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Conserved domains on  [gi|2172335821|gb|UHY15438|]
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translation elongation factor EF-1 alpha, partial [Physarum alpinum]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-241 8.86e-177

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 PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 493.11  E-value: 8.86e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDEKSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PTZ00141  137 ALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:PTZ00141  217 LEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNV 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNVPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:PTZ00141  297 GFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLE 376


                  .
gi 2172335821 241 E 241
Cdd:PTZ00141  377 E 377
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-241 8.86e-177

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 493.11  E-value: 8.86e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDEKSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PTZ00141  137 ALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:PTZ00141  217 LEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNV 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNVPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:PTZ00141  297 GFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLE 376


                  .
gi 2172335821 241 E 241
Cdd:PTZ00141  377 E 377
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-241 7.83e-131

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: 375.81  E-value: 7.83e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:COG5256   130 AFLARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:COG5256   208 LEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNI 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNvPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:COG5256   288 GFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKE 366


                  .
gi 2172335821 241 E 241
Cdd:COG5256   367 E 367
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-241 8.18e-127

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 365.72  E-value: 8.18e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:TIGR00483 133 AFLARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTL 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:TIGR00483 211 LEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNI 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNvPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:TIGR00483 291 GFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLE 369


                  .
gi 2172335821 241 E 241
Cdd:TIGR00483 370 E 370
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 94-183 4.08e-60

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 184.31  E-value: 4.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  94 TDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIR 173
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|
gi 2172335821 174 RGMVAGDSKN 183
Cdd:cd03693    81 RGDVAGDSKN 90
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 112-177 2.00e-15

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: 68.83  E-value: 2.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2172335821 112 GTVPVGRVETGILKPGMVVTFAPA-----NLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-241 8.86e-177

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 493.11  E-value: 8.86e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDEKSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PTZ00141  137 ALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:PTZ00141  217 LEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNV 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNVPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:PTZ00141  297 GFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLE 376


                  .
gi 2172335821 241 E 241
Cdd:PTZ00141  377 E 377
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-241 7.83e-131

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: 375.81  E-value: 7.83e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:COG5256   130 AFLARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:COG5256   208 LEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNI 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNvPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:COG5256   288 GFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKE 366


                  .
gi 2172335821 241 E 241
Cdd:COG5256   367 E 367
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-241 2.69e-130

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 375.20  E-value: 2.69e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDEKSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PLN00043  137 ALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:PLN00043  217 LEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNV 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNVPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:PLN00043  297 GFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELE 376


                  .
gi 2172335821 241 E 241
Cdd:PLN00043  377 K 377
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-241 4.05e-129

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 371.57  E-value: 4.05e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PRK12317  131 VFLARTLGINQLIVAINKMD--AVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:PRK12317  209 LEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNI 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNvPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:PRK12317  289 GFNVRGVGKKDIKRGDVCGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAE 367


                  .
gi 2172335821 241 E 241
Cdd:PRK12317  368 E 368
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-241 8.18e-127

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 365.72  E-value: 8.18e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:TIGR00483 133 AFLARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTL 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV 160
Cdd:TIGR00483 211 LEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNI 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 161 GFNVKNLSVKDIRRGMVAGDSKNvPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVE 240
Cdd:TIGR00483 291 GFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLE 369


                  .
gi 2172335821 241 E 241
Cdd:TIGR00483 370 E 370
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 94-183 4.08e-60

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 184.31  E-value: 4.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  94 TDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIR 173
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|
gi 2172335821 174 RGMVAGDSKN 183
Cdd:cd03693    81 RGDVAGDSKN 90
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-91 3.73e-51

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: 165.74  E-value: 3.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDEKSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:cd01883   129 ALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTL 208

                          90
                  ....*....|.
gi 2172335821  81 LEALDAITEPK 91
Cdd:cd01883   209 LEALDSLEPPE 219
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-232 1.47e-50

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 170.27  E-value: 1.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYnpEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:COG2895   140 SYIASLLGIRHVVVAVNKMD--LVDYSEEVFEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWYDGPTL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKiggigtvP-------VGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPE 153
Cdd:COG2895   216 LEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEE 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 154 ATPGDNVGfnvknLSVK---DIRRG--MVAGDSknvPPQETESFNAQVIILN-HPGTIHNGYapVLDCHTAHIACKFTEI 227
Cdd:COG2895   289 AFAGQSVT-----LTLEdeiDISRGdvIVAADA---PPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAI 358


                  ....*
gi 2172335821 228 LSKVD 232
Cdd:COG2895   359 KYRID 363
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 188-241 6.17e-32

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 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 model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 112.67  E-value: 6.17e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2172335821 188 ETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQAVEE 241
Cdd:cd03705     2 EAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEE 55
GTPBP1 COG5258
GTPase [General function prediction only];
13-227 5.85e-30

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 116.57  E-value: 5.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  13 IVAINKMDEKSVNwsqpRYDEIVKETSSFVKKIGYNP-------------EKIN--FVPIsgwagdnmLEKSPnlgwykg 77
Cdd:COG5258   264 IVAITKIDKVDDE----RVEEVEREIENLLRIVGRTPlevesrhdvdaaiEEINgrVVPI--------LKTSA------- 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  78 VTLlEALDAITE-----PKRPT--DKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLS----TEVKSVEM 146
Cdd:COG5258   325 VTG-EGLDLLDElferlPKRATdeDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGsfreVEVKSIEM 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 147 HHVSLPEATPGDNVGFNVKNLSVKDIRRGMVAGDSKNvPPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTE 226
Cdd:COG5258   404 HYHRVDKAEAGRIVGIALKGVEEEELERGMVLLPRDA-DPKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEP 482


                  .
gi 2172335821 227 I 227
Cdd:COG5258   483 I 483
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-197 8.71e-30

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 115.40  E-value: 8.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPEkINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PRK05124  152 SFIATLLGIKHLVVAVNKMD--LVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTL 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKI-----GGIGTvpvgrVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEAT 155
Cdd:PRK05124  229 LEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAF 303

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2172335821 156 PGDNVgfnvkNLSVK---DIRRG--MVAGDSKnvpPQETESFNAQVI 197
Cdd:PRK05124  304 AGEAI-----TLVLEdeiDISRGdlLVAADEA---LQAVQHASADVV 342
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-197 2.62e-29

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 115.41  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYnpEKINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:PRK05506  149 SFIASLLGIRHVVLAVNKMD--LVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPSL 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  81 LEALDAITEPKRPTDKPLRVPLQDVYKI-----GGIGTvpvgrVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEAT 155
Cdd:PRK05506  225 LEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAF 299

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2172335821 156 PGDNVgfnvkNLSVKD---IRRG-MVAgdSKNVPPQETESFNAQVI 197
Cdd:PRK05506  300 AGQAV-----TLTLADeidISRGdMLA--RADNRPEVADQFDATVV 338
tufA CHL00071
elongation factor Tu
 2-200 1.03e-26

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 106.20  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDeksvnwsQPRYDEIV----KETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLG---- 73
Cdd:CHL00071  121 LLAKQVGVPNIVVFLNKED-------QVDDEELLelveLEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIKrgen 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  74 -WYKGV-TLLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANL--STEVKSVEMHH 148
Cdd:CHL00071  194 kWVDKIyNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLREtkTTTVTGLEMFQ 273

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2172335821 149 VSLPEATPGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQETesFNAQVIILN 200
Cdd:CHL00071  274 KTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTK--FEAQVYILT 323
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-87 1.72e-25

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: 99.18  E-value: 1.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKQMIVAINKMDekSVNWSQPRYDEIVKETSSFVKKIGYNPekINFVPISGWAGDNMLEKSPNLGWYKGVTL 80
Cdd:cd04166   123 SYIASLLGIRHVVVAVNKMD--LVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTL 198


                  ....*..
gi 2172335821  81 LEALDAI 87
Cdd:cd04166   199 LEHLETV 205
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 2-211 3.81e-25

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 101.77  E-value: 3.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDekSVnwSQPRYDEIVK-ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPNLGWYKGVT- 79
Cdd:COG0050   121 LLARQVGVPYIVVFLNKCD--MV--DDEELLELVEmEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKILe 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  80 LLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPAnLSTEVKSVEMHHVSLPEAT 155
Cdd:COG0050   194 LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGE 272

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172335821 156 PGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQeTEsFNAQVIILN-------HPgtIHNGYAP 211
Cdd:COG0050   273 AGDNVGLLLRGIKREDVERGQVLAKPGSITPH-TK-FEAEVYVLSkeeggrhTP--FFNGYRP 331
PLN03127 PLN03127
Elongation factor Tu; Provisional
 2-200 3.21e-23

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 97.20  E-value: 3.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDEKSvnwsQPRYDEIV----KETSSFVKKIGYNPEKINFVPISGWAGDNmleksPNLGWYKG 77
Cdd:PLN03127  170 LLARQVGVPSLVVFLNKVDVVD----DEELLELVemelRELLSFYKFPGDEIPIIRGSALSALQGTN-----DEIGKNAI 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  78 VTLLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAP-ANLSTEVKSVEMHHVSLP 152
Cdd:PLN03127  241 LKLMDAVDEyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILD 320

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2172335821 153 EATPGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQetESFNAQVIILN 200
Cdd:PLN03127  321 QGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTY--KKFEAEIYVLT 366
PRK12735 PRK12735
elongation factor Tu; Reviewed
 2-211 5.12e-23

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 96.06  E-value: 5.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDEKSvnwsQPRYDEIVK-ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPNLGWYKGV-T 79
Cdd:PRK12735  121 LLARQVGVPYIVVFLNKCDMVD----DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKIlE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  80 LLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPaNLSTEVKSVEMHHVSLPEAT 155
Cdd:PRK12735  194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKE-TQKTTVTGVEMFRKLLDEGQ 272

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172335821 156 PGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQetESFNAQVIILN------H-PgtIHNGYAP 211
Cdd:PRK12735  273 AGDNVGVLLRGTKREDVERGQVLAKPGSIKPH--TKFEAEVYVLSkeeggrHtP--FFNGYRP 331
PRK00049 PRK00049
elongation factor Tu; Reviewed
 2-199 7.66e-23

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 95.64  E-value: 7.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDekSVNwsQPRYDEIVK-ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPNLGWYKGV-T 79
Cdd:PRK00049  121 LLARQVGVPYIVVFLNKCD--MVD--DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKIlE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  80 LLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPAnLSTEVKSVEMHHVSLPEAT 155
Cdd:PRK00049  194 LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDT-QKTTVTGVEMFRKLLDEGQ 272

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2172335821 156 PGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQETesFNAQVIIL 199
Cdd:PRK00049  273 AGDNVGALLRGIKREDVERGQVLAKPGSITPHTK--FEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-199 1.74e-22

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 94.63  E-value: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDEKSvnwsQPRYDEIVK-ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPnlGWYKGV-T 79
Cdd:PRK12736  121 LLARQVGVPYLVVFLNKVDLVD----DEELLELVEmEVRELLSEYDFPGDDIPVIRGSALKA---LEGDP--KWEDAImE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  80 LLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPAnLSTEVKSVEMHHVSLPEAT 155
Cdd:PRK12736  192 LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQ 270

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2172335821 156 PGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQETesFNAQVIIL 199
Cdd:PRK12736  271 AGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTK--FKAEVYIL 312
PLN03126 PLN03126
Elongation factor Tu; Provisional
 2-232 8.04e-22

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 93.53  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDeksvnwsQPRYDEIVK----ETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLG---- 73
Cdd:PLN03126  190 LLAKQVGVPNMVVFLNKQD-------QVDDEELLElvelEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIKrgdn 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  74 -WY-KGVTLLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PANLSTEVKSVEMHH 148
Cdd:PLN03126  263 kWVdKIYELMDAVDSyIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVglRETRSTTVTGVEMFQ 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821 149 VSLPEATPGDNVGFNVKNLSVKDIRRGMVAGDSKNVPPQETesFNAQVIIL-NHPGTIHN----GYAPVLDCHTAHIACK 223
Cdd:PLN03126  343 KILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTK--FEAIVYVLkKEEGGRHSpffaGYRPQFYMRTTDVTGK 420


                  ....*....
gi 2172335821 224 FTEILSKVD 232
Cdd:PLN03126  421 VTSIMNDKD 429
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 2-199 3.50e-20

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. 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. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 88.30  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   2 LLAYTLGVKQMIVAINKMDEKSVNWSQPRYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKspnlgwyKGVTLL 81
Cdd:TIGR00485 121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEA-------KILELM 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  82 EALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MVVTFAPANLSTeVKSVEMHHVSLPEATPG 157
Cdd:TIGR00485 194 DAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAG 272

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2172335821 158 DNVGFNVKNLSVKDIRRGMVAGDSKNVPPQetESFNAQVIIL 199
Cdd:TIGR00485 273 DNVGLLLRGIKREEIERGMVLAKPGSIKPH--TKFEAEVYVL 312
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 98-177 1.31e-19

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: 80.00  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  98 LRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNVGFNVKNlsVKDIRRGMV 177
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 101-177 1.01e-18

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 77.94  E-value: 1.01e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172335821 101 PLQDVYKIGGIGTVPVGRVETGILKPGMVVTFA--PANLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:cd03697     4 PIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 98-177 2.13e-16

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: 71.79  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  98 LRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 112-177 2.00e-15

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: 68.83  E-value: 2.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2172335821 112 GTVPVGRVETGILKPGMVVTFAPA-----NLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 185-241 3.08e-14

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 66.52  E-value: 3.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2172335821 185 PPQETESFNAQVIILNH-----PGTIHNGYAPVLDCHTAHIACKFTEILSKVDrrTGQAVEE 241
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN 60
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-90 4.35e-13

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: 65.62  E-value: 4.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   1 ALLAYTLGVKqMIVAINKMDEKsvnwSQPRYDEIVKETSS-FVKKIGYNPEKINFVPISGWAGDNMLekspnlgwykgvT 79
Cdd:pfam00009 114 LRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQ------------T 176

                          90
                  ....*....|.
gi 2172335821  80 LLEALDAITEP 90
Cdd:pfam00009 177 LLDALDEYLPS 187
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 97-177 5.36e-12

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 59.81  E-value: 5.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  97 PLRVPLQDVYKigGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIRRGM 176
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 2172335821 177 V 177
Cdd:cd04089    79 V 79
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 97-172 7.83e-12

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 59.45  E-value: 7.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  97 PLRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNV-----GFNVKNLSVKD 171
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVtltltGIDPNHLRVGS 80


                  .
gi 2172335821 172 I 172
Cdd:cd16267    81 I 81
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 104-177 8.53e-11

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: 56.84  E-value: 8.53e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2172335821 104 DVYKIGGIGTVPVGRVETGILKPGMVVTFAPAN----LSTEVKSVEMHHVSLPEATPGDNVGFNVKNLSVKDIRRGMV 177
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 187-236 1.52e-10

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 56.63  E-value: 1.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2172335821 187 QETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTG 236
Cdd:cd01513     1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTK 50
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 97-180 3.31e-09

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation 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: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 52.50  E-value: 3.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  97 PLRVPLQDVYKiGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMH-HVSLPEATPGDNVGFNVKNLSVKDIRRG 175
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 2172335821 176 MVAGD 180
Cdd:cd03698    80 DILSS 84
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 98-162 7.42e-09

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 51.41  E-value: 7.42e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2172335821  98 LRVPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPANLSTEVKSVEMHHVSLPEATPGDNVGF 162
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 7-90 6.51e-06

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: 45.36  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   7 LGVKQMIVAINKMDEKsvnwSQPRYDEIVKETSSFVKKIGY---NPEKINFVPISGWAGDNMLEkspnlgwykgvtLLEA 83
Cdd:cd00881   112 AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------------LLDA 175


                  ....*..
gi 2172335821  84 LDAITEP 90
Cdd:cd00881   176 IVEHLPP 182
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 192-237 3.38e-05

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: 41.35  E-value: 3.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2172335821 192 FNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDrRTGQ 237
Cdd:cd03708     6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVL-RTGD 50
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 7-186 3.84e-05

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 44.07  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821   7 LGVKQMIVAINKMD----EKSVNwsqpRYDEIVKetssFVKkiGYNPEKINFVPISGWAGDNMlekspnlgwykGVtLLE 82
Cdd:PRK04000  137 IGIKNIVIVQNKIDlvskERALE----NYEQIKE----FVK--GTVAENAPIIPVSALHKVNI-----------DA-LIE 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172335821  83 ALDA-ITEPKRPTDKPlrvPLQ------DVYK--------IGGI--GTVPVGRVETG--I-LKPGMVVTFAPAN----LS 138
Cdd:PRK04000  195 AIEEeIPTPERDLDKP---PRMyvarsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeIeIRPGIKVEEGGKTkwepIT 271

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2172335821 139 TEVKSVEMHHVSLPEATPGDNVGFNVK---NLSVKDIRRGMVAGDSKNVPP 186
Cdd:PRK04000  272 TKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPP 322
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 189-237 1.58e-04

C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 39.85  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2172335821 189 TESFNAQVIILNHPGTI-HNGYAPVLDCHTAHIACKFTEILSKVDRRTGQ 237
Cdd:cd03704     3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGK 52
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 185-237 3.47e-04

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: 39.07  E-value: 3.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2172335821 185 PPQETESFNAQVIILNHPGTIHNGYAPVLDCHTAHIACKFTEILSKVDRRTGQ 237
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGE 53
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 103-161 2.76e-03

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 35.73  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2172335821 103 QDVYKIGGiGTVPVGRVETGILKPGMVVTfaPANLSTEVKSVEMHHVSLPEATPGDNVG 161
Cdd:cd16265     6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
 
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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