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Conserved domains on  [gi|1218187414|gb|ASM61839|]
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elongation factor 1-alpha, partial [Wohlfahrtia bella]

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 ...
 1-231 7.43e-162

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: 454.98  E-value: 7.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:PTZ00141  199 DNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSKASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:PTZ00141  267 TFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYT 346

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:PTZ00141  347 PVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-231 7.43e-162

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 454.98  E-value: 7.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:PTZ00141  199 DNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSKASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:PTZ00141  267 TFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYT 346

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:PTZ00141  347 PVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-231 3.23e-122

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: 353.40  E-value: 3.23e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:TIGR00483 193 DNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKV 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSKaSPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:TIGR00483 261 VFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYT 339

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:TIGR00483 340 PVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDM 410
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-231 8.17e-122

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: 352.31  E-value: 8.17e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:COG5256   190 DNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSkASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:COG5256   258 VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYT 336

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:COG5256   337 PVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDM 407
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 137-231 4.27e-68

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: 204.35  E-value: 4.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 137 KGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEA 216
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                          90
                  ....*....|....*
gi 1218187414 217 FQEFPPLGRFAVRDM 231
Cdd:cd03705    81 FSEYPPLGRFAVRDM 95
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 135-231 1.94e-32

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: 113.51  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 135 PPKGAADFTAQVIVLNH-----PGQISNGYTPVLDCHTAHIACKFAEIKEKVDrrSGKTTeENPKFIKSGDAAIVNLVPS 209
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVS-ENPEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|..
gi 1218187414 210 KPLCVEAFQefpplgRFAVRDM 231
Cdd:pfam03143  78 KPIALEKGQ------RFAIREG 93
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-231 7.43e-162

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 454.98  E-value: 7.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:PTZ00141  199 DNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSKASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:PTZ00141  267 TFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYT 346

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:PTZ00141  347 PVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-231 3.23e-122

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: 353.40  E-value: 3.23e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:TIGR00483 193 DNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKV 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSKaSPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:TIGR00483 261 VFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYT 339

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:TIGR00483 340 PVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDM 410
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-231 8.17e-122

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: 352.31  E-value: 8.17e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:COG5256   190 DNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSkASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:COG5256   258 VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYT 336

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:COG5256   337 PVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDM 407
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-231 1.04e-119

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 346.91  E-value: 1.04e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:PRK12317  191 DNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKV 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGdSKASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:PRK12317  259 VFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYT 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:PRK12317  338 PVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVKEIPQLGRFAIRDM 408
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-231 5.93e-116

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 338.60  E-value: 5.93e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 80
Cdd:PLN00043  199 DNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  81 VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAGDSKASPPKGAADFTAQVIVLNHPGQISNGYT 160
Cdd:PLN00043  267 TFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYA 346

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 161 PVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDM 231
Cdd:PLN00043  347 PVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYPPLGRFAVRDM 417
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 137-231 4.27e-68

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: 204.35  E-value: 4.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 137 KGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEA 216
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                          90
                  ....*....|....*
gi 1218187414 217 FQEFPPLGRFAVRDM 231
Cdd:cd03705    81 FSEYPPLGRFAVRDM 95
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 44-132 1.87e-59

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: 182.00  E-value: 1.87e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  44 TEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELR 123
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80


                  ....*....
gi 1218187414 124 RGYVAGDSK 132
Cdd:cd03693    81 RGDVAGDSK 89
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 135-231 1.94e-32

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: 113.51  E-value: 1.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 135 PPKGAADFTAQVIVLNH-----PGQISNGYTPVLDCHTAHIACKFAEIKEKVDrrSGKTTeENPKFIKSGDAAIVNLVPS 209
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVS-ENPEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|..
gi 1218187414 210 KPLCVEAFQefpplgRFAVRDM 231
Cdd:pfam03143  78 KPIALEKGQ------RFAIREG 93
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-226 1.24e-30

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: 117.11  E-value: 1.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGwkverkegnaegKTLIDALDAILPPSRPTEKPLRLPLQDVYKiggigtvP-------VGRVETGV 73
Cdd:COG2895   198 DNVVERSENMPWYDG------------PTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGT 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  74 LKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVK---NVSvkelrRGYVAGDSkASPPKGAADFTAQVIVLN 150
Cdd:COG2895   259 VRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS-----RGDVIVAA-DAPPEVADQFEATLVWMD 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 151 -HPGQISNGYtpVLDCHTAHIACKFAEIKEKVD-----RRSGKTTEENpkfiksgDAAIVNLVPSKPLCVEAFQEFPPLG 224
Cdd:COG2895   333 eEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDvntleHEAADSLELN-------DIGRVTLRLAEPIAFDPYADNRATG 403


                  ..
gi 1218187414 225 RF 226
Cdd:COG2895   404 SF 405
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 142-231 3.09e-27

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: 100.16  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 142 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKttEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFP 221
Cdd:cd01513     6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGKEFP 83

                          90
                  ....*....|
gi 1218187414 222 PLGRFAVRDM 231
Cdd:cd01513    84 TLGRFALRDG 93
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 142-230 4.14e-24

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: 92.23  E-value: 4.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 142 FTAQVIVLNHPGQI-SNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEF 220
Cdd:cd03704     6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85

                          90
                  ....*....|
gi 1218187414 221 PPLGRFAVRD 230
Cdd:cd03704    86 PQLGRFTLRD 95
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 48-127 9.10e-21

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: 82.70  E-value: 9.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  48 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNvsVKELRRGYV 127
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
tufA CHL00071
elongation factor Tu
 29-150 1.19e-19

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 86.55  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  29 TLIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TVVVFAPANITTeVKSVEMHHEALAEA 104
Cdd:CHL00071  201 NLMDAVDSYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRETKTTT-VTGLEMFQKTLDEG 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1218187414 105 VPGDNVGFNVKNVSVKELRRGYVAGDSKASPPKgaADFTAQVIVLN 150
Cdd:CHL00071  280 LAGDNVGILLRGIQKEDIERGMVLAKPGTITPH--TKFEAQVYILT 323
PLN03126 PLN03126
Elongation factor Tu; Provisional
 30-230 5.78e-19

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 84.67  E-value: 5.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV--VFAPANITTEVKSVEMHHEALAEAVP 106
Cdd:PLN03126  271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdiVGLRETRSTTVTGVEMFQKILDEALA 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 107 GDNVGFNVKNVSVKELRRGYVAgdSKASPPKGAADFTAQVIVLNHP--GQIS---NGYTPVLDCHTAHIACKFAEIKEKV 181
Cdd:PLN03126  351 GDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDK 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1218187414 182 DrrsgktteENPKFIKSGDAA--IVNLVpsKPLCVEAFQefpplgRFAVRD 230
Cdd:PLN03126  429 D--------EESKMVMPGDRVkmVVELI--VPVACEQGM------RFAIRE 463
PLN03127 PLN03127
Elongation factor Tu; Provisional
 30-230 6.02e-19

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 84.49  E-value: 6.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TVVVFAP-ANITTEVKSVEMHHEALAEA 104
Cdd:PLN03127  243 LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 105 VPGDNVGFNVKNVSVKELRRGYVAgdSKASPPKGAADFTAQVIVLN------HPGQISNgYTPVLDCHTAHIACKFaeik 178
Cdd:PLN03127  323 QAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADVTGKV---- 395

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1218187414 179 ekvdrrsgkTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQefpplgRFAVRD 230
Cdd:PLN03127  396 ---------ELPEGVKMVMPGDNVTAVFELISPVPLEPGQ------RFALRE 432
PRK00049 PRK00049
elongation factor Tu; Reviewed
 30-149 1.28e-18

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 83.31  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV--VFAPANITTEVKSVEMHHEALAEAVP 106
Cdd:PRK00049  194 LMDAVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVeiVGIRDTQKTTVTGVEMFRKLLDEGQA 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1218187414 107 GDNVGFNVKNVSVKELRRGYVAgdSKASPPKGAADFTAQVIVL 149
Cdd:PRK00049  274 GDNVGALLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
PRK12735 PRK12735
elongation factor Tu; Reviewed
 30-149 1.28e-18

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 83.35  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV--VFAPANITTEVKSVEMHHEALAEAVP 106
Cdd:PRK12735  194 LMDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVeiVGIKETQKTTVTGVEMFRKLLDEGQA 273

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1218187414 107 GDNVGFNVKNVSVKELRRGYVAgdSKASPPKGAADFTAQVIVL 149
Cdd:PRK12735  274 GDNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 48-127 3.59e-18

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: 76.03  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  48 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYV 127
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 9-149 5.50e-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: 81.75  E-value: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   9 NMPWFKGWKVERKEGNAEGKT----LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV--V 81
Cdd:TIGR00485 167 DTPIIRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVeiV 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1218187414  82 FAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYVAgdSKASPPKGAADFTAQVIVL 149
Cdd:TIGR00485 247 GLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVL 312
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 30-149 8.55e-18

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: 80.96  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---VVVFAPANITTeVKSVEMHHEALAEAV 105
Cdd:COG0050   194 LMDAVDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDeveIVGIRDTQKTV-VTGVEMFRKLLDEGE 272

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1218187414 106 PGDNVGFNVKNVSVKELRRGYVAgdSKASPPKGAADFTAQVIVL 149
Cdd:COG0050   273 AGDNVGLLLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 30-149 1.45e-17

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 80.37  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAILP-PSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV--VFAPANITTEVKSVEMHHEALAEAVP 106
Cdd:PRK12736  192 LMDAVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVeiVGIKETQKTVVTGVEMFRKLLDEGQA 271

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1218187414 107 GDNVGFNVKNVSVKELRRGYVAGDSKASPPkgAADFTAQVIVL 149
Cdd:PRK12736  272 GDNVGVLLRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYIL 312
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 135-230 3.36e-17

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: 74.12  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 135 PPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCV 214
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80

                          90
                  ....*....|....*.
gi 1218187414 215 EAFQEFPPLGRFAVRD 230
Cdd:cd04093    81 ETFKDNKELGRFVLRR 96
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 50-127 6.45e-16

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: 70.24  E-value: 6.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  50 LPLQDVYKIGGIGTVPVGRVETGVLKPGTVV--VFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYV 127
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVeiVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 62-127 1.24e-15

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 69.22  E-value: 1.24e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1218187414  62 GTVPVGRVETGVLKPGTVVVFAPA-----NITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYV 127
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 ...
 47-130 2.77e-15

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: 68.31  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  47 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGY 126
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80


                  ....
gi 1218187414 127 VAGD 130
Cdd:cd16267    81 ILCD 84
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 30-127 3.09e-15

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: 74.18  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  30 LIDALDAIL--PPSRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPG 107
Cdd:COG3276   157 LRAALDALAaaVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAG 236

                          90       100
                  ....*....|....*....|
gi 1218187414 108 DNVGFNVKNVSVKELRRGYV 127
Cdd:COG3276   237 QRVALNLAGVEKEEIERGDV 256
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-230 3.31e-12

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 65.34  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFkgwkverkegnaEGKTLIDALDAILPPSRPTEKPLRLPLQDVYKI-----GGIGTVPvgrveTGVLK 75
Cdd:PRK05506  207 DNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGTVA-----SGVVR 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  76 PGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKN---VSvkelrRGYV---AGDskasPPKGAADFTAQVIVL 149
Cdd:PRK05506  270 PGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS-----RGDMlarADN----RPEVADQFDATVVWM 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414 150 N----HPGqisNGYtpVLDCHTAHIACKFAEIKEKVD-----RRSGKTTEENpkfiksgDAAIVNLVPSKPLCVEAFQEF 220
Cdd:PRK05506  341 AeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDvntleRLAAKTLELN-------EIGRCNLSTDAPIAFDPYARN 408

                         250
                  ....*....|
gi 1218187414 221 PPLGRFAVRD 230
Cdd:PRK05506  409 RTTGSFILID 418
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 47-127 8.12e-12

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


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 59.04  E-value: 8.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  47 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGY 126
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 1218187414 127 V 127
Cdd:cd04089    79 V 79
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 47-130 1.30e-11

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: 58.67  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414  47 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMH-HEALAEAVPGDNVGFNVKNVSVKELRRG 125
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 1218187414 126 YVAGD 130
Cdd:cd03698    80 DILSS 84
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 54-127 6.19e-10

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: 54.15  E-value: 6.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1218187414  54 DVYKIGGIGTVPVGRVETGVLKPGTVVVFAPAN----ITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSVKELRRGYV 127
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 48-112 8.20e-09

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 51.03  E-value: 8.20e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1218187414  48 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGF 112
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-110 8.81e-07

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 48.76  E-value: 8.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFkgwkverkegnaEGKTLIDALDAILPPSRPTEKPLRLPLQDVYKI-----GGIGTvpvgrVETGVLK 75
Cdd:PRK05124  211 DNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVK 273

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1218187414  76 PGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNV 110
Cdd:PRK05124  274 VGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-40 7.05e-06

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: 45.56  E-value: 7.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1218187414   1 DNMLEASTNMPWFKGWkverkegnaegkTLIDALDAILPP 40
Cdd:cd01883   191 DNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 53-111 7.34e-05

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: 39.97  E-value: 7.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1218187414  53 QDVYKIGGiGTVPVGRVETGVLKPGTVVVfaPANITTEVKSVEMHHEALAEAVPGDNVG 111
Cdd:cd16265     6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 142-204 1.61e-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: 1.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1218187414 142 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIkekvdrrsgktteeNPKFIKSGDAAIV 204
Cdd:cd03708     6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISI--------------DKEVLRTGDRALV 54
IF2_aeIF5B_IV cd16266
Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ...
 66-119 3.57e-03

Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents the domain IV of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologs IF5B. IF2, the largest initiation factor is an essential GTP binding protein. In E. coli three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.


Pssm-ID: 293911 [Multi-domain]  Cd Length: 87  Bit Score: 35.60  E-value: 3.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1218187414  66 VG-RVETGVLKPGTVVVFAPANITTEVKSVEMHHEALAEAVPGDNVGFNVKNVSV 119
Cdd:cd16266    19 VGvEVLEGTLKPGVPLIVPDGKDVGRVKSIQDNGENVKEAKKGQEVAVSIEGPTV 73
 
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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