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Conserved domains on  [gi|2312626658|gb|UXQ89374|]
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translation elongation factor 1-alpha, partial [Lepidoderma neoperforatum]

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 ...
 1-243 4.89e-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: 493.88  E-value: 4.89e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:PTZ00141  140 AFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:PTZ00141  220 LDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFN 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNDPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:PTZ00141  300 VKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379


                  ...
gi 2312626658 241 KNI 243
Cdd:PTZ00141  380 KAI 382
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-243 4.89e-177

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 493.88  E-value: 4.89e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:PTZ00141  140 AFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:PTZ00141  220 LDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFN 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNDPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:PTZ00141  300 VKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379


                  ...
gi 2312626658 241 KNI 243
Cdd:PTZ00141  380 KAI 382
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-243 1.38e-128

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: 370.03  E-value: 1.38e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:COG5256   133 ARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEA 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:COG5256   211 LDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFN 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNdPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:COG5256   291 VRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENP 369


                  ...
gi 2312626658 241 KNI 243
Cdd:COG5256   370 QFL 372
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-241 2.13e-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: 367.26  E-value: 2.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:TIGR00483 136 ARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEA 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:TIGR00483 214 LDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFN 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNdPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:TIGR00483 294 VRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENP 372


                  .
gi 2312626658 241 K 241
Cdd:TIGR00483 373 Q 373
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 91-181 3.47e-61

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: 187.01  E-value: 3.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  91 TDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIR 170
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 2312626658 171 RGMVAGDSKND 181
Cdd:cd03693    81 RGDVAGDSKND 91
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 109-174 3.26e-16

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: 70.76  E-value: 3.26e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2312626658 109 GTVPVGRVETGILKPGMIVTFAPA-----NLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 174
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-243 4.89e-177

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 493.88  E-value: 4.89e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:PTZ00141  140 AFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:PTZ00141  220 LDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFN 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNDPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:PTZ00141  300 VKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379


                  ...
gi 2312626658 241 KNI 243
Cdd:PTZ00141  380 KAI 382
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-241 8.42e-130

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 374.04  E-value: 8.42e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:PLN00043  140 AFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:PLN00043  220 LDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFN 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNDPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:PLN00043  300 VKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEP 379


                  .
gi 2312626658 241 K 241
Cdd:PLN00043  380 K 380
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-243 1.38e-128

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: 370.03  E-value: 1.38e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:COG5256   133 ARTLGINQLIVAVNKMD--AVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEA 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:COG5256   211 LDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFN 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNdPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:COG5256   291 VRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENP 369


                  ...
gi 2312626658 241 KNI 243
Cdd:COG5256   370 QFL 372
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-241 2.13e-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: 367.26  E-value: 2.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:TIGR00483 136 ARTLGINQLIVAINKMD--SVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEA 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:TIGR00483 214 LDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFN 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGDSKNdPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:TIGR00483 294 VRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENP 372


                  .
gi 2312626658 241 K 241
Cdd:TIGR00483 373 Q 373
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-243 9.23e-127

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 365.40  E-value: 9.23e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:PRK12317  134 ARTLGINQLIVAINKMD--AVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFN 160
Cdd:PRK12317  212 LDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFN 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 161 VKNLSVKDIRRGMVAGdSKNDPPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVP 240
Cdd:PRK12317  292 VRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENP 370


                  ...
gi 2312626658 241 KNI 243
Cdd:PRK12317  371 QFI 373
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 91-181 3.47e-61

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: 187.01  E-value: 3.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  91 TDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIR 170
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 2312626658 171 RGMVAGDSKND 181
Cdd:cd03693    81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 4-242 3.52e-51

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: 171.81  E-value: 3.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   4 LGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYnpEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEALDA 83
Cdd:COG2895   146 LGIRHVVVAVNKMD--LVDYSEEVFEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWYDGPTLLEHLET 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  84 ITEPKRPTDKPLRVPLQDVYKiggigtvP-------VGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDN 156
Cdd:COG2895   222 VEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQS 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 157 VGfnvknLSVK---DIRRG-MVAgdSKNDPPQETESFNAQVIILN-HPGQIHAGYapVLDCHTAHIACKFTELLNKVDRR 231
Cdd:COG2895   295 VT-----LTLEdeiDISRGdVIV--AADAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVN 365

                         250
                  ....*....|...
gi 2312626658 232 TGA--AQEEVPKN 242
Cdd:COG2895   366 TLEheAADSLELN 378
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-88 1.61e-49

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: 161.50  E-value: 1.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:cd01883   132 ARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEA 211


                  ....*...
gi 2312626658  81 LDAITEPK 88
Cdd:cd01883   212 LDSLEPPE 219
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 185-243 6.67e-33

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: 115.37  E-value: 6.67e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2312626658 185 ETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVPKNI 243
Cdd:cd03705     2 EAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFL 60
GTPBP1 COG5258
GTPase [General function prediction only];
10-224 7.10e-31

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 119.27  E-value: 7.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  10 IVAINKMDEksvnWSQARYDEIVKETSSFVKKIGYNP-------------EKIN--FVPIsgwagdnmLEKSPnlgwykg 74
Cdd:COG5258   264 IVAITKIDK----VDDERVEEVEREIENLLRIVGRTPlevesrhdvdaaiEEINgrVVPI--------LKTSA------- 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  75 VTLlEALDAITE-----PKRPT--DKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLS----TEVKSVEM 143
Cdd:COG5258   325 VTG-EGLDLLDElferlPKRATdeDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGsfreVEVKSIEM 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 144 HHVALPEAVPGDNVGFNVKNLSVKDIRRGMVAGDSKNDpPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTE 223
Cdd:COG5258   404 HYHRVDKAEAGRIVGIALKGVEEEELERGMVLLPRDAD-PKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRFEP 482


                  .
gi 2312626658 224 L 224
Cdd:COG5258   483 I 483
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 4-194 1.29e-30

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 117.71  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   4 LGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPEkINFVPISGWAGDNMLEKSPNLGWYKGVTLLEALDA 83
Cdd:PRK05124  158 LGIKHLVVAVNKMD--LVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLET 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  84 ITEPKRPTDKPLRVPLQDVYKI-----GGIGTvpvgrVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVg 158
Cdd:PRK05124  235 VDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI- 308

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2312626658 159 fnvkNLSVK---DIRRG--MVAGDSKndpPQETESFNAQVI 194
Cdd:PRK05124  309 ----TLVLEdeiDISRGdlLVAADEA---LQAVQHASADVV 342
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-194 2.70e-30

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 118.11  E-value: 2.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYnpEKINFVPISGWAGDNMLEKSPNLGWYKGVTLLEA 80
Cdd:PRK05506  152 ASLLGIRHVVLAVNKMD--LVDYDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPSLLEH 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDAITEPKRPTDKPLRVPLQDVYKI-----GGIGTvpvgrVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGD 155
Cdd:PRK05506  228 LETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQ 302

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2312626658 156 NVgfnvkNLSVKD---IRRG-MVAgdSKNDPPQETESFNAQVI 194
Cdd:PRK05506  303 AV-----TLTLADeidISRGdMLA--RADNRPEVADQFDATVV 338
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 4-84 1.26e-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: 99.57  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   4 LGVKQMIVAINKMDekSVNWSQARYDEIVKETSSFVKKIGYNPekINFVPISGWAGDNMLEKSPNLGWYKGVTLLEALDA 83
Cdd:cd04166   129 LGIRHVVVAVNKMD--LVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLET 204


                  .
gi 2312626658  84 I 84
Cdd:cd04166   205 V 205
tufA CHL00071
elongation factor Tu
 4-197 3.71e-25

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 101.96  E-value: 3.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   4 LGVKQMIVAINKMDeksvnwsQARYDEIV----KETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLG-----WYKG 74
Cdd:CHL00071  126 VGVPNIVVFLNKED-------QVDDEELLelveLEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIKrgenkWVDK 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  75 V-TLLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAPANlSTEVKSVEMHHVALP 149
Cdd:CHL00071  199 IyNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRETK-TTTVTGLEMFQKTLD 277

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2312626658 150 EAVPGDNVGFNVKNLSVKDIRRGMVAGDSKNDPPQETesFNAQVIILN 197
Cdd:CHL00071  278 EGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTK--FEAQVYILT 323
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-174 9.94e-23

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: 95.22  E-value: 9.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDeksvnwsQARYDEIVK----ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPNLGWYKGVT 76
Cdd:COG0050   123 ARQVGVPYIVVFLNKCD-------MVDDEELLElvemEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKIL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  77 -LLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAPAnLSTEVKSVEMHHVALPEA 151
Cdd:COG0050   193 eLMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEG 271

                         170       180
                  ....*....|....*....|...
gi 2312626658 152 VPGDNVGFNVKNLSVKDIRRGMV 174
Cdd:COG0050   272 EAGDNVGLLLRGIKREDVERGQV 294
PRK12735 PRK12735
elongation factor Tu; Reviewed
 63-196 3.42e-22

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 93.75  E-value: 3.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  63 LEKSPNLGWYKGV-TLLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAPaNLSTE 137
Cdd:PRK12735  179 LEGDDDEEWEAKIlELMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKE-TQKTT 257

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2312626658 138 VKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMVAGDSKNDPPQetESFNAQVIIL 196
Cdd:PRK12735  258 VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPH--TKFEAEVYVL 314
PRK00049 PRK00049
elongation factor Tu; Reviewed
 5-174 2.31e-21

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.40  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   5 GVKQMIVAINKMDeksvnwsQARYDEIVK----ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPNLGWYKGV-TLLE 79
Cdd:PRK00049  127 GVPYIVVFLNKCD-------MVDDEELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKIlELMD 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  80 ALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAPAnLSTEVKSVEMHHVALPEAVPGD 155
Cdd:PRK00049  197 AVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDT-QKTTVTGVEMFRKLLDEGQAGD 275

                         170
                  ....*....|....*....
gi 2312626658 156 NVGFNVKNLSVKDIRRGMV 174
Cdd:PRK00049  276 NVGALLRGIKREDVERGQV 294
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-197 6.92e-21

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 90.65  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNmleksPNLGWYKGVTLLEA 80
Cdd:PLN03127  172 ARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTN-----DEIGKNAILKLMDA 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAP-ANLSTEVKSVEMHHVALPEAVPGD 155
Cdd:PLN03127  247 VDEyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGD 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2312626658 156 NVGFNVKNLSVKDIRRGMVAgdSKNDPPQETESFNAQVIILN 197
Cdd:PLN03127  327 NVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLT 366
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-229 7.22e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 90.83  E-value: 7.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSvnwsQARYDEIVK-ETSSFVKKIGYNPEKINFVPISGWAGDNMLEKSPNLG-----WY-K 73
Cdd:PLN03126  192 AKQVGVPNMVVFLNKQDQVD----DEELLELVElEVRELLSSYEFPGDDIPIISGSALLALEALMENPNIKrgdnkWVdK 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  74 GVTLLEALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFA--PANLSTEVKSVEMHHVALPE 150
Cdd:PLN03126  268 IYELMDAVDSyIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVglRETRSTTVTGVEMFQKILDE 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658 151 AVPGDNVGFNVKNLSVKDIRRGMVAGDSKNDPPQETesFNAQVIIL-NHPGQIH----AGYAPVLDCHTAHIACKFTELL 225
Cdd:PLN03126  348 ALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTK--FEAIVYVLkKEEGGRHspffAGYRPQFYMRTTDVTGKVTSIM 425


                  ....
gi 2312626658 226 NKVD 229
Cdd:PLN03126  426 NDKD 429
PRK12736 PRK12736
elongation factor Tu; Reviewed
 5-196 4.30e-20

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 87.69  E-value: 4.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   5 GVKQMIVAINKMDeksvnwsQARYDEIVK----ETSSFVKKIGYNPEKINFVPISGWAGdnmLEKSPnlGWYKGV-TLLE 79
Cdd:PRK12736  127 GVPYLVVFLNKVD-------LVDDEELLElvemEVRELLSEYDFPGDDIPVIRGSALKA---LEGDP--KWEDAImELMD 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  80 ALDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAPAnLSTEVKSVEMHHVALPEAVPGD 155
Cdd:PRK12736  195 AVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGD 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2312626658 156 NVGFNVKNLSVKDIRRGMVAGDSKNDPPQETesFNAQVIIL 196
Cdd:PRK12736  274 NVGVLLRGVDRDEVERGQVLAKPGSIKPHTK--FKAEVYIL 312
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 95-174 1.63e-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: 79.62  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  95 LRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFNVKNlsVKDIRRGMV 174
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 ...
 98-174 6.19e-19

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: 78.33  E-value: 6.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  98 PLQDVYKIGGIGTVPVGRVETGILKPGM---IVTFAPaNLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 174
Cdd:cd03697     4 PIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-174 1.66e-18

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: 83.29  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKQMIVAINKMDEKSVNWSQARYDEIVKETSSFVKKIGYNPEKINFVPISGWAGDNMLEKspnlgwyKGVTLLEA 80
Cdd:TIGR00485 123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEA-------KILELMDA 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  81 LDA-ITEPKRPTDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPG---MIVTFAPANLSTeVKSVEMHHVALPEAVPGDN 156
Cdd:TIGR00485 196 VDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDN 274

                         170
                  ....*....|....*...
gi 2312626658 157 VGFNVKNLSVKDIRRGMV 174
Cdd:TIGR00485 275 VGLLLRGIKREEIERGMV 292
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 109-174 3.26e-16

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: 70.76  E-value: 3.26e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2312626658 109 GTVPVGRVETGILKPGMIVTFAPA-----NLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 174
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 95-174 5.86e-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: 70.63  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  95 LRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 174
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 182-229 7.88e-15

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: 68.06  E-value: 7.88e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2312626658 182 PPQETESFNAQVIILNH-----PGQIHAGYAPVLDCHTAHIACKFTELLNKVD 229
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD 53
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-87 1.11e-12

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: 64.47  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   1 AYTLGVKqMIVAINKMDEKsvnwSQARYDEIVKETSS-FVKKIGYNPEKINFVPISGWAGDNMLekspnlgwykgvTLLE 79
Cdd:pfam00009 117 ARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQ------------TLLD 179


                  ....*...
gi 2312626658  80 ALDAITEP 87
Cdd:pfam00009 180 ALDEYLPS 187
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 101-174 3.35e-12

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: 60.70  E-value: 3.35e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2312626658 101 DVYKIGGIGTVPVGRVETGILKPGMIVTFAPAN----LSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGMV 174
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 94-169 3.75e-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: 60.22  E-value: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  94 PLRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNV-----GFNVKNLSVKD 168
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVtltltGIDPNHLRVGS 80


                  .
gi 2312626658 169 I 169
Cdd:cd16267    81 I 81
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 184-234 1.46e-11

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: 59.33  E-value: 1.46e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2312626658 184 QETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGA 234
Cdd:cd01513     1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE 51
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 94-174 2.58e-11

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: 57.88  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  94 PLRVPLQDVYKigGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGFNVKNLSVKDIRRGM 173
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 2312626658 174 V 174
Cdd:cd04089    79 V 79
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 94-177 5.00e-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: 51.73  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  94 PLRVPLQDVYKiGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMH-HVALPEAVPGDNVGFNVKNLSVKDIRRG 172
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 2312626658 173 MVAGD 177
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 ...
 95-159 1.66e-08

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: 50.26  E-value: 1.66e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2312626658  95 LRVPLQDVYKIGGIGTVPVGRVETGILKPGMIVTFAPANLSTEVKSVEMHHVALPEAVPGDNVGF 159
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 4-87 8.17e-07

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: 48.06  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   4 LGVKQMIVAINKMDEKsvnwSQARYDEIVKETSSFVKKIGY---NPEKINFVPISGWAGDNMLEkspnlgwykgvtLLEA 80
Cdd:cd00881   112 AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE------------LLDA 175


                  ....*..
gi 2312626658  81 LDAITEP 87
Cdd:cd00881   176 IVEHLPP 182
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 186-241 2.41e-05

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: 42.16  E-value: 2.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2312626658 186 TESFNAQVIILNHPGQI-HAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVPK 241
Cdd:cd03704     3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPK 59
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 189-233 1.51e-04

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: 39.42  E-value: 1.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2312626658 189 FNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDrRTG 233
Cdd:cd03708     6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVL-RTG 49
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 4-183 1.81e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 42.15  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658   4 LGVKQMIVAINKMDekSVNWSQAR--YDEIVKetssFVKkiGYNPEKINFVPISGWAGDNMlekspnlgwykGVtLLEAL 81
Cdd:PRK04000  137 IGIKNIVIVQNKID--LVSKERALenYEQIKE----FVK--GTVAENAPIIPVSALHKVNI-----------DA-LIEAI 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312626658  82 DA-ITEPKRPTDKPlrvPLQ------DVYK--------IGGI--GTVPVGRVETG--I-LKPGMIVTFAPAN----LSTE 137
Cdd:PRK04000  197 EEeIPTPERDLDKP---PRMyvarsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeIeIRPGIKVEEGGKTkwepITTK 273

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2312626658 138 VKSVEMHHVALPEAVPGDNVGFNVK---NLSVKDIRRGMVAGDSKNDPP 183
Cdd:PRK04000  274 IVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPP 322
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 100-158 6.03e-04

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: 37.66  E-value: 6.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2312626658 100 QDVYKIGGiGTVPVGRVETGILKPGMIVTfaPANLSTEVKSVEMHHVALPEAVPGDNVG 158
Cdd:cd16265     6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 182-243 1.65e-03

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


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 37.14  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2312626658 182 PPQETESFNAQVIILNHPGQIHAGYAPVLDCHTAHIACKFTELLNKVDRRTGAAQEEVPKNI 243
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCL 62
 
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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