTEEEQKTVALIKAvfgKSAMKHMVILFTRKEELEGQSfhdfiADADVGLKSIVKECGNRCCAFS 168
Cdd:cd00882  74 RGADLILLVVdSTDRESEEDAKLLILRRL---RKEGIPIILVGNKIDLLEERE-----VEELLRLEELAKILGVPVFEVS 145

                       170       180
                ....*....|....*....|.
gi 23397516 169 NSKKtskaekeSQVQELVELI 189
Cdd:cd00882 146 AKTG-------EGVDELFEKL 159
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 9-138 1.42e-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: 47.54  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   9 LRIVLVGKTGSGKSATANTILGEEIFDSRIaaQAVTKNCQKASREWQgRDLLVVDTPGLFDTKESLDttckEISRCIISS 88
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGV--TPTTAVITVLRYGLL-KGVVLVDTPGLNSTIEHHT----EITESFLPR 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 23397516  89 CpgpHAIVLVLLLGR-YTEEEQKTVALIKAVFGksamKHMVILFTRKEELE 138
Cdd:cd09912  74 A---DAVIFVLSADQpLTESEREFLKEILKWSG----KKIFFVLNKIDLLS 117
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 12-83 9.07e-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: 9.07e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397516  12 VLVGKTGSGKSATANTILGEEIFD-SRIAaqAVTKNCQKASREWQG-RDLLVVDTPGLFDTKESLDTTCKEISR 83
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIvSPIP--GTTRDPVRKEWELLPlGPVVLIDTPGLDEEGGLGRERVEEARQ 72
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
 3-69 1.09e-04

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


Pssm-ID: 130064  Cd Length: 313  Bit Score: 42.96  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397516     3 ESEDRSLRIVLVGKTGSGKSATANTILGEEIFdSRIAAQAVTKNCQKASREWQGRDLLVVDTPGLFD 69
Cdd:TIGR00991  33 EEDVSSLTILVMGKGGVGKSSTVNSIIGERIA-TVSAFQSEGLRPMMVSRTRAGFTLNIIDTPGLIE 98
PRK01889 PRK01889
GTPase RsgA; Reviewed
 11-89 3.21e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.84  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397516   11 IVLVGKTGSGKSATANTILGEEifdsRIAAQAVTKNCQK-----ASREW----QGRdlLVVDTPG-----LFDTKESLDT 76
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEE----VQKTGAVREDDSKgrhttTHRELhplpSGG--LLIDTPGmrelqLWDAEDGVEE 271

                         90
                 ....*....|....*..
gi 23397516   77 TCKEI----SRCIISSC 89
Cdd:PRK01889 272 TFSDIeelaAQCRFRDC 288
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
 12-75 4.82e-04

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: 39.73  E-value: 4.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397516  12 VLVGKTGSGKSATANTILGeeifdSRIAAQA----VTKNCQKASREWQGRDLLVVDTPGLFDTKESLD 75
Cdd:cd01894   1 AIVGRPNVGKSTLFNRLTG-----RRDAIVSdtpgVTRDRKYGEAEWGGREFILIDTGGIEPDDEGIS 63
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 12-66 5.92e-03

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: 36.55  E-value: 5.92e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23397516  12 VLVGKTGSGKSATANTILGEEIFDSRIAAqAVTKNCQKASREWQGRDLLVVDTPG 66
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEVAAVGDRR-PTTRAAQAYVWQTGGDGLVLLDLPG 54
 
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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