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Conserved domains on  [gi|443496589|gb|AGC93055|]
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translation elongation factor 1-alpha, partial [Pholiotina pygmaeoaffinis]

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 ...
 1-295 0e+00

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: 554.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPI 78
Cdd:PTZ00141 114 LVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  79 SGWHGDNMLEPSENMTWYKGwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 158
Cdd:PTZ00141 194 SGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILK 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 159 SGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKEAASFNAQVIVLNHPGQI 238
Cdd:PTZ00141 262 PGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQI 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443496589 239 GAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:PTZ00141 342 KNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPM 398
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-295 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 554.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPI 78
Cdd:PTZ00141 114 LVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  79 SGWHGDNMLEPSENMTWYKGwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 158
Cdd:PTZ00141 194 SGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILK 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 159 SGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKEAASFNAQVIVLNHPGQI 238
Cdd:PTZ00141 262 PGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQI 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443496589 239 GAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:PTZ00141 342 KNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPM 398
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-295 2.19e-153

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: 435.45  E-value: 2.19e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589    1 LIIAAGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPISG 80
Cdd:TIGR00483 114 LVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISA 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   81 WHGDNMLEPSENMTWYKGwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG 160
Cdd:TIGR00483 190 WNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  161 MVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNdPAKEAASFNAQVIVLNHPGQIGA 240
Cdd:TIGR00483 258 DKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITV 336

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 443496589  241 GYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:TIGR00483 337 GYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPM 391
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 18-295 1.72e-144

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: 412.79  E-value: 1.72e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  18 GQTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPISGWHGDNMLEPSENMTWYK 97
Cdd:COG5256  124 GQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  98 GwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSV 177
Cdd:COG5256  204 G------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSI 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 178 EMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKeAASFNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKF 257
Cdd:COG5256  272 EMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTV-AEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTF 350

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 443496589 258 AELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:COG5256  351 VELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPL 388
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-124 7.11e-64

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: 200.41  E-value: 7.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEERFLEICKETSNFIKKVGYNPKTVAFVPI 78
Cdd:cd01883  106 LVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPI 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 443496589  79 SGWHGDNMLEPSENMTWYKGWtrdgktgslkgkTLLDAIDAIEPPV 124
Cdd:cd01883  186 SGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 218-295 1.62e-27

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: 102.73  E-value: 1.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  218 PAKEAASFNAQVIVLNH-----PGQIGAGYAPVLDCHTAHIACKFAELIEKIDrrTGKSLENaPKFVKSGDAAIVKLVPI 292
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77


                  ...
gi 443496589  293 KPM 295
Cdd:pfam03143  78 KPI 80
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-295 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 554.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPI 78
Cdd:PTZ00141 114 LVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  79 SGWHGDNMLEPSENMTWYKGwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 158
Cdd:PTZ00141 194 SGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILK 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 159 SGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKEAASFNAQVIVLNHPGQI 238
Cdd:PTZ00141 262 PGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQI 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443496589 239 GAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:PTZ00141 342 KNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPM 398
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-295 2.19e-153

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: 435.45  E-value: 2.19e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589    1 LIIAAGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPISG 80
Cdd:TIGR00483 114 LVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISA 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   81 WHGDNMLEPSENMTWYKGwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG 160
Cdd:TIGR00483 190 WNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPG 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  161 MVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNdPAKEAASFNAQVIVLNHPGQIGA 240
Cdd:TIGR00483 258 DKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITV 336

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 443496589  241 GYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:TIGR00483 337 GYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPM 391
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-295 2.67e-150

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 428.35  E-value: 2.67e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEERFLEICKETSNFIKKVGYNPKTVAFVPI 78
Cdd:PLN00043 114 LIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  79 SGWHGDNMLEPSENMTWYKGwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 158
Cdd:PLN00043 194 SGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIK 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 159 SGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKEAASFNAQVIVLNHPGQI 238
Cdd:PLN00043 262 PGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQI 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443496589 239 GAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:PLN00043 342 GNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPM 398
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 18-295 1.72e-144

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: 412.79  E-value: 1.72e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  18 GQTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPISGWHGDNMLEPSENMTWYK 97
Cdd:COG5256  124 GQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  98 GwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSV 177
Cdd:COG5256  204 G------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSI 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 178 EMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKeAASFNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKF 257
Cdd:COG5256  272 EMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPPTV-AEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTF 350

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 443496589 258 AELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:COG5256  351 VELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPL 388
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 18-295 1.09e-142

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 408.16  E-value: 1.09e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  18 GQTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPKTVAFVPISGWHGDNMLEPSENMTWYK 97
Cdd:PRK12317 125 PQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  98 GwtrdgktgslkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSV 177
Cdd:PRK12317 205 G------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSI 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 178 EMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASdSKNDPAKEAASFNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKF 257
Cdd:PRK12317 273 EMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTF 351

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 443496589 258 AELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:PRK12317 352 EELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPL 389
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-124 7.11e-64

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: 200.41  E-value: 7.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEERFLEICKETSNFIKKVGYNPKTVAFVPI 78
Cdd:cd01883  106 LVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPI 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 443496589  79 SGWHGDNMLEPSENMTWYKGWtrdgktgslkgkTLLDAIDAIEPPV 124
Cdd:cd01883  186 SGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 127-217 1.84e-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: 189.71  E-value: 1.84e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 127 SDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIR 206
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                         90
                 ....*....|.
gi 443496589 207 RGNVASDSKND 217
Cdd:cd03693   81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 19-273 1.56e-53

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: 179.90  E-value: 1.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYnpKTVAFVPISGWHGDNMLEPSENMTWYkg 98
Cdd:COG2895  135 QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWY-- 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  99 wtrdgktgslKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKiggigtvP-------VGRVETGIIKSGMVVTFAPTNVT 171
Cdd:COG2895  211 ----------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKT 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 172 TEVKSVEMHHEQLEQGNPGDNVGF----NVknvsvkDIRRGNVASDSkNDPAKEAASFNAQVIVLN-HPGQIGAGYapVL 246
Cdd:COG2895  274 STVKSIVTFDGDLEEAFAGQSVTLtledEI------DISRGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LL 344

                        250       260       270
                 ....*....|....*....|....*....|..
gi 443496589 247 DCHTAHIACKFAELIEKID-----RRTGKSLE 273
Cdd:COG2895  345 KHGTRTVRATVTAIKYRIDvntleHEAADSLE 376
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 220-295 3.69e-49

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: 158.51  E-value: 3.69e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443496589 220 KEAASFNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:cd03705    1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPL 76
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 19-242 2.85e-33

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 125.95  E-value: 2.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGynPKTVAFVPISGWHGDNMLEPSENMTWYkg 98
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY-- 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   99 wtrdgktgslKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTVPVGRVETgiiksGMVVTFAPTNVTTE 173
Cdd:TIGR02034 196 ----------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHV-----GDEVVVLPSGRSSR 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 443496589  174 VKSVEMHHEQLEQGNPGDNVGFNVKNVSvkDIRRGN--VASDSkndPAKEAASFNAQVIVL-NHPGQIGAGY 242
Cdd:TIGR02034 261 VARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDllAAADS---APEVADQFAATLVWMaEEPLLPGRSY 327
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 19-230 6.38e-31

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 120.40  E-value: 6.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPkTVAFVPISGWHGDNMLEPSENMTWYkg 98
Cdd:PRK05124 147 QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWY-- 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  99 wtrdgktgslKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGIIKSGMVVTFAPTNVTTE 173
Cdd:PRK05124 224 ----------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESN 288

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443496589 174 VKSVEMHHEQLEQGNPGDNVGFNVKNVSvkDIRRGNVASDSKNDPAkEAASFNAQVI 230
Cdd:PRK05124 289 VARIVTFDGDLEEAFAGEAITLVLEDEI--DISRGDLLVAADEALQ-AVQHASADVV 342
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 19-230 1.09e-30

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 120.80  E-value: 1.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNpkTVAFVPISGWHGDNMLEPSENMTWYkg 98
Cdd:PRK05506 144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY-- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  99 wtrdgktgslKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGIIKSGMVVTFAPTNVTTE 173
Cdd:PRK05506 220 ----------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSR 284

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 174 VKSVEMHHEQLEQGNPGDNVgfnvkNVSVKD---IRRGNVASDSkNDPAKEAASFNAQVI 230
Cdd:PRK05506 285 VKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRGDMLARA-DNRPEVADQFDATVV 338
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 19-123 7.80e-30

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: 111.89  E-value: 7.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  19 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEERFLEICKETSNFIKKVGYNPktVAFVPISGWHGDNMLEPSENMTWYkg 98
Cdd:cd04166  118 QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY-- 193

                         90       100
                 ....*....|....*....|....*
gi 443496589  99 wtrdgktgslKGKTLLDAIDAIEPP 123
Cdd:cd04166  194 ----------KGPTLLEHLETVEIA 208
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 17-232 2.11e-28

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: 112.17  E-value: 2.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGWhgdNMLEPSEN 92
Cdd:COG0050  110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSKYGFPGDDTPIIRGSAL---KALEGDPD 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  93 MTWYKgwtrdgktgslKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG---MVVTFAPT 168
Cdd:COG0050  185 PEWEK-----------KILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT 253

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 443496589 169 nVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQVIVL 232
Cdd:COG0050  254 -QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
tufA CHL00071
elongation factor Tu
 17-233 2.95e-28

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 112.36  E-value: 2.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  17 DG---QTREHALLAFTLGVRQLIVAVNKMDttKWSEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGwhgdnmLEPSEN 92
Cdd:CHL00071 110 DGpmpQTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVSGSA------LLALEA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  93 MTWYKGWTRDGKTGSLKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVT---FAPT 168
Cdd:CHL00071 182 LTENPKIKRGENKWVDKIYNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRET 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 443496589 169 NVTTeVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQVIVLN 233
Cdd:CHL00071 262 KTTT-VTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVL--AKPGTITPHTKFEAQVYILT 323
PRK00049 PRK00049
elongation factor Tu; Reviewed
 17-232 7.65e-28

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 110.66  E-value: 7.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTKwsEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGWHGdnmLEPSEN 92
Cdd:PRK00049 110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMVD--DEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDD 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  93 MTWYKgwtrdgktgslKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG---MVVTFAPT 168
Cdd:PRK00049 185 EEWEK-----------KILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDT 253

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 443496589 169 NVTTeVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQVIVL 232
Cdd:PRK00049 254 QKTT-VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 218-295 1.62e-27

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: 102.73  E-value: 1.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  218 PAKEAASFNAQVIVLNH-----PGQIGAGYAPVLDCHTAHIACKFAELIEKIDrrTGKSLENaPKFVKSGDAAIVKLVPI 292
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77


                  ...
gi 443496589  293 KPM 295
Cdd:pfam03143  78 KPI 80
PLN03127 PLN03127
Elongation factor Tu; Provisional
 6-233 2.31e-27

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 110.30  E-value: 2.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   6 GTGEFEAGI----SKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEIC----KETSNFIKKVGYNPKTVA 74
Cdd:PLN03127 144 GAAQMDGGIlvvsAPDGpmpQTKEHILLARQVGVPSLVVFLNKVDVV--DDEELLELVemelRELLSFYKFPGDEIPIIR 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  75 FVPISGWHGDNmlepsenmtwykgwTRDGKTGSLKgktLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 153
Cdd:PLN03127 222 GSALSALQGTN--------------DEIGKNAILK---LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVE 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 154 TGIIKSG---MVVTFAPT-NVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQV 229
Cdd:PLN03127 285 QGTIKVGeevEIVGLRPGgPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEI 362


                 ....
gi 443496589 230 IVLN 233
Cdd:PLN03127 363 YVLT 366
PRK12736 PRK12736
elongation factor Tu; Reviewed
 17-232 1.88e-26

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 106.95  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGWHGdnmLEPSEn 92
Cdd:PRK12736 110 DGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDDIPVIRGSALKA---LEGDP- 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  93 mTWYKgwtrdgktgslKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG---MVVTFAPT 168
Cdd:PRK12736 184 -KWED-----------AIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET 251

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 443496589 169 nVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNV-ASDSKNDPAKEaasFNAQVIVL 232
Cdd:PRK12736 252 -QKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVlAKPGSIKPHTK---FKAEVYIL 312
PRK12735 PRK12735
elongation factor Tu; Reviewed
 17-232 3.01e-26

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 106.46  E-value: 3.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGWHGdnmLEPSEN 92
Cdd:PRK12735 110 DGpmpQTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDD 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  93 MTWYKgwtrdgktgslKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG---MVVTFAPT 168
Cdd:PRK12735 185 EEWEA-----------KILELMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKET 253

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 443496589 169 NVTTeVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQVIVL 232
Cdd:PRK12735 254 QKTT-VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 19-232 6.20e-24

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: 100.24  E-value: 6.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   19 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGwhgdnmLEPSENMTWYK 97
Cdd:TIGR00485 115 QTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSQYDFPGDDTPIIRGSA------LKALEGDAEWE 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   98 GWTRDgktgslkgktLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSG---MVVTFAPTNVTTe 173
Cdd:TIGR00485 187 AKILE----------LMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT- 255

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 443496589  174 VKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQVIVL 232
Cdd:TIGR00485 256 VTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVL 312
PLN03126 PLN03126
Elongation factor Tu; Provisional
 19-295 1.06e-21

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 94.30  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  19 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGwhgdnmLEPSENMTWYK 97
Cdd:PLN03126 184 QTKEHILLAKQVGVPNMVVFLNKQDQV--DDEELLELVElEVRELLSSYEFPGDDIPIISGSA------LLALEALMENP 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  98 GWTRDGKTGSLKGKTLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVT--TEV 174
Cdd:PLN03126 256 NIKRGDNKWVDKIYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTV 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 175 KSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVAsdSKNDPAKEAASFNAQVIVLNHP-----GQIGAGYAPVLDCH 249
Cdd:PLN03126 336 TGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMR 413

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 443496589 250 TAHIACKFAELIEKIDRRTgkslenapKFVKSGDAAIVKLVPIKPM 295
Cdd:PLN03126 414 TTDVTGKVTSIMNDKDEES--------KMVMPGDRVKMVVELIVPV 451
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-213 5.02e-20

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


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 89.97  E-value: 5.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAgtgefeagisKDG---QTREH-ALLAFtLGVRQLIVAVNKMDTTkwSEERFLEICKETSNFIKkvGYNPKTVAFV 76
Cdd:COG3276   80 LVVAA----------DEGvmpQTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLEDAPIV 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  77 PISGwhgdnmlepsenmtwykgwtrdgKTGslKG-KTLLDAIDAI--EPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 153
Cdd:COG3276  145 PVSA-----------------------VTG--EGiDELRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLL 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 154 TGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASD 213
Cdd:COG3276  200 SGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAA 259
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 131-210 7.26e-20

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: 81.93  E-value: 7.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 131 LRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNvsVKDIRRGNV 210
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-123 1.06e-18

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


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 81.80  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589    1 LIIAAGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEERFLEICKETSN-FIKKVGYNPKTVAFVPIS 79
Cdd:pfam00009  98 LVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGS 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 443496589   80 GWHGDNMlepsenmtwykgwtrdgktgslkgKTLLDAIDAIEPP 123
Cdd:pfam00009 168 ALKGEGV------------------------QTLLDALDEYLPS 187
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 222-295 3.75e-18

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: 77.82  E-value: 3.75e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 443496589 222 AASFNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKFAELIEKIDRRTGKslENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:cd01513    3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPV 74
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 19-288 1.33e-17

selenocysteine-specific elongation factor SelB; 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-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 82.61  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   19 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEERFLEICKETSNFIKKVGYNPKTVAFVpISGWHGDNMLEPSENMtwykg 98
Cdd:TIGR00475  90 QTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL----- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   99 wtrdgktgslkgKTLLDAIDAieppvRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVE 178
Cdd:TIGR00475 162 ------------KNLLESLDI-----KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQ 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  179 MHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNVASDSKNDPAKEAASFNAQVIVLnhPGQIgagyapvldCHTAHIACKFA 258
Cdd:TIGR00475 225 AQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLL--ELQP---------YHIAHGMSVTT 293

                         250       260       270
                  ....*....|....*....|....*....|
gi 443496589  259 ELIEKIDRRTGKSLENAPKFVKSGDAAIVK 288
Cdd:TIGR00475 294 GKISLLDKGIALLTLDAPLILAKGDKLVLR 323
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 133-212 1.46e-17

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: 75.63  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 133 LPLQDVYKIGGIGTVPVGRVETGIIKSGM---VVTFAPTNVTTeVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGN 209
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKETLKTT-VTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81


                 ...
gi 443496589 210 VAS 212
Cdd:cd03697   82 VLA 84
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 131-210 4.45e-17

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: 74.49  E-value: 4.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 131 LRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNV 210
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 145-210 3.18e-14

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: 66.52  E-value: 3.18e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 443496589  145 GTVPVGRVETGIIKSGMVVTFAP-----TNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNV 210
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 130-213 1.29e-13

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: 64.84  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 130 PLRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGN 209
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80


                 ....
gi 443496589 210 VASD 213
Cdd:cd16267   81 ILCD 84
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 130-210 4.92e-13

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: 63.27  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 130 PLRLPLQDVYKigGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGN 209
Cdd:cd04089    1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                 .
gi 443496589 210 V 210
Cdd:cd04089   79 V 79
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 225-289 5.13e-13

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: 64.11  E-value: 5.13e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443496589 225 FNAQVIVLNHPGQI-GAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKL 289
Cdd:cd03704    6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARL 71
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-123 6.13e-12

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: 63.08  E-value: 6.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589   1 LIIAAGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEERFLEICKETSNFIKKVGY---NPKTVAFVP 77
Cdd:cd00881   91 LVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPIIP 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 443496589  78 ISGWHGDNMLEpsenmtwykgwtrdgktgslkgktLLDAIDAIEPP 123
Cdd:cd00881  161 ISALTGEGIEE------------------------LLDAIVEHLPP 182
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 130-213 2.54e-10

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: 55.97  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 130 PLRLPLQDVYKiGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMH-HEQLEQGNPGDNVGFNVKNVSVKDIRRG 208
Cdd:cd03698    1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                 ....*
gi 443496589 209 NVASD 213
Cdd:cd03698   80 DILSS 84
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 137-210 1.46e-09

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: 53.76  E-value: 1.46e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443496589 137 DVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTN----VTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVSVKDIRRGNV 210
Cdd:cd03694    7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 218-295 4.33e-08

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: 50.24  E-value: 4.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443496589 218 PAKEAASFNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKFAELIEKIDRRTGKSLENAPKFVKSGDAAIVKLVPIKPM 295
Cdd:cd04093    1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPI 78
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 131-210 4.96e-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: 49.49  E-value: 4.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589 131 LRLPLQDVYKIGGIGTVPVGRVETGIIKSGMVVTFAPTNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKN-VsvkDIRRGN 209
Cdd:cd03695    1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77


                 .
gi 443496589 210 V 210
Cdd:cd03695   78 L 78
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 19-194 9.16e-06

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 46.77  E-value: 9.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  19 QTREHaLLAFT-LGVRQLIVAVNKMDTTkwSEERFLEICKETSNFIKkvgynpKTVA----FVPISGWHGDNMlepsenm 93
Cdd:PRK04000 126 QTKEH-LMALDiIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK------GTVAenapIIPVSALHKVNI------- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  94 twykgwtrdgktgslkgKTLLDAIDA-IEPPVRPSDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG--I- 156
Cdd:PRK04000 190 -----------------DALIEAIEEeIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeIe 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 443496589 157 IKSGMVVTFAP----TNVTTEVKSVEMHHEQLEQGNPGDNVG 194
Cdd:PRK04000 253 IRPGIKVEEGGktkwEPITTKIVSLRAGGEKVEEARPGGLVG 294
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 225-283 8.55e-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: 40.58  E-value: 8.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443496589 225 FNAQVIVLNHPGQIGAGYAPVLDCHTAHIACKfaelIEKIDR---RTGKSLE------NAPKFVKSGD 283
Cdd:cd03708    6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTAR----IISIDKevlRTGDRALvrfrflYRPEYLREGQ 69
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 17-123 1.17e-04

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


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 42.19  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443496589  17 DG---QTREHALLAFTLGVRQLIVAVNKMDTTKwsEERFLEICK-ETSNFIKKVGYNPKTVAFVPISGWhgdNMLEPSEN 92
Cdd:cd01884  100 DGpmpQTREHLLLARQVGVPYIVVFLNKADMVD--DEELLELVEmEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDP 174

                         90       100       110
                 ....*....|....*....|....*....|..
gi 443496589  93 MTWYKgwtrdgktgslKGKTLLDAIDA-IEPP 123
Cdd:cd01884  175 NKWVD-----------KILELLDALDSyIPTP 195
 
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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