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Conserved domains on  [gi|1907169636|ref|XP_036021614|]
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GTPase IMAP family member 4 isoform X1 [Mus musculus]

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 ...
31-212 4.12e-96

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: 278.26  E-value: 4.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALT 110
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636 111 SPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEKAPKFFQEVMHEFQNRYCLFN 190
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                         170       180
                  ....*....|....*....|..
gi 1907169636 191 NRASGAEKEEQKMQLLTLVQSM 212
Cdd:cd01852   161 NKAKGREQEQQVKELLAKVEEM 182
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
31-212 4.12e-96

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: 278.26  E-value: 4.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALT 110
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636 111 SPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEKAPKFFQEVMHEFQNRYCLFN 190
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                         170       180
                  ....*....|....*....|..
gi 1907169636 191 NRASGAEKEEQKMQLLTLVQSM 212
Cdd:cd01852   161 NKAKGREQEQQVKELLAKVEEM 182
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
31-212 5.05e-83

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 245.21  E-value: 5.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALT 110
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636 111 SPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEK-APKFFQEVMHEfqnryclf 189
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgCPEFLKEVLRT-------- 152
                         170       180
                  ....*....|....*....|...
gi 1907169636 190 nnrASGAEKEEQKMQLLTLVQSM 212
Cdd:pfam04548 153 ---ADGEEKEEQVQQLLALVEAI 172
YeeP COG3596
Predicted GTPase [General function prediction only];
29-173 7.08e-15

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 71.72  E-value: 7.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  29 PQLRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDAdTQREITRYVa 108
Cdd:COG3596    38 PPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPGLVLLDTPGLGEVNERDR-EYRELRELL- 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169636 109 ltsPGPHALLLVVPLGRYTVE-EHKATQKILDmFGKQARrfMILLLTRKDDLE---DTDIHEYLEKAPK 173
Cdd:COG3596   116 ---PEADLILWVVKADDRALAtDEEFLQALRA-QYPDPP--VLVVLTQVDRLEperEWDPPYNWPSPPK 178
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
4-121 1.82e-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: 56.88  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636   4 QCGGAGFIPESSRSSHEL--GNQDQGIPQLRIVLLGKTGAGKSSTGNSILGEKVFNS---GICAKSITKVcekrVSTWDG 78
Cdd:TIGR00993  90 QGGGAFSLDAAKAMAEQLeaEGQDPLDFSLNILVLGKSGVGKSATINSIFGEVKFSTdafGMGTTSVQEI----EGLVQG 165
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907169636  79 KELVVVDTPGIFDTEVPDADTQREITRYVALTSPGPHALLLVV 121
Cdd:TIGR00993 166 VKIRVIDTPGLKSSASDQSKNEKILSSVKKFIKKNPPDIVLYV 208
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
31-89 5.88e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.03  E-value: 5.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEK---VFN-SGICAKSI-TKVcekrvsTWDGKELVVVDTPGI 89
Cdd:PRK00093  174 IKIAIIGRPNVGKSSLINALLGEErviVSDiAGTTRDSIdTPF------ERDGQKYTLIDTAGI 231
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
31-212 4.12e-96

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: 278.26  E-value: 4.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALT 110
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636 111 SPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEKAPKFFQEVMHEFQNRYCLFN 190
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                         170       180
                  ....*....|....*....|..
gi 1907169636 191 NRASGAEKEEQKMQLLTLVQSM 212
Cdd:cd01852   161 NKAKGREQEQQVKELLAKVEEM 182
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
31-212 5.05e-83

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 245.21  E-value: 5.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDADTQREITRYVALT 110
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636 111 SPGPHALLLVVPLGRYTVEEHKATQKILDMFGKQARRFMILLLTRKDDLEDTDIHEYLEK-APKFFQEVMHEfqnryclf 189
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgCPEFLKEVLRT-------- 152
                         170       180
                  ....*....|....*....|...
gi 1907169636 190 nnrASGAEKEEQKMQLLTLVQSM 212
Cdd:pfam04548 153 ---ADGEEKEEQVQQLLALVEAI 172
YeeP COG3596
Predicted GTPase [General function prediction only];
29-173 7.08e-15

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 71.72  E-value: 7.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  29 PQLRIVLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPDAdTQREITRYVa 108
Cdd:COG3596    38 PPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPGLVLLDTPGLGEVNERDR-EYRELRELL- 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907169636 109 ltsPGPHALLLVVPLGRYTVE-EHKATQKILDmFGKQARrfMILLLTRKDDLE---DTDIHEYLEKAPK 173
Cdd:COG3596   116 ---PEADLILWVVKADDRALAtDEEFLQALRA-QYPDPP--VLVVLTQVDRLEperEWDPPYNWPSPPK 178
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
6-154 6.16e-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: 65.80  E-value: 6.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636   6 GGAGFIPESSRSSHEL--GNQDQGIPQLRIVLLGKTGAGKSSTGNSILGEKV-----FNSGicAKSITKVcekrVSTWDG 78
Cdd:cd01853     5 GFQFFPDATQTKLHELeaKLKKELDFSLTILVLGKTGVGKSSTINSIFGERKvsvsaFQSE--TLRPREV----SRTVDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  79 KELVVVDTPGIFDTEVPDADTQ--REITRYVaLTSPgPHALLLVVPLGRYTVeeHKATQKIL----DMFGKQARRFMILL 152
Cdd:cd01853    79 FKLNIIDTPGLLESQDQRVNRKilSIIKRFL-KKKT-IDVVLYVDRLDMYRV--DNLDVPLLraitDSFGPSIWRNAIVV 154

                  ..
gi 1907169636 153 LT 154
Cdd:cd01853   155 LT 156
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
34-169 2.71e-12

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: 62.47  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  34 VLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVST-WDGKELVVVDTPGIFDTEVPDadtQREITRYVAltsP 112
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELdKGKVKLVLVDTPGLDEFGGLG---REELARLLL---R 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907169636 113 GPHALLLVVPLGRYTVEEHKATQKILDMFGKQARrfMILLLTRKDDLEDTDIHEYLE 169
Cdd:cd00882    75 GADLILLVVDSTDRESEEDAKLLILRRLRKEGIP--IILVGNKIDLLEEREVEELLR 129
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
4-121 1.82e-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: 56.88  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636   4 QCGGAGFIPESSRSSHEL--GNQDQGIPQLRIVLLGKTGAGKSSTGNSILGEKVFNS---GICAKSITKVcekrVSTWDG 78
Cdd:TIGR00993  90 QGGGAFSLDAAKAMAEQLeaEGQDPLDFSLNILVLGKSGVGKSATINSIFGEVKFSTdafGMGTTSVQEI----EGLVQG 165
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907169636  79 KELVVVDTPGIFDTEVPDADTQREITRYVALTSPGPHALLLVV 121
Cdd:TIGR00993 166 VKIRVIDTPGLKSSASDQSKNEKILSSVKKFIKKNPPDIVLYV 208
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-155 4.96e-09

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: 52.24  E-value: 4.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  32 RIVLLGKTGAGKSSTGNSILGEKVFNSGIcaKSITKVCEKRVSTWDGKELVVVDTPGIFDtevpDADTQREITR-YVALT 110
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDY--PGTTRDPNEGRLELKGKQIILVDTPGLIE----GASEGEGLGRaFLAII 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907169636 111 SpgPHALLLVVPlgryTVEEHKATQKILDMFGKQARRFMILLLTR 155
Cdd:pfam01926  75 E--ADLILFVVD----SEEGITPLDEELLELLRENKKPIILVLNK 113
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
30-182 6.65e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 53.45  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  30 QLRIVLLGKTGAGKSSTGNSILGEKVFNS------GIcaksitKVCEKRVSTWDGK-ELVVVDTPGIfdtevpdaDTQRE 102
Cdd:COG1100     3 EKKIVVVGTGGVGKTSLVNRLVGDIFSLEkylstnGV------TIDKKELKLDGLDvDLVIWDTPGQ--------DEFRE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636 103 ITRYVALTSPGPHALLLVV----PLGRYTVEEHkatQKILDMFGKQARrfMILLLTRKDDLEDTDIHEYLEKAPKFFQEV 178
Cdd:COG1100    69 TRQFYARQLTGASLYLFVVdgtrEETLQSLYEL---LESLRRLGKKSP--IILVLNKIDLYDEEEIEDEERLKEALSEDN 143

                  ....
gi 1907169636 179 MHEF 182
Cdd:COG1100   144 IVEV 147
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
34-174 2.94e-08

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: 51.09  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  34 VLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTWDGKELVVVDTPGIFDTEVPD----ADTQREITRYval 109
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGrervEEARQVADRA--- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169636 110 tspgpHALLLVVPLGRYTVEEhkaTQKILDMFGKQARrfMILLLTrKDDLEDTDIHEYLEKAPKF 174
Cdd:cd00880    78 -----DLVLLVVDSDLTPVEE---EAKLGLLRERGKP--VLLVLN-KIDLVPESEEEELLRERKL 131
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
10-154 6.82e-08

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


Pssm-ID: 130064  Cd Length: 313  Bit Score: 51.82  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  10 FIPESSRSSHE-LGN-QDQGIPQLRIVLLGKTGAGKSSTGNSILGEKVFN-SGICAKSITKVCEKRvsTWDGKELVVVDT 86
Cdd:TIGR00991  16 FPPATQTKLLElLGKlKEEDVSSLTILVMGKGGVGKSSTVNSIIGERIATvSAFQSEGLRPMMVSR--TRAGFTLNIIDT 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  87 PGIFDTEVPDADTQREITRYvaLTSPGPHALLLVVPLGRYTVE--EHKATQKILDMFGKQARRFMILLLT 154
Cdd:TIGR00991  94 PGLIEGGYINDQAVNIIKRF--LLGKTIDVLLYVDRLDAYRVDtlDGQVIRAITDSFGKDIWRKSLVVLT 161
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
34-122 7.57e-07

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: 46.95  E-value: 7.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  34 VLLGKTGAGKSSTGNSILGEKVFNSGICAKSITKVCEKRVSTwDGKELVVVDTPGIFDTEVPDADTQREITRYVALTSpg 113
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQT-GGDGLVLLDLPGVGERGRRDREYEELYRRLLPEAD-- 77

                  ....*....
gi 1907169636 114 phALLLVVP 122
Cdd:cd11383    78 --LVLWLLD 84
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
31-161 5.03e-05

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: 42.53  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVFNSGI--CAKSITKVcekRVSTWDGkeLVVVDTPGIFDTEvpdaDTQREITRYVA 108
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVtpTTAVITVL---RYGLLKG--VVLVDTPGLNSTI----EHHTEITESFL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907169636 109 LTSpgpHALLLVVPLGR-YTVEEHKATQKILDMFGKQarrfMILLLTRKDDLED 161
Cdd:cd09912    72 PRA---DAVIFVLSADQpLTESEREFLKEILKWSGKK----IFFVLNKIDLLSE 118
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
31-89 3.87e-04

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 39.72  E-value: 3.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEK---VFN-SGICAKSI-TKVcekrvsTWDGKELVVVDTPGI 89
Cdd:cd01895     3 IKIAIIGRPNVGKSSLLNALLGEErviVSDiAGTTRDSIdVPF------EYDGQKYTLIDTAGI 60
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
31-178 5.45e-04

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: 39.37  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEKVfnsgicakSIT--KVCEKR-----VSTWDGKELVVVDTPGIFDTE---------- 93
Cdd:cd04163     4 GFVAIIGRPNVGKSTLLNALVGQKI--------SIVspKPQTTRnrirgIYTDDDAQIIFVDTPGIHKPKkklgermvka 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  94 ----VPDADtqreitryvaltspgphALLLVVPLGRYTVEEHKatqKILDMFgKQARRFMILLLTRKDDLEDTD-----I 164
Cdd:cd04163    76 awsaLKDVD-----------------LVLFVVDASEWIGEGDE---FILELL-KKSKTPVILVLNKIDLVKDKEdllplL 134
                         170
                  ....*....|....
gi 1907169636 165 HEYLEKAPkfFQEV 178
Cdd:cd04163   135 EKLKELHP--FAEI 146
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
31-89 5.88e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.03  E-value: 5.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEK---VFN-SGICAKSI-TKVcekrvsTWDGKELVVVDTPGI 89
Cdd:PRK00093  174 IKIAIIGRPNVGKSSLINALLGEErviVSDiAGTTRDSIdTPF------ERDGQKYTLIDTAGI 231
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
24-89 1.09e-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: 38.53  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907169636  24 QDQGIPQLR-------IVLLGKTGAGKSSTGNSILGEKVFnsgicaksitKVCEkrVSTWDGK--------ELV------ 82
Cdd:cd01854    72 TGEGLDELRellkgktSVLVGQSGVGKSTLLNALLPELVL----------ATGE--ISEKLGRgrhttthrELFplpggg 139

                  ....*...
gi 1907169636  83 -VVDTPGI 89
Cdd:cd01854   140 lIIDTPGF 147
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
31-89 2.01e-03

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 38.47  E-value: 2.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907169636  31 LRIVLLGKTGAGKSSTGNSILGEK---VFN-SGICAKSI-TKVcekrvsTWDGKELVVVDTPGI 89
Cdd:COG1160   176 IKIAIVGRPNVGKSSLINALLGEErviVSDiAGTTRDSIdTPF------ERDGKKYTLIDTAGI 233
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
32-91 4.76e-03

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: 36.58  E-value: 4.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907169636  32 RIVLLGKTGAGKSSTGNSILGEKVFNSGICAkSITKVCEKRVSTWDGK--ELVVVDTPGIFD 91
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLLGNKGSITEYYP-GTTRNYVTTVIEEDGKtyKFNLLDTAGQED 63
era PRK00089
GTPase Era; Reviewed
33-90 4.95e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 36.95  E-value: 4.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907169636  33 IVLLGKTGAGKSSTGNSILGEKVfnsgicakSIT--KVCEKR-----VSTWDGKELVVVDTPGIF 90
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKI--------SIVspKPQTTRhrirgIVTEDDAQIIFVDTPGIH 64
 
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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