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Conserved domains on  [gi|1370508239|ref|XP_024302245|]
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GTP-binding protein 2 isoform X3 [Homo sapiens]

Protein Classification

GTPBP1_like and GTPBP_III domain-containing protein( domain architecture ID 10135033)

protein containing domains GTPBP1_like, GTPBP_II, and GTPBP_III

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 86-306 4.02e-131

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: 379.71  E-value: 4.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  86 RVAVLGNVDSGKSTLLGVLTQGELDNGRGRARLNLFRHLHEIQSGRTSSISFEILGFNSKGEVVNYSDSRTAE---EICE 162
Cdd:cd04165     1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGEldvEICE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 163 SSSKMITFIDLAGHHKYLHTTIFGLTSYCPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERTV 242
Cdd:cd04165    81 KSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQETL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508239 243 RQLERVLKQPGCHKVPMLVTSEDDAVTAAQQFaQSPNVTPIFTLSSVSGESLDLLKVFLNILPP 306
Cdd:cd04165   161 KDLKRLLKSPGVRKLPVPVKSKDDVVLSASNL-SSGRVVPIFQVSNVTGEGLDLLRRFLNLLPP 223
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 413-500 3.77e-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: 145.35  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 413 TICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHaKDKLRTGEKAVVRFRFLKHPEYLKVGAKLLFREGVTK 492
Cdd:cd03708     1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISID-KEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTK 79


                  ....*...
gi 1370508239 493 GIGHVTDV 500
Cdd:cd03708    80 GIGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 321-407 8.77e-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: 141.59  E-value: 8.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 321 TEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLR 400
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                  ....*..
gi 1370508239 401 KGMVMVS 407
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 ...
 86-306 4.02e-131

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: 379.71  E-value: 4.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  86 RVAVLGNVDSGKSTLLGVLTQGELDNGRGRARLNLFRHLHEIQSGRTSSISFEILGFNSKGEVVNYSDSRTAE---EICE 162
Cdd:cd04165     1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGEldvEICE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 163 SSSKMITFIDLAGHHKYLHTTIFGLTSYCPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERTV 242
Cdd:cd04165    81 KSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQETL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508239 243 RQLERVLKQPGCHKVPMLVTSEDDAVTAAQQFaQSPNVTPIFTLSSVSGESLDLLKVFLNILPP 306
Cdd:cd04165   161 KDLKRLLKSPGVRKLPVPVKSKDDVVLSASNL-SSGRVVPIFQVSNVTGEGLDLLRRFLNLLPP 223
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 413-500 3.77e-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: 145.35  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 413 TICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHaKDKLRTGEKAVVRFRFLKHPEYLKVGAKLLFREGVTK 492
Cdd:cd03708     1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISID-KEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTK 79


                  ....*...
gi 1370508239 493 GIGHVTDV 500
Cdd:cd03708    80 GIGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 321-407 8.77e-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: 141.59  E-value: 8.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 321 TEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLR 400
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                  ....*..
gi 1370508239 401 KGMVMVS 407
Cdd:cd03694    81 KGMVLVS 87
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 168-502 9.75e-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: 111.16  E-value: 9.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 168 ITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVP-FFIVVSKIDLCAKTTVERTVRQLE 246
Cdd:COG3276    53 LGFVDVPGHEKFIKNMLAGAGGI--DLVLLVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADLVDEEWLELVEEEIR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 247 RVLKQpgchkvpmlvTSEDDAvtaaqqfaqspnvtPIFTLSSVSGESLDLLKVFLnilppltnskeqEELMQQLTEFQ-- 324
Cdd:COG3276   131 ELLAG----------TFLEDA--------------PIVPVSAVTGEGIDELRAAL------------DALAAAVPARDad 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 325 ------VDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQ-RNRSACRVlRAGQAATLALGDFDRA 397
Cdd:COG3276   175 gpfrlpIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQvHGQPVEEA-YAGQRVALNLAGVEKE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 398 LLRKGMVMVSPEmNPTICSVFEAEIVLLFHAT-TFRRGFQVTVHVGNVRQTAVVeKIHAKDKLRTGEKAVVRFRfLKHPE 476
Cdd:COG3276   250 EIERGDVLAAPG-ALRPTDRIDVRLRLLPSAPrPLKHWQRVHLHHGTAEVLARV-VLLDREELAPGEEALAQLR-LEEPL 326

                         330       340
                  ....*....|....*....|....*....
gi 1370508239 477 YLKVGAKLLFREG---VTKGIGHVTDVQA 502
Cdd:COG3276   327 VAARGDRFILRDYsprRTIGGGRVLDPNP 355
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 87-306 3.72e-23

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: 96.44  E-value: 3.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTQ--GELDNGRGRA---RLNLFRHLHEIQSGRTSSISfeilgfnskgevvnysdsrTAEeiC 161
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLYytGAISKRGEVKgegEAGLDNLPEERERGITIKSA-------------------AVS--F 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 162 ESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERT 241
Cdd:pfam00009  65 ETKDYLINLIDTPGHVDFVKEVIRGLAQ--ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEEV 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508239 242 VRQLERVLkqpgchkvpmlvtseddavtaAQQFAQSPNVTPIFTLSSVSGESLD-LLKVFLNILPP 306
Cdd:pfam00009 143 VEEVSREL---------------------LEKYGEDGEFVPVVPGSALKGEGVQtLLDALDEYLPS 187
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 87-402 6.43e-12

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 67.77  E-value: 6.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTqgeldnGRGRARLNlfrhlHEIQSGRTSSisfeiLGFNskgevvnY---SDSRtaeeices 163
Cdd:PRK10512    3 IATAGHVDHGKTTLLQAIT------GVNADRLP-----EEKKRGMTID-----LGYA-------YwpqPDGR-------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 164 sskMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLG-LALALKVPFFIVVSKIDLCAKTTVERTV 242
Cdd:PRK10512   52 ---VLGFIDVPGHEKFLSNMLAGVGGI--DHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEVR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 243 RQLErvlkqpgchkvpmlvtseddAVTAAQQFAQSpnvtPIFTLSSVSGESLDLLKVFLNILPpltnskEQEELMQQLTE 322
Cdd:PRK10512  127 RQVK--------------------AVLREYGFAEA----KLFVTAATEGRGIDALREHLLQLP------EREHAAQHRFR 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 323 FQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVgptdDGCFLELRVCSIQRNRSACRVLRAGQAATLAL-GDFDRALLRK 401
Cdd:PRK10512  177 LAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWL----TGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIaGDAEKEQINR 252


                  .
gi 1370508239 402 G 402
Cdd:PRK10512  253 G 253
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 335-406 4.10e-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: 41.87  E-value: 4.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508239 335 GTVVGGTLSSGICREGDQLVVGPTD-DGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLRKGMVMV 406
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 ...
 86-306 4.02e-131

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: 379.71  E-value: 4.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  86 RVAVLGNVDSGKSTLLGVLTQGELDNGRGRARLNLFRHLHEIQSGRTSSISFEILGFNSKGEVVNYSDSRTAE---EICE 162
Cdd:cd04165     1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLNLFRHKHEVESGRTSSVSNDILGFDSDGEVVNYPDNHLGEldvEICE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 163 SSSKMITFIDLAGHHKYLHTTIFGLTSYCPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERTV 242
Cdd:cd04165    81 KSSKVVTFIDLAGHERYLKTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQETL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508239 243 RQLERVLKQPGCHKVPMLVTSEDDAVTAAQQFaQSPNVTPIFTLSSVSGESLDLLKVFLNILPP 306
Cdd:cd04165   161 KDLKRLLKSPGVRKLPVPVKSKDDVVLSASNL-SSGRVVPIFQVSNVTGEGLDLLRRFLNLLPP 223
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 413-500 3.77e-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: 145.35  E-value: 3.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 413 TICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHaKDKLRTGEKAVVRFRFLKHPEYLKVGAKLLFREGVTK 492
Cdd:cd03708     1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISID-KEVLRTGDRALVRFRFLYRPEYLREGQRLIFREGRTK 79


                  ....*...
gi 1370508239 493 GIGHVTDV 500
Cdd:cd03708    80 GIGTVTKV 87
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 321-407 8.77e-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: 141.59  E-value: 8.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 321 TEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLR 400
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                  ....*..
gi 1370508239 401 KGMVMVS 407
Cdd:cd03694    81 KGMVLVS 87
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 86-306 4.50e-36

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: 132.42  E-value: 4.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  86 RVAVLGNVDSGKSTLLGVLTQGELDNGRGRARLNLF--RHLHEIQSGRTSSISFEILGFNSKgevvnysdsrtaeeices 163
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFldTLKEERERGITIKTGVVEFEWPKR------------------ 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 164 sskMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERTVR 243
Cdd:cd00881    63 ---RINFIDTPGHEDFSKETVRGLAQ--ADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLR 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508239 244 QLERVLKQPGCHKVPmlvtseddavtaaqqfaqsPNVTPIFTLSSVSGES-LDLLKVFLNILPP 306
Cdd:cd00881   138 EIKELLKLIGFTFLK-------------------GKDVPIIPISALTGEGiEELLDAIVEHLPP 182
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 168-502 9.75e-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: 111.16  E-value: 9.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 168 ITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVP-FFIVVSKIDLCAKTTVERTVRQLE 246
Cdd:COG3276    53 LGFVDVPGHEKFIKNMLAGAGGI--DLVLLVVAADEGVMPQTREHLAILDLLGIKrGIVVLTKADLVDEEWLELVEEEIR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 247 RVLKQpgchkvpmlvTSEDDAvtaaqqfaqspnvtPIFTLSSVSGESLDLLKVFLnilppltnskeqEELMQQLTEFQ-- 324
Cdd:COG3276   131 ELLAG----------TFLEDA--------------PIVPVSAVTGEGIDELRAAL------------DALAAAVPARDad 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 325 ------VDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQ-RNRSACRVlRAGQAATLALGDFDRA 397
Cdd:COG3276   175 gpfrlpIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG----KPVRVRGIQvHGQPVEEA-YAGQRVALNLAGVEKE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 398 LLRKGMVMVSPEmNPTICSVFEAEIVLLFHAT-TFRRGFQVTVHVGNVRQTAVVeKIHAKDKLRTGEKAVVRFRfLKHPE 476
Cdd:COG3276   250 EIERGDVLAAPG-ALRPTDRIDVRLRLLPSAPrPLKHWQRVHLHHGTAEVLARV-VLLDREELAPGEEALAQLR-LEEPL 326

                         330       340
                  ....*....|....*....|....*....
gi 1370508239 477 YLKVGAKLLFREG---VTKGIGHVTDVQA 502
Cdd:COG3276   327 VAARGDRFILRDYsprRTIGGGRVLDPNP 355
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 87-306 3.72e-23

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: 96.44  E-value: 3.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTQ--GELDNGRGRA---RLNLFRHLHEIQSGRTSSISfeilgfnskgevvnysdsrTAEeiC 161
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLYytGAISKRGEVKgegEAGLDNLPEERERGITIKSA-------------------AVS--F 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 162 ESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERT 241
Cdd:pfam00009  65 ETKDYLINLIDTPGHVDFVKEVIRGLAQ--ADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDGAELEEV 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508239 242 VRQLERVLkqpgchkvpmlvtseddavtaAQQFAQSPNVTPIFTLSSVSGESLD-LLKVFLNILPP 306
Cdd:pfam00009 143 VEEVSREL---------------------LEKYGEDGEFVPVVPGSALKGEGVQtLLDALDEYLPS 187
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 85-473 1.22e-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: 84.98  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  85 LRVAVLGNVDSGKSTL-------LGVLTQGELDNGR------GRARLN----LFRHLHEIQSGRTSSISFEilGFNSKge 147
Cdd:COG5256     8 LNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEeeaekkGKESFKfawvMDRLKEERERGVTIDLAHK--KFETD-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 148 vvNYsdsrtaeeicessskMITFIDLAGHHKYLHTTIFGlTSYCpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV- 226
Cdd:COG5256    84 --KY---------------YFTIIDAPGHRDFVKNMITG-ASQA-DAAILVVSAKDGVMGQTREHAFLARTLGINQLIVa 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 227 VSKIDLC--AKTTVERTVRQLERVLKQPG--CHKVPMLVTSeddAVTAAQQFAQSPNvTPIF---TLSsvsgESLDLLKV 299
Cdd:COG5256   145 VNKMDAVnySEKRYEEVKEEVSKLLKMVGykVDKIPFIPVS---AWKGDNVVKKSDN-MPWYngpTLL----EALDNLKE 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 300 flnilPPLTNSKEqeelmqqlTEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTddGCFLELRvcSIQRNRSACR 379
Cdd:COG5256   217 -----PEKPVDKP--------LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPA--GVVGEVK--SIEMHHEELE 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 380 VLRAGQAATLALGDFDRALLRKGMVMVSPEMNPTICSVFEAEIVLLFHATTFRRGFQVTVHVGN----VRQTAVVEKIHA 455
Cdd:COG5256   280 QAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTaqvaCTFVELVSKLDP 359

                         410       420
                  ....*....|....*....|....*..
gi 1370508239 456 K---------DKLRTGEKAVVRFRFLK 473
Cdd:COG5256   360 RtgqvkeenpQFLKTGDAAIVKIKPTK 386
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 91-306 1.38e-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: 77.26  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  91 GNVDSGKSTLLGVLTQGELDngrgrarlnlfrHLHEIQSgRTSSISfeiLGFNskgevvnYSDSRtaeeicesSSKMITF 170
Cdd:cd04171     6 GHIDHGKTTLIKALTGIETD------------RLPEEKK-RGITID---LGFA-------YLDLP--------DGKRLGF 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 171 IDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIVV-SKIDLCAKTTVERTVRQLERVL 249
Cdd:cd04171    55 IDVPGHEKFVKNMLAGAGGI--DAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVlTKADLVDEDRLELVEEEILELL 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508239 250 KQPGCHKVpmlvtseddavtaaqqfaqspnvtPIFTLSSVSGESLDLLKVFLNILPP 306
Cdd:cd04171   133 AGTFLADA------------------------PIFPVSSVTGEGIEELKNYLDELAE 165
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 87-402 6.43e-12

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 67.77  E-value: 6.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTqgeldnGRGRARLNlfrhlHEIQSGRTSSisfeiLGFNskgevvnY---SDSRtaeeices 163
Cdd:PRK10512    3 IATAGHVDHGKTTLLQAIT------GVNADRLP-----EEKKRGMTID-----LGYA-------YwpqPDGR-------- 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 164 sskMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLG-LALALKVPFFIVVSKIDLCAKTTVERTV 242
Cdd:PRK10512   52 ---VLGFIDVPGHEKFLSNMLAGVGGI--DHALLVVACDDGVMAQTREHLAiLQLTGNPMLTVALTKADRVDEARIAEVR 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 243 RQLErvlkqpgchkvpmlvtseddAVTAAQQFAQSpnvtPIFTLSSVSGESLDLLKVFLNILPpltnskEQEELMQQLTE 322
Cdd:PRK10512  127 RQVK--------------------AVLREYGFAEA----KLFVTAATEGRGIDALREHLLQLP------EREHAAQHRFR 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 323 FQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVgptdDGCFLELRVCSIQRNRSACRVLRAGQAATLAL-GDFDRALLRK 401
Cdd:PRK10512  177 LAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWL----TGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIaGDAEKEQINR 252


                  .
gi 1370508239 402 G 402
Cdd:PRK10512  253 G 253
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 87-251 2.33e-09

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: 56.99  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTQ----GELDngrgrarlnlfRHLHEIQSGRTSSisfeiLGFNSKgeVVNYSDSRTAEEICE 162
Cdd:cd01889     3 VGLLGHVDSGKTSLAKALSEiastAAFD-----------KNPQSQERGITLD-----LGFSSF--EVDKPKHLEDNENPQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 163 SSSKMITFIDLAGHHKYLHTTIFGltSYCPDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTTVERTV 242
Cdd:cd01889    65 IENYQITLVDCPGHASLIRTIIGG--AQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKI 142


                  ....*....
gi 1370508239 243 RQLERVLKQ 251
Cdd:cd01889   143 EKMKKRLQK 151
PLN03127 PLN03127
Elongation factor Tu; Provisional
 85-500 4.66e-09

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 58.68  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  85 LRVAVLGNVDSGKSTLLGVLTqgeldngrgrarlnlfRHLHEIqsGRTSSISFEILGF----NSKGEVVNysdsrTAEEI 160
Cdd:PLN03127   62 VNVGTIGHVDHGKTTLTAAIT----------------KVLAEE--GKAKAVAFDEIDKapeeKARGITIA-----TAHVE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 161 CESSSKMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLCAKTT-- 237
Cdd:PLN03127  119 YETAKRHYAHVDCPGHADYVKNMITGAAQM--DGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVfLNKVDVVDDEEll 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 238 --VERTVRQLERVLKQPGcHKVPMLVTSeddAVTAAQQFAQSPNVTPIftlssvsgesLDLLKVFLNILPPLTNSKEQEE 315
Cdd:PLN03127  197 elVEMELRELLSFYKFPG-DEIPIIRGS---ALSALQGTNDEIGKNAI----------LKLMDAVDEYIPEPVRVLDKPF 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 316 LMqqltefQVDEIYTVPEVGTVVGGTLSSGICREGDQL-VVGPTDDGCfLELRVCSIQRNRsacRVLRAGQAAT---LAL 391
Cdd:PLN03127  263 LM------PIEDVFSIQGRGTVATGRVEQGTIKVGEEVeIVGLRPGGP-LKTTVTGVEMFK---KILDQGQAGDnvgLLL 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 392 GDFDRALLRKGMVMVSPEMNPTIcSVFEAEIVLLfhatTFRRGFQVTVHVGNVR-----QTAvveKIHAKDKLRTGEKAV 466
Cdd:PLN03127  333 RGLKREDVQRGQVICKPGSIKTY-KKFEAEIYVL----TKDEGGRHTPFFSNYRpqfylRTA---DVTGKVELPEGVKMV 404

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1370508239 467 -----VRFRF-LKHPEYLKVGAKLLFRE-GVTKGIGHVTDV 500
Cdd:PLN03127  405 mpgdnVTAVFeLISPVPLEPGQRFALREgGRTVGAGVVSKV 445
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 85-481 6.75e-09

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 58.18  E-value: 6.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  85 LRVAVLGNVDSGKSTLLGVLTQ--GELDN------GRGRARLNL--FRH---LHEIQSGRTSSISFEILGFnsKGEVVNY 151
Cdd:PLN00043    8 INIVVIGHVDSGKSTTTGHLIYklGGIDKrvierfEKEAAEMNKrsFKYawvLDKLKAERERGITIDIALW--KFETTKY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 152 sdsrtaeeicessskMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTG-------IAGTTREHLGLALALKVPFF 224
Cdd:PLN00043   86 ---------------YCTVIDAPGHRDFIKNMITGTSQ--ADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQM 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 225 IVV-SKIDlcaKTTVERTVRQLERVLKQpgchkvpmlvtseddAVTAAQQFAQSPNVTPIFTLSSVSGESLDLLKVFLN- 302
Cdd:PLN00043  149 ICCcNKMD---ATTPKYSKARYDEIVKE---------------VSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDw 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 303 -----ILPPLTNSKEQEELMQQLTEFQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQRNRSA 377
Cdd:PLN00043  211 ykgptLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTG----LTTEVKSVEMHHES 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 378 CRVLRAGQAATLALGDFDRALLRKGMVMVSPEMNPTICSV-FEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHAK 456
Cdd:PLN00043  287 LQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAAnFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTK 366

                         410       420
                  ....*....|....*....|....*
gi 1370508239 457 DKLRTGEKavvrfrFLKHPEYLKVG 481
Cdd:PLN00043  367 IDRRSGKE------LEKEPKFLKNG 385
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 325-404 2.86e-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: 50.99  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 325 VDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDdgcfLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLRKGMV 404
Cdd:cd03696     5 IDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG----KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 87-245 9.79e-07

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: 49.01  E-value: 9.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTqgELDNGRGRARlnlfrhlheiqsGRTSSI-SFEIlgfnskgevvnysdsrtaeEIcESSS 165
Cdd:cd01887     3 VTVMGHVDHGKTTLLDKIR--KTNVAAGEAG------------GITQHIgAYQV-------------------PI-DVKI 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 166 KMITFIDLAGHHKYLHTTIFG--LTsycpDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLCAKTT--VERT 241
Cdd:cd01887    49 PGITFIDTPGHEAFTNMRARGasVT----DIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEadPERV 124


                  ....
gi 1370508239 242 VRQL 245
Cdd:cd01887   125 KNEL 128
infB CHL00189
translation initiation factor 2; Provisional
 55-245 1.80e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 50.60  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  55 EREVDYDSDMPRKITEVLVRKVPdnqqfldlRVAVLGNVDSGKSTLLGVLTQGELDNgrgrarlnlfrhlHEIqSGRTSS 134
Cdd:CHL00189  223 INEKTSNLDNTSAFTENSINRPP--------IVTILGHVDHGKTTLLDKIRKTQIAQ-------------KEA-GGITQK 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 135 I-SFEilgfnskgevVNYsdsrtaeeICESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHL 213
Cdd:CHL00189  281 IgAYE----------VEF--------EYKDENQKIVFLDTPGHEAFSSMRSRGANV--TDIAILIIAADDGVKPQTIEAI 340

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370508239 214 GLALALKVPFFIVVSKIDLcAKTTVERTVRQL 245
Cdd:CHL00189  341 NYIQAANVPIIVAINKIDK-ANANTERIKQQL 371
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 87-252 4.33e-06

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: 48.36  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLL-------GVLT-QGELDNGrgrarlNLFRHLHEIQSGRTSSISFEILGFNSKGevvnysdsrtae 158
Cdd:cd04170     2 IALVGHSGSGKTTLAeallyatGAIDrLGRVEDG------NTVSDYDPEEKKRKMSIETSVAPLEWNG------------ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 159 eicesssKMITFIDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLcAKTTV 238
Cdd:cd04170    64 -------HKINLIDTPGYADFVGETLSALRAV--DAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR-ARADF 133

                         170
                  ....*....|....
gi 1370508239 239 ERTVRQLERVLKQP 252
Cdd:cd04170   134 DKTLAALREAFGRP 147
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 87-232 1.16e-05

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: 46.33  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLLGVLTQ--GELDNgrgrarlnlfRHLHEI-----QSGRTSsisFEilgfnskgevvnYS---DSRT 156
Cdd:cd01883     2 LVVIGHVDAGKSTLTGHLLYklGGVDK----------RTIEKYekeakEMGKES---FK------------YAwvlDKLK 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 157 AE-------EIC----ESSSKMITFIDLAGHHKYLHTTIFGLTSycPDCALLLVSANTG-------IAGTTREHLGLALA 218
Cdd:cd01883    57 EErergvtiDVGlakfETEKYRFTIIDAPGHRDFVKNMITGASQ--ADVAVLVVSARKGefeagfeKGGQTREHALLART 134

                         170
                  ....*....|....*
gi 1370508239 219 LKVPFFIV-VSKIDL 232
Cdd:cd01883   135 LGVKQLIVaVNKMDD 149
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 335-406 4.10e-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: 41.87  E-value: 4.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508239 335 GTVVGGTLSSGICREGDQLVVGPTD-DGCFLELRVCSIQRNRSACRVLRAGQAATLALGDFDRALLRKGMVMV 406
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 323-404 1.45e-04

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: 40.33  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 323 FQVDEIYTVPEVGTVVGGTLSSGICREGDQLVVGPTDDGcfleLRVCSIQRNRSACRVLRAGQAATLA-LGDFDralLRK 401
Cdd:cd01342     3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGIT----GRVTSIERFHEEVDEAKAGDIVGIGiLGVKD---ILT 75


                  ...
gi 1370508239 402 GMV 404
Cdd:cd01342    76 GDT 78
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 171-245 4.35e-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: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 171 IDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLCAKTT----VERTVRQL 245
Cdd:cd01884    70 VDCPGHADYIKNMITGAAQM--DGAILVVSATDGPMPQTREHLLLARQVGVPYIVVfLNKADMVDDEEllelVEMEVREL 147
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 86-232 5.39e-04

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: 41.40  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  86 RVAVLGNVDSGKSTLLGVL---TQGELDNgrgrarlnlfrHLHEIQSGRTSsisfeilgfNSKGEVVNYS---DSRTAEE 159
Cdd:cd04166     1 RFITCGSVDDGKSTLIGRLlydSKSIFED-----------QLAALERSKSS---------GTQGEKLDLAllvDGLQAER 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 160 ----------ICESSSKMiTFI--DLAGHHKYLHTTIFGLTSycPDCALLLVSANTGIAGTTREHLGLALALKVPFFIV- 226
Cdd:cd04166    61 eqgitidvayRYFSTPKR-KFIiaDTPGHEQYTRNMVTGAST--ADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVa 137


                  ....*.
gi 1370508239 227 VSKIDL 232
Cdd:cd04166   138 VNKMDL 143
tufA CHL00071
elongation factor Tu
 171-351 1.36e-03

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 41.10  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 171 IDLAGHHKYLHTTIFGLTSYcpDCALLLVSANTGIAGTTREHLGLALALKVPFFIV-VSKIDLCAKTT----VERTVRQL 245
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQM--DGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVfLNKEDQVDDEEllelVELEVREL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 246 ERVLKQPGcHKVPMLVTSeddAVTAAQQFAQSPNVTP--------IFTLSsvsgESLDllkvflNILPPLTNSKEQEELM 317
Cdd:CHL00071  158 LSKYDFPG-DDIPIVSGS---ALLALEALTENPKIKRgenkwvdkIYNLM----DAVD------SYIPTPERDTDKPFLM 223

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370508239 318 qqltefQVDEIYTVPEVGTVVGGTLSSGICREGD 351
Cdd:CHL00071  224 ------AIEDVFSITGRGTVATGRIERGTVKVGD 251
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 414-500 5.17e-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: 36.75  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 414 ICSVFEAEIVLLFHATTFRRGFQVTVHVGNVRQTAVVEKIHAKDKLRTGEK-------------AVVRFRFLK------H 474
Cdd:cd04093     4 TTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVikkkprclgknqsAVVEIELERpipletF 83

                          90       100
                  ....*....|....*....|....*.
gi 1370508239 475 PEYLKVGAKLLFREGVTKGIGHVTDV 500
Cdd:cd04093    84 KDNKELGRFVLRRGGETIAAGIVTEI 109
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 87-232 5.99e-03

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 38.02  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239  87 VAVLGNVDSGKSTLL----GVLTQgeldngrgrarlnlfRHLHEIQSGRTSSISFEILGFNSKGEVVNYSDSRTAEEICE 162
Cdd:cd01888     3 IGTIGHVAHGKTTLVkalsGVWTV---------------RHKEELKRNITIKLGYANAKIYKCPNCGCPRPYDTPECECP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 163 SS-SKM-----ITFIDLAGHHKYLHTTIFGltSYCPDCALLLVSANTGIAGT-TREHLglaLALKV----PFFIVVSKID 231
Cdd:cd01888    68 GCgGETklvrhVSFVDCPGHEILMATMLSG--AAVMDGALLLIAANEPCPQPqTSEHL---AALEImglkHIIILQNKID 142


                  .
gi 1370508239 232 L 232
Cdd:cd01888   143 L 143
era PRK00089
GTPase Era; Reviewed
 193-306 9.92e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 38.10  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508239 193 DCALLLVSANTGIAGTTREHLGLALALKVPFFIVVSKIDLcakttvertVRQLERVLKQpgchkvpmlvtseddavtaAQ 272
Cdd:PRK00089   86 DLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDL---------VKDKEELLPL-------------------LE 137

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1370508239 273 QFAQSPNVTPIFTLSSVSGESLD-LLKVFLNILPP 306
Cdd:PRK00089  138 ELSELMDFAEIVPISALKGDNVDeLLDVIAKYLPE 172
 
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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