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Conserved domains on  [gi|966938842|ref|XP_014991858|]
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GTP-binding protein 2 isoform X1 [Macaca mulatta]

Protein Classification

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 ...
 169-328 1.50e-81

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 cd04165:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 224  Bit Score: 253.75  E-value: 1.50e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 169 QVVNYSDSRTAE---EICESSSKMITFIDLAGHHKYLHTTIFGLTSYCPDCALLLVSANTGIAGTTREHLGLALALKVPF 245
Cdd:cd04165   62 EVVNYPDNHLGEldvEICEKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 246 FIVVSKIDLCAKTTVERTVRQLERVLKQPGCHKVPMLVTSEDDAVTAAQQFaQSPNVTPIFTLSSVSGESLDLLKVFLNI 325
Cdd:cd04165  142 FVVVTKIDMTPANVLQETLKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNL-SSGRVVPIFQVSNVTGEGLDLLRRFLNL 220


                 ...
gi 966938842 326 LPP 328
Cdd:cd04165  221 LPP 223
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 435-522 2.25e-42

Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


:

Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 146.12  E-value: 2.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 435 TICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHaKDKLRTGEKAVVRFRFLKHPEYLKVGAKLLFREGVTK 514
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISID-KEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTK 79


                 ....*...
gi 966938842 515 GIGHVTDV 522
Cdd:cd03708   80 GIGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 343-429 4.25e-41

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


:

Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 142.74  E-value: 4.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 343 TEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLR 422
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*..
gi 966938842 423 KGMVMVS 429
Cdd:cd03694   81 KGMVLVS 87
 
Name Accession Description Interval E-value
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 169-328 1.50e-81

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 253.75  E-value: 1.50e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 169 QVVNYSDSRTAE---EICESSSKMITFIDLAGHHKYLHTTIFGLTSYCPDCALLLVSANTGIAGTTREHLGLALALKVPF 245
Cdd:cd04165   62 EVVNYPDNHLGEldvEICEKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 246 FIVVSKIDLCAKTTVERTVRQLERVLKQPGCHKVPMLVTSEDDAVTAAQQFaQSPNVTPIFTLSSVSGESLDLLKVFLNI 325
Cdd:cd04165  142 FVVVTKIDMTPANVLQETLKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNL-SSGRVVPIFQVSNVTGEGLDLLRRFLNL 220


                 ...
gi 966938842 326 LPP 328
Cdd:cd04165  221 LPP 223
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 435-522 2.25e-42

Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 146.12  E-value: 2.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 435 TICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHaKDKLRTGEKAVVRFRFLKHPEYLKVGAKLLFREGVTK 514
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISID-KEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTK 79


                 ....*...
gi 966938842 515 GIGHVTDV 522
Cdd:cd03708   80 GIGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 343-429 4.25e-41

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 142.74  E-value: 4.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 343 TEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLR 422
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*..
gi 966938842 423 KGMVMVS 429
Cdd:cd03694   81 KGMVLVS 87
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 190-524 2.71e-26

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 113.08  E-value: 2.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 190 ITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVP-FFIVVSKIDLCAKTTVERTVRQLE 268
Cdd:COG3276   53 LGFVDVPGHEKFIKNMLAGAGGI--DLVLLVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADLVDEEWLELVEEEIR 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 269 RVLKQpgchkvpmlvTSEDDAvtaaqqfaqspnvtPIFTLSSVSGESLDLLKVFLnilppltnskeqEELMQQLTEFQ-- 346
Cdd:COG3276  131 ELLAG----------TFLEDA--------------PIVPVSAVTGEGIDELRAAL------------DALAAAVPARDad 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 347 ------VDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQ-RNRSACRVlRAGQAATLALGDFDRA 419
Cdd:COG3276  175 gpfrlpIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQvHGQPVEEA-YAGQRVALNLAGVEKE 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 420 LLRKGMVMVSPEmNPTICSVFEAEIVLLFHAT-TFRRGFQVTVHVGNVRQTAVVeKIHAKDKLRTGEKAVVRFRfLKHPE 498
Cdd:COG3276  250 EIERGDVLAAPG-ALRPTDRIDVRLRLLPSAPrPLKHWQRVHLHHGTAEVLARV-VLLDREELAPGEEALAQLR-LEEPL 326

                        330       340
                 ....*....|....*....|....*....
gi 966938842 499 YLKVGAKLLFREG---VTKGIGHVTDVQA 524
Cdd:COG3276  327 VAARGDRFILRDYsprRTIGGGRVLDPNP 355
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 183-328 1.05e-17

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 81.03  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842  183 CESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVER 262
Cdd:pfam00009  64 FETKDYLINLIDTPGHVDFVKEVIRGLAQ--ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEE 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966938842  263 TVRQLERVLkqpgchkvpmlvtseddavtaAQQFAQSPNVTPIFTLSSVSGESLD-LLKVFLNILPP 328
Cdd:pfam00009 142 VVEEVSREL---------------------LEKYGEDGEFVPVVPGSALKGEGVQtLLDALDEYLPS 187
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 188-424 6.26e-12

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 68.15  E-value: 6.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 188 KMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLG-LALALKVPFFIVVSKIDLCAKTTVERTVRQ 266
Cdd:PRK10512  51 RVLGFIDVPGHEKFLSNMLAGVGGI--DHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEVRRQ 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 267 LErvlkqpgchkvpmlvtseddAVTAAQQFAQSpnvtPIFTLSSVSGESLDLLKVFLNILPpltnskEQEELMQQLTEFQ 346
Cdd:PRK10512 129 VK--------------------AVLREYGFAEA----KLFVTAATEGRGIDALREHLLQLP------EREHAAQHRFRLA 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966938842 347 VDEIYTVPEVGTVVGGTLSSGICREGDQLVVgptdDGCFLELRVCSIQRNRSACRVLRAGQAATLAL-GDFDRALLRKG 424
Cdd:PRK10512 179 IDRAFTVKGAGLVVTGTALSGEVKVGDTLWL----TGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIaGDAEKEQINRG 253
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 357-428 2.73e-05

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 42.25  E-value: 2.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966938842  357 GTVVGGTLSSGICREGDQLVVGPTD-DGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLRKGMVMV 428
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
 
Name Accession Description Interval E-value
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 169-328 1.50e-81

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 253.75  E-value: 1.50e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 169 QVVNYSDSRTAE---EICESSSKMITFIDLAGHHKYLHTTIFGLTSYCPDCALLLVSANTGIAGTTREHLGLALALKVPF 245
Cdd:cd04165   62 EVVNYPDNHLGEldvEICEKSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPV 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 246 FIVVSKIDLCAKTTVERTVRQLERVLKQPGCHKVPMLVTSEDDAVTAAQQFaQSPNVTPIFTLSSVSGESLDLLKVFLNI 325
Cdd:cd04165  142 FVVVTKIDMTPANVLQETLKDLKRLLKSPGVRKLPVPVKSKDDVVLSASNL-SSGRVVPIFQVSNVTGEGLDLLRRFLNL 220


                 ...
gi 966938842 326 LPP 328
Cdd:cd04165  221 LPP 223
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 435-522 2.25e-42

Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in the cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 146.12  E-value: 2.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 435 TICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHaKDKLRTGEKAVVRFRFLKHPEYLKVGAKLLFREGVTK 514
Cdd:cd03708    1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISID-KEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTK 79


                 ....*...
gi 966938842 515 GIGHVTDV 522
Cdd:cd03708   80 GIGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 343-429 4.25e-41

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 142.74  E-value: 4.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 343 TEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLR 422
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*..
gi 966938842 423 KGMVMVS 429
Cdd:cd03694   81 KGMVLVS 87
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 190-524 2.71e-26

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 113.08  E-value: 2.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 190 ITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVP-FFIVVSKIDLCAKTTVERTVRQLE 268
Cdd:COG3276   53 LGFVDVPGHEKFIKNMLAGAGGI--DLVLLVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADLVDEEWLELVEEEIR 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 269 RVLKQpgchkvpmlvTSEDDAvtaaqqfaqspnvtPIFTLSSVSGESLDLLKVFLnilppltnskeqEELMQQLTEFQ-- 346
Cdd:COG3276  131 ELLAG----------TFLEDA--------------PIVPVSAVTGEGIDELRAAL------------DALAAAVPARDad 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 347 ------VDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQ-RNRSACRVlRAGQAATLALGDFDRA 419
Cdd:COG3276  175 gpfrlpIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQvHGQPVEEA-YAGQRVALNLAGVEKE 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 420 LLRKGMVMVSPEmNPTICSVFEAEIVLLFHAT-TFRRGFQVTVHVGNVRQTAVVeKIHAKDKLRTGEKAVVRFRfLKHPE 498
Cdd:COG3276  250 EIERGDVLAAPG-ALRPTDRIDVRLRLLPSAPrPLKHWQRVHLHHGTAEVLARV-VLLDREELAPGEEALAQLR-LEEPL 326

                        330       340
                 ....*....|....*....|....*....
gi 966938842 499 YLKVGAKLLFREG---VTKGIGHVTDVQA 524
Cdd:COG3276  327 VAARGDRFILRDYsprRTIGGGRVLDPNP 355
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 183-328 5.12e-24

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 98.91  E-value: 5.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 183 CESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVER 262
Cdd:cd00881   57 FEWPKRRINFIDTPGHEDFSKETVRGLAQ--ADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDE 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966938842 263 TVRQLERVLKQPGCHKVPmlvtseddavtaaqqfaqsPNVTPIFTLSSVSGES-LDLLKVFLNILPP 328
Cdd:cd00881  135 VLREIKELLKLIGFTFLK-------------------GKDVPIIPISALTGEGiEELLDAIVEHLPP 182
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 183-328 1.05e-17

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 81.03  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842  183 CESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVER 262
Cdd:pfam00009  64 FETKDYLINLIDTPGHVDFVKEVIRGLAQ--ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEE 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966938842  263 TVRQLERVLkqpgchkvpmlvtseddavtaAQQFAQSPNVTPIFTLSSVSGESLD-LLKVFLNILPP 328
Cdd:pfam00009 142 VVEEVSREL---------------------LEKYGEDGEFVPVVPGSALKGEGVQtLLDALDEYLPS 187
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 190-495 8.72e-17

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 82.67  E-value: 8.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 190 ITFIDLAGHHKYLHTTIFGlTSYCpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLC--AKTTVERTVRQ 266
Cdd:COG5256   87 FTIIDAPGHRDFVKNMITG-ASQA-DAAILVVSAKDGVMGQTREHAFLARTLGINQLIVaVNKMDAVnySEKRYEEVKEE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 267 LERVLKQPG--CHKVPMLVTSeddAVTAAQQFAQSPNvTPIF---TLSsvsgESLDLLKVflnilPPLTNSKEqeelmqq 341
Cdd:COG5256  165 VSKLLKMVGykVDKIPFIPVS---AWKGDNVVKKSDN-MPWYngpTLL----EALDNLKE-----PEKPVDKP------- 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 342 lTEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTddGCFLELRvcSIQRNRSACRVLRAGQAATLALGDFDRALL 421
Cdd:COG5256  225 -LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPA--GVVGEVK--SIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 422 RKGMVMVSPEMNPTICSVFEAEIVLLFHATTFRRGFQVTVHVGN----VRQTAVVEKIHAK---------DKLRTGEKAV 488
Cdd:COG5256  300 KRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTaqvaCTFVELVSKLDPRtgqvkeenpQFLKTGDAAI 379


                 ....*..
gi 966938842 489 VRFRFLK 495
Cdd:COG5256  380 VKIKPTK 386
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 186-328 7.10e-16

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 75.33  E-value: 7.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 186 SSKMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIVV-SKIDLCAKTTVERTV 264
Cdd:cd04171   48 DGKRLGFIDVPGHEKFVKNMLAGAGGI--DAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVlTKADLVDEDRLELVE 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966938842 265 RQLERVLKQPGCHKVpmlvtseddavtaaqqfaqspnvtPIFTLSSVSGESLDLLKVFLNILPP 328
Cdd:cd04171  126 EEILELLAGTFLADA------------------------PIFPVSSVTGEGIEELKNYLDELAE 165
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 188-424 6.26e-12

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 68.15  E-value: 6.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 188 KMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLG-LALALKVPFFIVVSKIDLCAKTTVERTVRQ 266
Cdd:PRK10512  51 RVLGFIDVPGHEKFLSNMLAGVGGI--DHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEVRRQ 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 267 LErvlkqpgchkvpmlvtseddAVTAAQQFAQSpnvtPIFTLSSVSGESLDLLKVFLNILPpltnskEQEELMQQLTEFQ 346
Cdd:PRK10512 129 VK--------------------AVLREYGFAEA----KLFVTAATEGRGIDALREHLLQLP------EREHAAQHRFRLA 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966938842 347 VDEIYTVPEVGTVVGGTLSSGICREGDQLVVgptdDGCFLELRVCSIQRNRSACRVLRAGQAATLAL-GDFDRALLRKG 424
Cdd:PRK10512 179 IDRAFTVKGAGLVVTGTALSGEVKVGDTLWL----TGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIaGDAEKEQINRG 253
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 347-426 1.82e-08

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 51.76  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 347 VDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLRKGMV 426
Cdd:cd03696    5 IDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG----KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
PLN03127 PLN03127
Elongation factor Tu; Provisional
 184-522 1.57e-07

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 53.68  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 184 ESSSKMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLCAKTT--- 259
Cdd:PLN03127 120 ETAKRHYAHVDCPGHADYVKNMITGAAQM--DGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEElle 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 260 -VERTVRQLERVLKQPGcHKVPMLVTSeddAVTAAQQFAQSPNVTPIftlssvsgesLDLLKVFLNILPPLTNSKEQEEL 338
Cdd:PLN03127 198 lVEMELRELLSFYKFPG-DEIPIIRGS---ALSALQGTNDEIGKNAI----------LKLMDAVDEYIPEPVRVLDKPFL 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 339 MqqltefQVDEIYTVPEVGTVVGGTLSSGICREGDQL-VVGPTDDGCfLELRVCSIQRNRsacRVLRAGQAAT---LALG 414
Cdd:PLN03127 264 M------PIEDVFSIQGRGTVATGRVEQGTIKVGEEVeIVGLRPGGP-LKTTVTGVEMFK---KILDQGQAGDnvgLLLR 333

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 415 DFDRALLRKGMVMVSPEMNPTIcSVFEAEIVLLfhatTFRRGFQVTVHVGNVR-----QTAvveKIHAKDKLRTGEKAV- 488
Cdd:PLN03127 334 GLKREDVQRGQVICKPGSIKTY-KKFEAEIYVL----TKDEGGRHTPFFSNYRpqfylRTA---DVTGKVELPEGVKMVm 405

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 966938842 489 ----VRFRF-LKHPEYLKVGAKLLFRE-GVTKGIGHVTDV 522
Cdd:PLN03127 406 pgdnVTAVFeLISPVPLEPGQRFALREgGRTVGAGVVSKV 445
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 190-273 3.73e-07

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 50.44  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 190 ITFIDLAGHHKYLHTTIFGltSYCPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERTVRQLER 269
Cdd:cd01889   70 ITLVDCPGHASLIRTIIGG--AQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKK 147


                 ....
gi 966938842 270 VLKQ 273
Cdd:cd01889  148 RLQK 151
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 184-503 5.86e-07

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 52.01  E-value: 5.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 184 ESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTG-------IAGTTREHLGLALALKVPFFIVV-SKIDlc 255
Cdd:PLN00043  81 ETTKYYCTVIDAPGHRDFIKNMITGTSQ--ADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQMICCcNKMD-- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 256 aKTTVERTVRQLERVLKQpgchkvpmlvtseddAVTAAQQFAQSPNVTPIFTLSSVSGESLDLLKVFLN------ILPPL 329
Cdd:PLN00043 157 -ATTPKYSKARYDEIVKE---------------VSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDwykgptLLEAL 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 330 TNSKEQEELMQQLTEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQRNRSACRVLRAGQAA 409
Cdd:PLN00043 221 DQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTG----LTTEVKSVEMHHESLQEALPGDNV 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 410 TLALGDFDRALLRKGMVMVSPEMNPTICSV-FEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHAKDKLRTGEKav 488
Cdd:PLN00043 297 GFNVKNVAVKDLKRGYVASNSKDDPAKEAAnFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKE-- 374

                        330
                 ....*....|....*
gi 966938842 489 vrfrFLKHPEYLKVG 503
Cdd:PLN00043 375 ----LEKEPKFLKNG 385
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 184-267 2.14e-06

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 47.85  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 184 ESSSKMITFIDLAGHHKYLHTTIFG--LTsycpDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTT-- 259
Cdd:cd01887   45 DVKIPGITFIDTPGHEAFTNMRARGasVT----DIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEad 120


                 ....*...
gi 966938842 260 VERTVRQL 267
Cdd:cd01887  121 PERVKNEL 128
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 357-428 2.73e-05

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 42.25  E-value: 2.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966938842  357 GTVVGGTLSSGICREGDQLVVGPTD-DGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLRKGMVMV 428
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 190-267 3.53e-05

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 45.66  E-value: 3.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966938842 190 ITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLcAKTTVERTVRQL 267
Cdd:cd04170   66 INLIDTPGYADFVGETLSALRA--VDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR-ARADFDKTLAAL 140
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 345-426 9.44e-05

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 41.10  E-value: 9.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 345 FQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGcfleLRVCSIQRNRSACRVLRAGQAATLA-LGDFDralLRK 423
Cdd:cd01342    3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGIT----GRVTSIERFHEEVDEAKAGDIVGIGiLGVKD---ILT 75


                 ...
gi 966938842 424 GMV 426
Cdd:cd01342   76 GDT 78
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 184-254 1.35e-04

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 43.25  E-value: 1.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966938842 184 ESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTG-------IAGTTREHLGLALALKVPFFIV-VSKIDL 254
Cdd:cd01883   73 ETEKYRFTIIDAPGHRDFVKNMITGASQ--ADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVaVNKMDD 149
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 193-267 4.80e-04

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 41.42  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 193 IDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLCAKTT----VERTVRQL 267
Cdd:cd01884   70 VDCPGHADYIKNMITGAAQM--DGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMVDDEEllelVEMEVREL 147
infB CHL00189
translation initiation factor 2; Provisional
 185-267 5.49e-04

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 42.90  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 185 SSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLcAKTTVERTV 264
Cdd:CHL00189 292 DENQKIVFLDTPGHEAFSSMRSRGANV--TDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDK-ANANTERIK 368


                 ...
gi 966938842 265 RQL 267
Cdd:CHL00189 369 QQL 371
tufA CHL00071
elongation factor Tu
 193-373 1.38e-03

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 41.10  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 193 IDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLCAKTT----VERTVRQL 267
Cdd:CHL00071  80 VDCPGHADYVKNMITGAAQM--DGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVDDEEllelVELEVREL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 268 ERVLKQPGcHKVPMLVTSeddAVTAAQQFAQSPNVTP--------IFTLSsvsgESLDllkvflNILPPLTNSKEQEELM 339
Cdd:CHL00071 158 LSKYDFPG-DDIPIVSGS---ALLALEALTENPKIKRgenkwvdkIYNLM----DAVD------SYIPTPERDTDKPFLM 223

                        170       180       190
                 ....*....|....*....|....*....|....
gi 966938842 340 qqltefQVDEIYTVPEVGTVVGGTLSSGICREGD 373
Cdd:CHL00071 224 ------AIEDVFSITGRGTVATGRIERGTVKVGD 251
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 436-522 4.55e-03

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 37.14  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 436 ICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHAKDKLRTGEK-------------AVVRFRFLK------H 496
Cdd:cd04093    4 TTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVikkkprclgknqsAVVEIELERpipletF 83

                         90       100
                 ....*....|....*....|....*.
gi 966938842 497 PEYLKVGAKLLFREGVTKGIGHVTDV 522
Cdd:cd04093   84 KDNKELGRFVLRRGGETIAAGIVTEI 109
era PRK00089
GTPase Era; Reviewed
 215-328 9.09e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 38.10  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966938842 215 DCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLcakttvertVRQLERVLKQpgchkvpmlvtseddavtaAQ 294
Cdd:PRK00089  86 DLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL---------VKDKEELLPL-------------------LE 137

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 966938842 295 QFAQSPNVTPIFTLSSVSGESLD-LLKVFLNILPP 328
Cdd:PRK00089 138 ELSELMDFAEIVPISALKGDNVDeLLDVIAKYLPE 172
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 193-254 9.14e-03

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 37.55  E-value: 9.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966938842 193 IDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDL 254
Cdd:cd04166   83 ADTPGHEQYTRNMVTGAST--ADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaVNKMDL 143
 
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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