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Conserved domains on  [gi|56377824|dbj|BAD74131|]
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elongation factor-1 alpha, partial [Symmetrospora gracilis]

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 ...
 1-230 3.13e-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: 433.02  E-value: 3.13e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPW------------YKGPTLLEALDTLEPPKRP 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:PTZ00141 230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  161 RGNVCGDSKQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:PTZ00141 310 RGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-230 3.13e-153

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 433.02  E-value: 3.13e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPW------------YKGPTLLEALDTLEPPKRP 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:PTZ00141 230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  161 RGNVCGDSKQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:PTZ00141 310 RGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-230 4.64e-121

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: 350.70  E-value: 4.64e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824     1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:TIGR00483 156 YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPW------------YKGKTLLEALDALEPPEKP 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:TIGR00483 224 TDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIR 303

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   161 RGNVCGDSKqDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:TIGR00483 304 RGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENP 372
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-230 6.28e-112

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: 327.28  E-value: 6.28e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:COG5256 153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW------------YNGPTLLEALDNLKEPEKP 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:COG5256 221 VDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIK 300

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824 161 RGNVCGDSkQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:COG5256 301 RGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENP 369
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 81-171 1.24e-61

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 187.40  E-value: 1.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:cd03693   1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                        90
                ....*....|.
gi 56377824 161 RGNVCGDSKQD 171
Cdd:cd03693  81 RGDVAGDSKND 91
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 172-219 5.02e-17

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: 73.84  E-value: 5.02e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56377824   172 PPKEAASFNAQVIVLNH-----PGQIGNGYSPVLDCHTAHIACKFDTLLEKID 219
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD 53
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-230 3.13e-153

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 433.02  E-value: 3.13e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:PTZ00141 162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPW------------YKGPTLLEALDTLEPPKRP 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:PTZ00141 230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  161 RGNVCGDSKQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:PTZ00141 310 RGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-230 4.64e-121

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: 350.70  E-value: 4.64e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824     1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:TIGR00483 156 YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPW------------YKGKTLLEALDALEPPEKP 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:TIGR00483 224 TDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIR 303

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   161 RGNVCGDSKqDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:TIGR00483 304 RGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENP 372
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-230 2.26e-114

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 334.37  E-value: 2.26e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:PLN00043 162 YSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDW------------YKGPTLLEALDQINEPKRP 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:PLN00043 230 SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLK 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  161 RGNVCGDSKQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:PLN00043 310 RGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEP 379
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-230 4.30e-112

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 327.65  E-value: 4.30e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:PRK12317 154 YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPW------------YNGPTLLEALDNLKPPEKP 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:PRK12317 222 TDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIK 301

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  161 RGNVCGdSKQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:PRK12317 302 RGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENP 370
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-230 6.28e-112

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: 327.28  E-value: 6.28e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:COG5256 153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW------------YNGPTLLEALDNLKEPEKP 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:COG5256 221 VDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIK 300

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824 161 RGNVCGDSkQDPPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:COG5256 301 RGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENP 369
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 81-171 1.24e-61

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 187.40  E-value: 1.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  81 TDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIR 160
Cdd:cd03693   1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                        90
                ....*....|.
gi 56377824 161 RGNVCGDSKQD 171
Cdd:cd03693  81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-219 6.69e-40

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: 141.76  E-value: 6.69e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   1 WSEARYEEIVKETSNFIKKVGFNPKTvpFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:COG2895 163 YSEEVFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPW------------YDGPTLLEHLETVEVAEDR 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  81 TDKPLRLPLQDVYKiggigtvP-------VGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGF---- 149
Cdd:COG2895 229 NDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtled 301

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56377824 150 NIknvsvkDIRRGNVCGDSkQDPPKEAASFNAQVIVLN-HPGQIGNGYspVLDCHTAHIACKFDTLLEKID 219
Cdd:COG2895 302 EI------DISRGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRID 363
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 174-230 5.56e-34

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: 117.68  E-value: 5.56e-34
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56377824 174 KEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:cd03705   1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENP 57
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-78 2.10e-32

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: 117.21  E-value: 2.10e-32
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56377824   1 WSEARYEEIVKETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQ 78
Cdd:cd01883 154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPW------------YKGPTLLEALDSLEPPE 219
tufA CHL00071
elongation factor Tu
 8-187 3.10e-25

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 101.96  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    8 EIVK-ETSNFIKKVGFNPKTVPFVPISGWHGDNMLEESTNMGwfKGWKKEVKsgeyKGKTLLEAIDS-IEPPQRPTDKPL 85
Cdd:CHL00071 148 ELVElEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIK--RGENKWVD----KIYNLMDAVDSyIPTPERDTDKPF 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   86 RLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVT---FAPSAVTTeVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRG 162
Cdd:CHL00071 222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERG 300

                        170       180
                 ....*....|....*....|....*
gi 56377824  163 NVCgdSKQDPPKEAASFNAQVIVLN 187
Cdd:CHL00071 301 MVL--AKPGTITPHTKFEAQVYILT 323
PRK00049 PRK00049
elongation factor Tu; Reviewed
 67-186 4.06e-22

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 93.33  E-value: 4.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   67 LLEAIDS-IEPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MVVTFAPSAVTTeVKSVEMHHEQLEAGL 142
Cdd:PRK00049 194 LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQ 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 56377824  143 PGDNVGFNIKNVSVKDIRRGNVCgdSKQDPPKEAASFNAQVIVL 186
Cdd:PRK00049 273 AGDNVGALLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
PRK12735 PRK12735
elongation factor Tu; Reviewed
 67-186 8.88e-22

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 92.21  E-value: 8.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   67 LLEAIDS-IEPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MVVTFAPSAVTTeVKSVEMHHEQLEAGL 142
Cdd:PRK12735 194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQ 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 56377824  143 PGDNVGFNIKNVSVKDIRRGNVCgdSKQDPPKEAASFNAQVIVL 186
Cdd:PRK12735 273 AGDNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 67-198 5.17e-21

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: 90.21  E-value: 5.17e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  67 LLEAIDS-IEPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MVVTFAPSAVTTeVKSVEMHHEQLEAGL 142
Cdd:COG0050 194 LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDTQKTV-VTGVEMFRKLLDEGE 272

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56377824 143 PGDNVGFNIKNVSVKDIRRGNV-CGDSKQDPPKEaasFNAQVIVLN-------HPgqIGNGYSP 198
Cdd:COG0050 273 AGDNVGLLLRGIKREDVERGQVlAKPGSITPHTK---FEAEVYVLSkeeggrhTP--FFNGYRP 331
PLN03127 PLN03127
Elongation factor Tu; Provisional
 67-219 1.08e-20

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 89.50  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   67 LLEAIDSIEP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MVVTFAPSA-VTTEVKSVEMHHEQLEAG 141
Cdd:PLN03127 243 LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQG 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  142 LPGDNVGFNIKNVSVKDIRRGNVCgdSKQDPPKEAASFNAQVIVLN------HPGQIGNgYSPVLDCHTAHIACKFdTLL 215
Cdd:PLN03127 323 QAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADVTGKV-ELP 398


                 ....
gi 56377824  216 EKID 219
Cdd:PLN03127 399 EGVK 402
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-184 1.28e-20

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 89.60  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    1 WSEARYEEIVKETSNFIKKVGFNpkTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRP 80
Cdd:PRK05506 172 YDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPW------------YEGPSLLEHLETVEIASDR 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   81 TDKPLRLPLQDVYKI-----GGIGTvpvgrVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVgfnikNVS 155
Cdd:PRK05506 238 NLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLT 307

                        170       180       190
                 ....*....|....*....|....*....|..
gi 56377824  156 VKD---IRRGNVCGDSkQDPPKEAASFNAQVI 184
Cdd:PRK05506 308 LADeidISRGDMLARA-DNRPEVADQFDATVV 338
PRK12736 PRK12736
elongation factor Tu; Reviewed
 67-186 1.78e-20

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 88.46  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   67 LLEAIDS-IEPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MVVTFAPSaVTTEVKSVEMHHEQLEAGL 142
Cdd:PRK12736 192 LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQ 270

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 56377824  143 PGDNVGFNIKNVSVKDIRRGNV-CGDSKQDPPKEaasFNAQVIVL 186
Cdd:PRK12736 271 AGDNVGVLLRGVDRDEVERGQVlAKPGSIKPHTK---FKAEVYIL 312
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 85-166 4.25e-20

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


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 81.16  E-value: 4.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  85 LRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNvsVKDIRRGNV 164
Cdd:cd01342   1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78


                ..
gi 56377824 165 CG 166
Cdd:cd01342  79 LT 80
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 60-186 1.39e-19

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: 85.98  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    60 GEYKGKT--LLEAIDS-IEPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAG---MVVTFAPSAVTTeVKSVEM 133
Cdd:TIGR00485 183 AEWEAKIleLMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEM 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56377824   134 HHEQLEAGLPGDNVGFNIKNVSVKDIRRGNVCgdSKQDPPKEAASFNAQVIVL 186
Cdd:TIGR00485 262 FRKELDEGRAGDNVGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVL 312
PLN03126 PLN03126
Elongation factor Tu; Provisional
 54-198 1.79e-19

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 86.21  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   54 KKEVKSGEYKG----KTLLEAIDSIEP-PQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVT--T 126
Cdd:PLN03126 254 NPNIKRGDNKWvdkiYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsT 333

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56377824  127 EVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRGNVCgdSKQDPPKEAASFNAQVIVLNHpgQIGNGYSP 198
Cdd:PLN03126 334 TVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYVLKK--EEGGRHSP 401
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 85-165 2.26e-17

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


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 74.10  E-value: 2.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  85 LRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRGNV 164
Cdd:cd03696   1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80


                .
gi 56377824 165 C 165
Cdd:cd03696  81 L 81
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-184 3.11e-17

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 79.57  E-value: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824    2 SEARYEEIVKETSNFIKKVGFNPkTVPFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQRPT 81
Cdd:PRK05124 176 SEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPW------------YSGPTLLEVLETVDIQRVVD 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824   82 DKPLRLPLQDVYKI-----GGIGTvpvgrVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSv 156
Cdd:PRK05124 243 AQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI- 316

                        170       180
                 ....*....|....*....|....*...
gi 56377824  157 kDIRRGNVCGDSkQDPPKEAASFNAQVI 184
Cdd:PRK05124 317 -DISRGDLLVAA-DEALQAVQHASADVV 342
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 87-164 4.96e-17

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 73.32  E-value: 4.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  87 LPLQDVYKIGGIGTVPVGRVETGTIKAGM---VVTFAPSaVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRGN 163
Cdd:cd03697   3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKET-LKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81


                .
gi 56377824 164 V 164
Cdd:cd03697  82 V 82
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 172-219 5.02e-17

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: 73.84  E-value: 5.02e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 56377824   172 PPKEAASFNAQVIVLNH-----PGQIGNGYSPVLDCHTAHIACKFDTLLEKID 219
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD 53
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 67-164 5.82e-16

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: 76.11  E-value: 5.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  67 LLEAIDSI--EPPQRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPG 144
Cdd:COG3276 157 LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAG 236

                        90       100
                ....*....|....*....|
gi 56377824 145 DNVGFNIKNVSVKDIRRGNV 164
Cdd:COG3276 237 QRVALNLAGVEKEEIERGDV 256
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-78 3.09e-15

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: 71.45  E-value: 3.09e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56377824   1 WSEARYEEIVKETSNFIKKVGFNPKTvpFVPISGWHGDNMLEESTNMGWfkgwkkevksgeYKGKTLLEAIDSIEPPQ 78
Cdd:cd04166 146 YDEEVFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPW------------YKGPTLLEHLETVEIAS 209
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 99-164 7.35e-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: 66.91  E-value: 7.35e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56377824    99 GTVPVGRVETGTIKAGMVVTFAPSAV-----TTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRGNV 164
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 ...
 84-159 3.11e-14

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: 65.61  E-value: 3.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  84 PLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNV-----GFNIKNVSVKD 158
Cdd:cd16267   1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVtltltGIDPNHLRVGS 80


                .
gi 56377824 159 I 159
Cdd:cd16267  81 I 81
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 84-164 1.11e-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: 61.35  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  84 PLRLPLQDVYKigGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRGN 163
Cdd:cd04089   1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                .
gi 56377824 164 V 164
Cdd:cd04089  79 V 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 91-164 1.88e-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: 55.69  E-value: 1.88e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56377824  91 DVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSA----VTTEVKSVEMHHEQLEAGLPGDNVGFNIKNVSVKDIRRGNV 164
Cdd:cd03694   7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 84-164 3.21e-10

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 54.81  E-value: 3.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  84 PLRLPLQDVYKiGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMH-HEQLEAGLPGDNVGFNIKNVSVKDIRRG 162
Cdd:cd03698   1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                ..
gi 56377824 163 NV 164
Cdd:cd03698  80 DI 81
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 176-224 3.56e-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: 55.48  E-value: 3.56e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 56377824 176 AASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGK 224
Cdd:cd01513   3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE 51
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 85-164 8.28e-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: 8.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56377824  85 LRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVTFAPSAVTTEVKSVEMHHEQLEAGLPGDNVGFNIKN-VsvkDIRRGN 163
Cdd:cd03695   1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77


                .
gi 56377824 164 V 164
Cdd:cd03695  78 L 78
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-77 9.14e-08

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: 50.60  E-value: 9.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56377824     2 SEARYEEIVKETSN-FIKKVGFNPKTVPFVPISGWHGDNMleestnmgwfkgwkkevksgeykgKTLLEAIDSIEPP 77
Cdd:pfam00009 135 DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 179-230 1.58e-04

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


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 39.85  E-value: 1.58e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 56377824 179 FNAQVIVLNHPGQI-GNGYSPVLDCHTAHIACKFDTLLEKIDRRTGKSMEDLP 230
Cdd:cd03704   6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKP 58
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 179-225 1.53e-03

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: 36.73  E-value: 1.53e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 56377824 179 FNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFdtllEKIDR---RTGKS 225
Cdd:cd03708   6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDKevlRTGDR 51
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 172-224 4.96e-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: 35.60  E-value: 4.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 56377824 172 PPKEAASFNAQVIVLNHPGQIGNGYSPVLDCHTAHIACKFDTLLEKIDRRTGK 224
Cdd:cd04093   1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGE 53
 
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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