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Conserved domains on  [gi|1368344005|gb|AVP50019|]
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elongation factor 1-alpha, partial [Didymium umbilicatum]

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 ...
 1-206 9.81e-153

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: 430.71  E-value: 9.81e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:PTZ00141  167 YDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGG 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRECE 160
Cdd:PTZ00141  247 IGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECA 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:PTZ00141  327 DFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSG 372
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-206 9.81e-153

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 430.71  E-value: 9.81e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:PTZ00141  167 YDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGG 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRECE 160
Cdd:PTZ00141  247 IGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECA 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:PTZ00141  327 DFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSG 372
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-206 1.18e-111

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: 325.66  E-value: 1.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:TIGR00483 161 FEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQDVYSITG 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKqDPPRECE 160
Cdd:TIGR00483 241 VGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPD-NPPKVAK 319

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:TIGR00483 320 EFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTG 365
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-206 1.39e-111

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: 325.35  E-value: 1.39e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:COG5256   158 YEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISG 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSkQDPPRECE 160
Cdd:COG5256   238 IGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DNPPTVAE 316

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:COG5256   317 EFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTG 362
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 64-154 7.95e-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: 179.69  E-value: 7.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  64 SDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIR 143
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1368344005 144 RGMVAGDSKQD 154
Cdd:cd03693    81 RGDVAGDSKND 91
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 155-202 1.67e-16

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: 71.91  E-value: 1.67e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1368344005 155 PPRECESFTAQVIILNH-----PGQIHAGYAPVLDCHTAHIACKFSELLDKVD 202
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD 53
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-206 9.81e-153

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 430.71  E-value: 9.81e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:PTZ00141  167 YDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKGPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGG 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRECE 160
Cdd:PTZ00141  247 IGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECA 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:PTZ00141  327 DFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSG 372
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-206 1.84e-118

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 343.61  E-value: 1.84e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:PLN00043  167 YDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGG 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRECE 160
Cdd:PLN00043  247 IGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAA 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:PLN00043  327 NFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSG 372
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-206 1.18e-111

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: 325.66  E-value: 1.18e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:TIGR00483 161 FEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKGKTLLEALDALEPPEKPTDKPLRIPIQDVYSITG 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKqDPPRECE 160
Cdd:TIGR00483 241 VGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPD-NPPKVAK 319

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:TIGR00483 320 EFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTG 365
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-206 1.39e-111

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: 325.35  E-value: 1.39e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:COG5256   158 YEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPTLLEALDNLKEPEKPVDKPLRIPIQDVYSISG 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSkQDPPRECE 160
Cdd:COG5256   238 IGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP-DNPPTVAE 316

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:COG5256   317 EFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTG 362
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-206 2.10e-109

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 319.95  E-value: 2.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKIGG 80
Cdd:PRK12317  159 YEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPTLLEALDNLKPPEKPTDKPLRIPIQDVYSISG 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 IGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGdSKQDPPRECE 160
Cdd:PRK12317  239 VGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAE 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 161 SFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:PRK12317  318 EFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTG 363
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 64-154 7.95e-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: 179.69  E-value: 7.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  64 SDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIR 143
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1368344005 144 RGMVAGDSKQD 154
Cdd:cd03693    81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-202 3.27e-38

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: 136.37  E-value: 3.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYnpEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKigg 80
Cdd:COG2895   168 FEEIVADYRAFAAKLGL--EDITFIPISALKGDNVVERSENMPWYDGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR--- 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  81 igtvP-------VGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGfnvknLSVK---DIRRG-MVAg 149
Cdd:COG2895   243 ----PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVT-----LTLEdeiDISRGdVIV- 312

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1368344005 150 dSKQDPPRECESFTAQVIILN-HPGQIHAGYapVLDCHTAHIACKFSELLDKVD 202
Cdd:COG2895   313 -AADAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRID 363
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 157-206 8.61e-33

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 113.83  E-value: 8.61e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1368344005 157 RECESFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTG 50
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-61 3.26e-31

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: 113.35  E-value: 3.26e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPK 61
Cdd:cd01883   159 YDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPTLLEALDSLEPPE 219
GTPBP1 COG5258
GTPase [General function prediction only];
51-206 2.15e-29

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 113.88  E-value: 2.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  51 LEALDSIVE--PKR--PSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLS----TEVKSVEMHHVALP 122
Cdd:COG5258   330 LDLLDELFErlPKRatDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIGPTKDGsfreVEVKSIEMHYHRVD 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005 123 EAQPGDNVGFNVKNLSVKDIRRGMVAGDSKQDpPRECESFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFsELLDKVD 202
Cdd:COG5258   410 KAEAGRIVGIALKGVEEEELERGMVLLPRDAD-PKAVREFEAEVMVLNHPTTIKEGYEPVVHLETISEAVRF-EPIDKGY 487


                  ....
gi 1368344005 203 RRTG 206
Cdd:COG5258   488 LLPG 491
PRK12735 PRK12735
elongation factor Tu; Reviewed
 29-169 3.84e-22

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 92.59  E-value: 3.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  29 GFNGDNM----------LEKSANLPWYKG-PTLLEALDS-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKP 96
Cdd:PRK12735  162 DFPGDDTpiirgsalkaLEGDDDEEWEAKiLELMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKV 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1368344005  97 N---MIVTFAPgNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRecESFTAQVIIL 169
Cdd:PRK12735  242 GdevEIVGIKE-TQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPH--TKFEAEVYVL 314
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 29-169 5.18e-22

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: 92.14  E-value: 5.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  29 GFNGDNM----------LEKSANLPWYKGPT-LLEALDS-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKP 96
Cdd:COG0050   162 GFPGDDTpiirgsalkaLEGDPDPEWEKKILeLMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKV 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1368344005  97 N---MIVTFAPGnLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAgdSKQDPPRECESFTAQVIIL 169
Cdd:COG0050   242 GdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
PRK00049 PRK00049
elongation factor Tu; Reviewed
 29-147 1.02e-21

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.40  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  29 GFNGDNM----------LEKSANLPWYKG-PTLLEALDS-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKP 96
Cdd:PRK00049  162 DFPGDDTpiirgsalkaLEGDDDEEWEKKiLELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKV 241

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1368344005  97 N---MIVTFAPgNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMV 147
Cdd:PRK00049  242 GeevEIVGIRD-TQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-167 2.54e-21

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 91.14  E-value: 2.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYnpEKINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSI-VEPKRpSDKPLRVPLQDVYKI- 78
Cdd:PRK05506  177 FDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPSLLEHLETVeIASDR-NLKDFRFPVQYVNRPn 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  79 ----GGIGTvpvgrVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVgfnvkNLSVKD---IRRG-MVAgd 150
Cdd:PRK05506  254 ldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRGdMLA-- 321

                         170
                  ....*....|....*..
gi 1368344005 151 SKQDPPRECESFTAQVI 167
Cdd:PRK05506  322 RADNRPEVADQFDATVV 338
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-167 6.92e-21

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 89.59  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPEkINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKI-- 78
Cdd:PRK05124  180 FERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYSGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnl 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  79 ---GGIGTvpvgrVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVgfnvkNLSVK---DIRRG--MVAGD 150
Cdd:PRK05124  259 dfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI-----TLVLEdeiDISRGdlLVAAD 328

                         170
                  ....*....|....*..
gi 1368344005 151 SKQDPPReceSFTAQVI 167
Cdd:PRK05124  329 EALQAVQ---HASADVV 342
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-167 1.76e-20

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: 87.81  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   1 YDEIVKETSSFVKKIGYNPekINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSIVEPKRPSDKPLRVPLQDVYKI-- 78
Cdd:TIGR02034 153 FENIKKDYLAFAEQLGFRD--VTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnl 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  79 ---GGIGTVPVGRVETGilkpnMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNlsVKDIRRG--MVAGDSkq 153
Cdd:TIGR02034 231 dfrGYAGTIASGSVHVG-----DEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDD--EIDISRGdlLAAADS-- 301

                         170
                  ....*....|....
gi 1368344005 154 dPPRECESFTAQVI 167
Cdd:TIGR02034 302 -APEVADQFAATLV 314
tufA CHL00071
elongation factor Tu
 3-170 7.80e-20

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 86.16  E-value: 7.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005   3 EIVK-ETSSFVKKIGYNPEKINFVPISGFNGDNMLEKSANL-----PWY-KGPTLLEALDS-IVEPKRPSDKPLRVPLQD 74
Cdd:CHL00071  148 ELVElEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgenKWVdKIYNLMDAVDSyIPTPERDTDKPFLMAIED 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  75 VYKIGGIGTVPVGRVETGILKPN---MIVTFAPGNlSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMVAGDS 151
Cdd:CHL00071  228 VFSITGRGTVATGRIERGTVKVGdtvEIVGLRETK-TTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKP 306

                         170
                  ....*....|....*....
gi 1368344005 152 KQDPPRecESFTAQVIILN 170
Cdd:CHL00071  307 GTITPH--TKFEAQVYILT 323
PLN03127 PLN03127
Elongation factor Tu; Provisional
 50-170 1.11e-19

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 86.03  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  50 LLEALDS-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPN---MIVTFAP-GNLSTEVKSVEMHHVALPEA 124
Cdd:PLN03127  243 LMDAVDEyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQG 322

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1368344005 125 QPGDNVGFNVKNLSVKDIRRGMVAgdSKQDPPRECESFTAQVIILN 170
Cdd:PLN03127  323 QAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLT 366
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 71-147 1.52e-19

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 79.10  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  71 PLQDVYKIGGIGTVPVGRVETGILKPNM---IVTFAPgNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMV 147
Cdd:cd03697     4 PIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 68-147 6.48e-19

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 77.30  E-value: 6.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  68 LRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNlsVKDIRRGMV 147
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-57 1.13e-17

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: 77.61  E-value: 1.13e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1368344005   1 YDEIVKETSSFVKKIGYNPekINFVPISGFNGDNMLEKSANLPWYKGPTLLEALDSI 57
Cdd:cd04166   151 FEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETV 205
PRK12736 PRK12736
elongation factor Tu; Reviewed
 50-169 1.67e-17

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 79.60  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  50 LLEALDS-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPN---MIVTFAPgNLSTEVKSVEMHHVALPEAQ 125
Cdd:PRK12736  192 LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKE-TQKTVVTGVEMFRKLLDEGQ 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1368344005 126 PGDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRecESFTAQVIIL 169
Cdd:PRK12736  271 AGDNVGVLLRGVDRDEVERGQVLAKPGSIKPH--TKFKAEVYIL 312
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 50-147 2.30e-17

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: 79.05  E-value: 2.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  50 LLEALDS-IVEPKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPN---MIVTFAPGNLSTeVKSVEMHHVALPEAQ 125
Cdd:TIGR00485 192 LMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGR 270

                          90       100
                  ....*....|....*....|..
gi 1368344005 126 PGDNVGFNVKNLSVKDIRRGMV 147
Cdd:TIGR00485 271 AGDNVGLLLRGIKREEIERGMV 292
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 155-202 1.67e-16

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: 71.91  E-value: 1.67e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1368344005 155 PPRECESFTAQVIILNH-----PGQIHAGYAPVLDCHTAHIACKFSELLDKVD 202
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD 53
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 68-147 3.22e-16

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 70.25  E-value: 3.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  68 LRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMV 147
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
PLN03126 PLN03126
Elongation factor Tu; Provisional
 50-202 5.06e-16

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 75.42  E-value: 5.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  50 LLEALDSIVE-PKRPSDKPLRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFA--PGNLSTEVKSVEMHHVALPEAQP 126
Cdd:PLN03126  271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVglRETRSTTVTGVEMFQKILDEALA 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005 127 GDNVGFNVKNLSVKDIRRGMVAGDSKQDPPRecESFTAQVIIL-NHPGQIH----AGYAPVLDCHTAHIACKFSELLDKV 201
Cdd:PLN03126  351 GDNVGLLLRGIQKADIQRGMVLAKPGSITPH--TKFEAIVYVLkKEEGGRHspffAGYRPQFYMRTTDVTGKVTSIMNDK 428


                  .
gi 1368344005 202 D 202
Cdd:PLN03126  429 D 429
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 82-147 6.52e-16

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 69.22  E-value: 6.52e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1368344005  82 GTVPVGRVETGILKPNMIVTFAPG-----NLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMV 147
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 74-147 1.53e-13

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: 63.39  E-value: 1.53e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1368344005  74 DVYKIGGIGTVPVGRVETGILKPNMIVTFAP---GN-LSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGMV 147
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdadGKfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 67-147 8.38e-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: 58.65  E-value: 8.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  67 PLRVPLQDVYKigGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGFNVKNLSVKDIRRGM 146
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 1368344005 147 V 147
Cdd:cd04089    79 V 79
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 67-142 1.63e-10

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: 55.21  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  67 PLRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNV-----GFNVKNLSVKD 141
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVtltltGIDPNHLRVGS 80


                  .
gi 1368344005 142 I 142
Cdd:cd16267    81 I 81
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 159-206 1.85e-10

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


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 55.86  E-value: 1.85e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1368344005 159 CESFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:cd01513     3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTK 50
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 67-150 3.43e-08

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: 49.04  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1368344005  67 PLRVPLQDVYKiGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMH-HVALPEAQPGDNVGFNVKNLSVKDIRRG 145
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 1368344005 146 MVAGD 150
Cdd:cd03698    80 DILSS 84
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 68-132 8.44e-07

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: 45.25  E-value: 8.44e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1368344005  68 LRVPLQDVYKIGGIGTVPVGRVETGILKPNMIVTFAPGNLSTEVKSVEMHHVALPEAQPGDNVGF 132
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-60 3.67e-06

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: 45.59  E-value: 3.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1368344005   1 YDEIVKETSS-FVKKIGYNPEKINFVPISGFNGDNMleksanlpwykgPTLLEALDSIVEP 60
Cdd:pfam00009 139 LEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV------------QTLLDALDEYLPS 187
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 157-206 2.83e-05

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


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 41.77  E-value: 2.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1368344005 157 RECESFTAQVIILNHPGQI-HAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:cd03704     1 PVVTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTG 51
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 159-206 5.08e-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: 5.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1368344005 159 CESFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDrRTG 206
Cdd:cd03708     3 CWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVL-RTG 49
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 155-206 2.28e-03

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


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 36.37  E-value: 2.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1368344005 155 PPRECESFTAQVIILNHPGQIHAGYAPVLDCHTAHIACKFSELLDKVDRRTG 206
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTG 52
 
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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