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Conserved domains on  [gi|513167185|ref|XP_004939120|]
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GTPase IMAP family member 7 [Gallus gallus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
11-209 8.20e-67

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


The actual alignment was detected with superfamily member cd01852:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 201  Bit Score: 204.31  E-value: 8.20e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  11 LSIILVGKTGSGKSATGNTILGKKAFLSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREANEKTAEKIKNAFQYL 90
Cdd:cd01852    1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  91 YAGVHAIILVMQLGRISQEEQEVAEWVTKIFNTKAEKYTILLFTRAEELEHpEALKAFIEGS-SYLKGLAEKCGNRYIGF 169
Cdd:cd01852   81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEG-GSLEDYLEDScEALKRLLEKCGGRYVAF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 513167185 170 SNKATREARDGQVAELIHIIDAMVEKNGDApHYTREMLEE 209
Cdd:cd01852  160 NNKAKGREQEQQVKELLAKVEEMVRENGGK-PYTNEMYEE 198
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
11-209 8.20e-67

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: 204.31  E-value: 8.20e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  11 LSIILVGKTGSGKSATGNTILGKKAFLSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREANEKTAEKIKNAFQYL 90
Cdd:cd01852    1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  91 YAGVHAIILVMQLGRISQEEQEVAEWVTKIFNTKAEKYTILLFTRAEELEHpEALKAFIEGS-SYLKGLAEKCGNRYIGF 169
Cdd:cd01852   81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEG-GSLEDYLEDScEALKRLLEKCGGRYVAF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 513167185 170 SNKATREARDGQVAELIHIIDAMVEKNGDApHYTREMLEE 209
Cdd:cd01852  160 NNKAKGREQEQQVKELLAKVEEMVRENGGK-PYTNEMYEE 198
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
11-216 2.17e-57

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 180.50  E-value: 2.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185   11 LSIILVGKTGSGKSATGNTILGKKAFLSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREANEKTAEKIKNAFQYL 90
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185   91 YAGVHAIILVMQLGRISQEEQEVAEWVTKIFNTKAEKYTILLFTRAEELEhPEALKAFIEGSS--YLKGLAEkcgnryig 168
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLE-DDSLDDYLSDGCpeFLKEVLR-------- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 513167185  169 fsnKATREARDGQVAELIHIIDAMVEKNGDAPhYTREMLEEDRQKFRR 216
Cdd:pfam04548 152 ---TADGEEKEEQVQQLLALVEAIVKENGGKP-YTNDLYEKIKEEGER 195
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
11-84 1.60e-06

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 48.02  E-value: 1.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513167185   11 LSIILVGKTGSGKSATGNTILGKKAFlSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDT---REANEKTAEKIK 84
Cdd:TIGR00993 119 LNILVLGKSGVGKSATINSIFGEVKF-STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLKSSasdQSKNEKILSSVK 194
YeeP COG3596
Predicted GTPase [General function prediction only];
13-101 1.46e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 44.76  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  13 IILVGKTGSGKSATGNTILGKKAFL------STLTAQsltrEYEKAEDcfAGRPIEVVDTPGLFDTREANEKTAEkiknA 86
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEVAEvgvgrpCTREIQ----RYRLESD--GLPGLVLLDTPGLGEVNERDREYRE----L 111
                         90
                 ....*....|....*
gi 513167185  87 FQYLYAgVHAIILVM 101
Cdd:COG3596  112 RELLPE-ADLILWVV 125
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
11-209 8.20e-67

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: 204.31  E-value: 8.20e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  11 LSIILVGKTGSGKSATGNTILGKKAFLSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREANEKTAEKIKNAFQYL 90
Cdd:cd01852    1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  91 YAGVHAIILVMQLGRISQEEQEVAEWVTKIFNTKAEKYTILLFTRAEELEHpEALKAFIEGS-SYLKGLAEKCGNRYIGF 169
Cdd:cd01852   81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEG-GSLEDYLEDScEALKRLLEKCGGRYVAF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 513167185 170 SNKATREARDGQVAELIHIIDAMVEKNGDApHYTREMLEE 209
Cdd:cd01852  160 NNKAKGREQEQQVKELLAKVEEMVRENGGK-PYTNEMYEE 198
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
11-216 2.17e-57

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 180.50  E-value: 2.17e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185   11 LSIILVGKTGSGKSATGNTILGKKAFLSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREANEKTAEKIKNAFQYL 90
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185   91 YAGVHAIILVMQLGRISQEEQEVAEWVTKIFNTKAEKYTILLFTRAEELEhPEALKAFIEGSS--YLKGLAEkcgnryig 168
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLE-DDSLDDYLSDGCpeFLKEVLR-------- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 513167185  169 fsnKATREARDGQVAELIHIIDAMVEKNGDAPhYTREMLEEDRQKFRR 216
Cdd:pfam04548 152 ---TADGEEKEEQVQQLLALVEAIVKENGGKP-YTNDLYEKIKEEGER 195
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
15-155 5.48e-10

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: 56.10  E-value: 5.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  15 LVGKTGSGKSATGNTILGKKAFL------STLTAQSltREYEKAEdcfaGRPIEVVDTPGLFDTREANEKTAEKIKNAFQ 88
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIvspipgTTRDPVR--KEWELLP----LGPVVLIDTPGLDEEGGLGRERVEEARQVAD 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513167185  89 ylyaGVHAIILVMQlGRISQEEQEvaEWVTKIFntKAEKYTILLFTRAEELEHPEALKAFIEGSSYL 155
Cdd:cd00880   76 ----RADLVLLVVD-SDLTPVEEE--AKLGLLR--ERGKPVLLVLNKIDLVPESEEEELLRERKLEL 133
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
15-172 9.22e-09

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 52.84  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  15 LVGKTGSGKSATGNTILGKK-AFLSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREANEKTAEKIknafqyLYAG 93
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEvGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARL------LLRG 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 513167185  94 VHAIILVMQLGRISQEEQEVAEWVTKIFntKAEKYTILLFTRAEELEHPEalkafIEGSSYLKGLAEKCGNRYIGFSNK 172
Cdd:cd00882   76 ADLILLVVDSTDRESEEDAKLLILRRLR--KEGIPIILVGNKIDLLEERE-----VEELLRLEELAKILGVPVFEVSAK 147
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
13-135 9.63e-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: 48.77  E-value: 9.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185   13 IILVGKTGSGKSATGNTILGKKAflstLTAQSL--TREYEKAEDCFAGRPIEVVDTPGLFDtreaNEKTAEKIKNAFQyL 90
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAKA----IVSDYPgtTRDPNEGRLELKGKQIILVDTPGLIE----GASEGEGLGRAFL-A 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 513167185   91 YAGVHAIILVMQ-LGRISQEEQEVAEWvtkifNTKAEKYTILLFTR 135
Cdd:pfam01926  73 IIEADLILFVVDsEEGITPLDEELLEL-----LRENKKPIILVLNK 113
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
11-84 1.60e-06

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 48.02  E-value: 1.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513167185   11 LSIILVGKTGSGKSATGNTILGKKAFlSTLTAQSLTREYEKAEDCFAGRPIEVVDTPGLFDT---REANEKTAEKIK 84
Cdd:TIGR00993 119 LNILVLGKSGVGKSATINSIFGEVKF-STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGLKSSasdQSKNEKILSSVK 194
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
2-84 1.91e-06

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: 47.31  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185   2 AGHQSKGSKLSIILVGKTGSGKSATGNTILG-KKAFLSTLtaQSLTREYEKAEDCFAGRPIEVVDTPGLFDTREA--NEK 78
Cdd:cd01853   23 KLKKELDFSLTILVLGKTGVGKSSTINSIFGeRKVSVSAF--QSETLRPREVSRTVDGFKLNIIDTPGLLESQDQrvNRK 100

                 ....*.
gi 513167185  79 TAEKIK 84
Cdd:cd01853  101 ILSIIK 106
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
9-145 1.91e-06

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


Pssm-ID: 130064  Cd Length: 313  Bit Score: 47.59  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185    9 SKLSIILVGKTGSGKSATGNTILGKK-AFLSTLTAQSL-------TReyekaedcfAGRPIEVVDTPGLFDTREANEKTA 80
Cdd:TIGR00991  37 SSLTILVMGKGGVGKSSTVNSIIGERiATVSAFQSEGLrpmmvsrTR---------AGFTLNIIDTPGLIEGGYINDQAV 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513167185   81 EKIKNAFqyLYAGVHAIILVMQLG--RISQEEQEVAEWVTKIFNTKAEKYTILLFTRAeELEHPEAL 145
Cdd:TIGR00991 108 NIIKRFL--LGKTIDVLLYVDRLDayRVDTLDGQVIRAITDSFGKDIWRKSLVVLTHA-QFSPPDGL 171
YeeP COG3596
Predicted GTPase [General function prediction only];
13-101 1.46e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 44.76  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  13 IILVGKTGSGKSATGNTILGKKAFL------STLTAQsltrEYEKAEDcfAGRPIEVVDTPGLFDTREANEKTAEkiknA 86
Cdd:COG3596   42 IALVGKTGAGKSSLINALFGAEVAEvgvgrpCTREIQ----RYRLESD--GLPGLVLLDTPGLGEVNERDREYRE----L 111
                         90
                 ....*....|....*
gi 513167185  87 FQYLYAgVHAIILVM 101
Cdd:COG3596  112 RELLPE-ADLILWVV 125
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
13-199 1.22e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 38.42  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  13 IILVGKTGSGKSATGNTILGKK----AFLSTLTAQSLTREYEKAEDcfaGRPIEVVDTPGLFDTREANEKtaekiknaFQ 88
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIfsleKYLSTNGVTIDKKELKLDGL---DVDLVIWDTPGQDEFRETRQF--------YA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  89 YLYAGVHAIILVMqLGRISQEEQEVAEWVTKIFNTKAEKYTILLFTRA-----EELEHPEALKAFiegssylkgLAEKCG 163
Cdd:COG1100   75 RQLTGASLYLFVV-DGTREETLQSLYELLESLRRLGKKSPIILVLNKIdlydeEEIEDEERLKEA---------LSEDNI 144
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 513167185 164 NRYIGFSnkatreARDG-QVAELIHIIDAMVEKNGDA 199
Cdd:COG1100  145 VEVVATS------AKTGeGVEELFAALAEILRGEGDS 175
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
12-133 3.83e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 37.30  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  12 SIILVGKTGSGKSATGNTILGKKaFLSTLTaqSLT-REYEKAEDCFAGRPIEVVDTPGlfdtreaNEKTAEKIknaFQYL 90
Cdd:cd04105    2 TVLLLGPSDSGKTALFTKLTTGK-VRSTVT--SIEpNVASFYSNSSKGKKLTLVDVPG-------HEKLRDKL---LEYL 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 513167185  91 YAGVHAIILVMQLGRISQEEQEVAEWVTKIFNTKA---EKYTILLF 133
Cdd:cd04105   69 KASLKAIVFVVDSATFQKNIRDVAEFLYDILTDLEkikNKIPILIA 114
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
15-119 8.96e-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: 35.49  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513167185  15 LVGKTGSGKSATGNTILGKKaflSTLTAQ--SLTRE--YEKAEdcFAGRPIEVVDTPGL-FDTREANEKTAEKIKNAFQy 89
Cdd:cd01894    2 IVGRPNVGKSTLFNRLTGRR---DAIVSDtpGVTRDrkYGEAE--WGGREFILIDTGGIePDDEGISKEIREQAEIAIE- 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 513167185  90 lyaGVHAIILVM--QLGrISQEEQEVAEWVTK 119
Cdd:cd01894   76 ---EADVILFVVdgREG-LTPADEEIAKYLRK 103
 
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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