NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|635254461|gb|AHZ67063|]
View 

elongation factor 1-alpha, partial [Cinara moketa]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-180 2.55e-112

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: 326.70  E-value: 2.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:PTZ00141 166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKP 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PTZ00141 234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313

                        170
                 ....*....|....*....
gi 635254461 162 AGDTKNNPPKGAADFTAQV 180
Cdd:PTZ00141 314 ASDSKNDPAKECADFTAQV 332
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-180 2.55e-112

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 326.70  E-value: 2.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:PTZ00141 166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKP 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PTZ00141 234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313

                        170
                 ....*....|....*....
gi 635254461 162 AGDTKNNPPKGAADFTAQV 180
Cdd:PTZ00141 314 ASDSKNDPAKECADFTAQV 332
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 2-180 3.76e-85

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: 256.71  E-value: 3.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461    2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:TIGR00483 160 EFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:TIGR00483 228 LRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDV 307

                         170
                  ....*....|....*....
gi 635254461  162 AGDTKnNPPKGAADFTAQV 180
Cdd:TIGR00483 308 CGHPD-NPPKVAKEFTAQI 325
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-180 3.80e-82

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: 249.08  E-value: 3.80e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:COG5256  157 RYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKP 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:COG5256  225 LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDV 304

                        170
                 ....*....|....*....
gi 635254461 162 AGDTkNNPPKGAADFTAQV 180
Cdd:COG5256  305 AGHP-DNPPTVAEEFTAQI 322
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 78-168 1.93e-60

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 182.39  E-value: 1.93e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  78 TDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELR 157
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                         90
                 ....*....|.
gi 635254461 158 RGFVAGDTKNN 168
Cdd:cd03693   81 RGDVAGDSKND 91
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 96-161 4.37e-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: 4.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635254461   96 GTVPVGRVETGLLKPGMVVVFAPA-----NITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-180 2.55e-112

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 326.70  E-value: 2.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:PTZ00141 166 RYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKP 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PTZ00141 234 LRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313

                        170
                 ....*....|....*....
gi 635254461 162 AGDTKNNPPKGAADFTAQV 180
Cdd:PTZ00141 314 ASDSKNDPAKECADFTAQV 332
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 2-180 3.76e-85

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: 256.71  E-value: 3.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461    2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:TIGR00483 160 EFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKP 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:TIGR00483 228 LRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDV 307

                         170
                  ....*....|....*....
gi 635254461  162 AGDTKnNPPKGAADFTAQV 180
Cdd:TIGR00483 308 CGHPD-NPPKVAKEFTAQI 325
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-180 3.80e-82

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: 249.08  E-value: 3.80e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:COG5256  157 RYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKP 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:COG5256  225 LRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDV 304

                        170
                 ....*....|....*....
gi 635254461 162 AGDTkNNPPKGAADFTAQV 180
Cdd:COG5256  305 AGHP-DNPPTVAEEFTAQI 322
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-180 5.77e-82

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 248.69  E-value: 5.77e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:PRK12317 158 RYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKP 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PRK12317 226 LRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDV 305

                        170
                 ....*....|....*....
gi 635254461 162 AGDTkNNPPKGAADFTAQV 180
Cdd:PRK12317 306 CGHP-DNPPTVAEEFTAQI 323
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-180 8.58e-82

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 248.85  E-value: 8.58e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGwaverkegkadgKCLIEALDAILPPSRPTDKA 81
Cdd:PLN00043 166 RYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKP 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PLN00043 234 LRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313

                        170
                 ....*....|....*....
gi 635254461 162 AGDTKNNPPKGAADFTAQV 180
Cdd:PLN00043 314 ASNSKDDPAKEAANFTSQV 332
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 78-168 1.93e-60

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 182.39  E-value: 1.93e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  78 TDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELR 157
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                         90
                 ....*....|.
gi 635254461 158 RGFVAGDTKNN 168
Cdd:cd03693   81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 2-180 3.16e-33

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: 122.12  E-value: 3.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPaaVAFVPISGWNGDNMLEVSEKMPWFkgwaverkegkaDGKCLIEALDAILPPSRPTDKA 81
Cdd:COG2895  167 VFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDAP 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKiggigtvP-------VGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVK---NV 151
Cdd:COG2895  233 FRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDI 305

                        170       180
                 ....*....|....*....|....*....
gi 635254461 152 SvkelrRGFVAGDtKNNPPKGAADFTAQV 180
Cdd:COG2895  306 S-----RGDVIVA-ADAPPEVADQFEATL 328
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-74 1.43e-27

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: 102.95  E-value: 1.43e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635254461   1 TRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWNGDNMLEVSEKMPWFKGWaverkegkadgkCLIEALDAILPP 74
Cdd:cd01883  157 ERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 82-161 4.77e-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: 79.62  E-value: 4.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNvsVKELRRGFV 161
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 82-161 4.82e-18

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


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 74.49  E-value: 4.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 2-180 9.62e-18

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 79.59  E-value: 9.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYnpAAVAFVPISGWNGDNMLEVSEKMPWFKGWAverkegkadgkcLIEALDAILPPSRPTDKA 81
Cdd:PRK05506 176 VFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPS------------LLEHLETVEIASDRNLKD 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKI-----GGIGTVPVGRVetgllKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKN---VSv 153
Cdd:PRK05506 242 FRFPVQYVNRPnldfrGFAGTVASGVV-----RPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS- 315

                        170       180
                 ....*....|....*....|....*....
gi 635254461 154 kelrRG--FVAGDtknNPPKGAADFTAQV 180
Cdd:PRK05506 316 ----RGdmLARAD---NRPEVADQFDATV 337
PRK12735 PRK12735
elongation factor Tu; Reviewed
 51-161 5.44e-17

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 77.19  E-value: 5.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  51 AVERKEGKADGKC---LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTE 124
Cdd:PRK12735 178 ALEGDDDEEWEAKileLMDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVeiVGIKETQKTT 257

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 635254461 125 VKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PRK12735 258 VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQV 294
PRK00049 PRK00049
elongation factor Tu; Reviewed
 51-161 5.46e-17

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 77.15  E-value: 5.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  51 AVERKEGKADGKC---LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTE 124
Cdd:PRK00049 178 ALEGDDDEEWEKKileLMDAVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVeiVGIRDTQKTT 257

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 635254461 125 VKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PRK00049 258 VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294
tufA CHL00071
elongation factor Tu
 64-161 1.25e-16

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 76.15  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  64 LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG---MVVVFAPANITTeVKSVEMHHEALTEAV 139
Cdd:CHL00071 202 LMDAVDSYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRETKTTT-VTGLEMFQKTLDEGL 280

                         90       100
                 ....*....|....*....|..
gi 635254461 140 PGDNVGFNVKNVSVKELRRGFV 161
Cdd:CHL00071 281 AGDNVGILLRGIQKEDIERGMV 302
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-180 2.28e-16

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: 75.49  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461    1 TRFEEIKKEVSSYIKKIGynPAAVAFVPISGWNGDNMLEVSEKMPWFKgwaverkegkadGKCLIEALDAILPPSRPTDK 80
Cdd:TIGR02034 151 EVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYS------------GPTLLEILETVEVERDAQDL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   81 ALRLPLQDVYKI-----GGIGTVPVGRVetgllKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSvkE 155
Cdd:TIGR02034 217 PLRFPVQYVNRPnldfrGYAGTIASGSV-----HVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--D 289

                         170       180
                  ....*....|....*....|....*..
gi 635254461  156 LRRG--FVAGDtknNPPKGAADFTAQV 180
Cdd:TIGR02034 290 ISRGdlLAAAD---SAPEVADQFAATL 313
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 84-161 3.70e-16

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 69.47  E-value: 3.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  84 LPLQDVYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVeiVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 96-161 4.37e-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: 4.37e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635254461   96 GTVPVGRVETGLLKPGMVVVFAPA-----NITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
PLN03127 PLN03127
Elongation factor Tu; Provisional
 42-161 5.03e-16

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 74.86  E-value: 5.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  42 EKMPWFKGWAVERKEGKAD--GKC----LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG--- 111
Cdd:PLN03127 215 DEIPIIRGSALSALQGTNDeiGKNailkLMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeev 294

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 635254461 112 -MVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:PLN03127 295 eIVGLRPGGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQV 345
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 45-161 1.15e-15

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: 73.66  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   45 PWFKGWAVERKEGKADGKC----LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVV--VFA 117
Cdd:TIGR00485 169 PIIRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVeiVGL 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 635254461  118 PANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:TIGR00485 249 KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMV 292
PRK12736 PRK12736
elongation factor Tu; Reviewed
 64-161 1.52e-15

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 73.05  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  64 LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG--MVVVFAPANITTEVKSVEMHHEALTEAVP 140
Cdd:PRK12736 192 LMDAVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdeVEIVGIKETQKTVVTGVEMFRKLLDEGQA 271

                         90       100
                 ....*....|....*....|.
gi 635254461 141 GDNVGFNVKNVSVKELRRGFV 161
Cdd:PRK12736 272 GDNVGVLLRGVDRDEVERGQV 292
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 64-161 2.13e-15

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: 72.49  E-value: 2.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  64 LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPG---MVVVFAPANITTeVKSVEMHHEALTEAV 139
Cdd:COG0050  194 LMDAVDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDTQKTV-VTGVEMFRKLLDEGE 272

                         90       100
                 ....*....|....*....|..
gi 635254461 140 PGDNVGFNVKNVSVKELRRGFV 161
Cdd:COG0050  273 AGDNVGLLLRGIKREDVERGQV 294
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 64-161 5.86e-15

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


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 71.87  E-value: 5.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  64 LIEALDAIL--PPSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPG 141
Cdd:COG3276  157 LRAALDALAaaVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAG 236

                         90       100
                 ....*....|....*....|
gi 635254461 142 DNVGFNVKNVSVKELRRGFV 161
Cdd:COG3276  237 QRVALNLAGVEKEEIERGDV 256
PLN03126 PLN03126
Elongation factor Tu; Provisional
 64-161 1.60e-14

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 70.41  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  64 LIEALDAILP-PSRPTDKALRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVV--VFAPANITTEVKSVEMHHEALTEAVP 140
Cdd:PLN03126 271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdiVGLRETRSTTVTGVEMFQKILDEALA 350

                         90       100
                 ....*....|....*....|.
gi 635254461 141 GDNVGFNVKNVSVKELRRGFV 161
Cdd:PLN03126 351 GDNVGLLLRGIQKADIQRGMV 371
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 82-164 1.72e-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: 65.23  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:cd16267    2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGSI 81


                 ...
gi 635254461 162 AGD 164
Cdd:cd16267   82 LCD 84
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-144 9.78e-14

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 68.02  E-value: 9.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPAaVAFVPISGWNGDNMLEVSEKMPWFKgwaverkegkadGKCLIEALDAILPPSRPTDKA 81
Cdd:PRK05124 179 VFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWYS------------GPTLLEVLETVDIQRVVDAQP 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635254461  82 LRLPLQDVYKI-----GGIGTVPVGRVetgllKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNV 144
Cdd:PRK05124 246 FRFPVQYVNRPnldfrGYAGTLASGVV-----KVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 2-75 1.37e-12

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: 62.97  E-value: 1.37e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 635254461   2 RFEEIKKEVSSYIKKIGYNPaaVAFVPISGWNGDNMLEVSEKMPWFKgwaverkegkadGKCLIEALDAILPPS 75
Cdd:cd04166  150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETVEIAS 209
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 82-161 8.74e-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: 57.88  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKigGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:cd04089    2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFV 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 88-161 4.66e-11

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: 56.46  E-value: 4.66e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 635254461  88 DVYKIGGIGTVPVGRVETGLLKPGMVVVFAPAN----ITTEVKSVEMHHEALTEAVPGDNVGFNVKNVSVKELRRGFV 161
Cdd:cd03694    7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 82-164 5.79e-11

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


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 55.97  E-value: 5.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635254461  82 LRLPLQDVYKiGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMH-HEALTEAVPGDNVGFNVKNVSVKELRRGF 160
Cdd:cd03698    2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPGD 80


                 ....
gi 635254461 161 VAGD 164
Cdd:cd03698   81 ILSS 84
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 82-146 1.28e-08

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.87  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 635254461  82 LRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVVVFAPANITTEVKSVEMHHEALTEAVPGDNVGF 146
Cdd:cd03695    1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 87-145 2.27e-04

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 38.04  E-value: 2.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 635254461  87 QDVYKIGGiGTVPVGRVETGLLKPGMVVVfaPANITTEVKSVEMHHEALTEAVPGDNVG 145
Cdd:cd16265    6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH