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Conserved domains on  [gi|1050145317|gb|ANY95107|]
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elongation factor 1-alpha, partial [Obama applanata]

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 ...
 2-178 1.25e-100

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: 297.04  E-value: 1.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317   2 GEFEAGISKNGQTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDN 81
Cdd:PTZ00141  121 GEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  82 MVTPSTNMPWFKgwtikrkngatkkeesltGITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKP 161
Cdd:PTZ00141  201 MIEKSDNMPWYK------------------GPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKP 262

                         170
                  ....*....|....*..
gi 1050145317 162 GMVVCFAPHGLTTEVKS 178
Cdd:PTZ00141  263 GMVVTFAPSGVTTEVKS 279
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-178 1.25e-100

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 297.04  E-value: 1.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317   2 GEFEAGISKNGQTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDN 81
Cdd:PTZ00141  121 GEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  82 MVTPSTNMPWFKgwtikrkngatkkeesltGITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKP 161
Cdd:PTZ00141  201 MIEKSDNMPWYK------------------GPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKP 262

                         170
                  ....*....|....*..
gi 1050145317 162 GMVVCFAPHGLTTEVKS 178
Cdd:PTZ00141  263 GMVVTFAPSGVTTEVKS 279
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 12-178 1.54e-72

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: 224.43  E-value: 1.54e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  12 GQTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDNMVTPSTNMPW 91
Cdd:COG5256   124 GQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  92 FKGwtikrkngatkkeesltgITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHG 171
Cdd:COG5256   202 YNG------------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAG 263


                  ....*..
gi 1050145317 172 LTTEVKS 178
Cdd:COG5256   264 VVGEVKS 270
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-125 4.65e-59

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: 183.46  E-value: 4.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317   1 VGEFEAGISKNGQTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGD 80
Cdd:cd01883   112 KGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGD 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1050145317  81 NMVTPSTNMPWFKGWtikrkngatkkeesltgiTLLEAMDAIDPP 125
Cdd:cd01883   192 NLIEKSENMPWYKGP------------------TLLEALDSLEPP 218
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 13-178 3.69e-24

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: 97.06  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGynPDTVAFVPISGWVGDNMVTPSTNMPWF 92
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  93 kgwtikrkngatkkeeslTGITLLEAMDAIDPPARPTEKPLRLPLQDVYKI-----GGIGTVPVGRVEtgiikPGMVVCF 167
Cdd:TIGR02034 196 ------------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVH-----VGDEVVV 252

                         170
                  ....*....|.
gi 1050145317 168 APHGLTTEVKS 178
Cdd:TIGR02034 253 LPSGRSSRVAR 263
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 12-84 2.66e-15

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: 69.86  E-value: 2.66e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050145317  12 GQTREHALLAYTLGVKqMIVGINKIDSAEppy*E*RYNEIKKEVSG-Y*KKVGYNPDTVAFVPISGWVGDNMVT 84
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRVD----GAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-178 1.25e-100

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 297.04  E-value: 1.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317   2 GEFEAGISKNGQTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDN 81
Cdd:PTZ00141  121 GEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  82 MVTPSTNMPWFKgwtikrkngatkkeesltGITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKP 161
Cdd:PTZ00141  201 MIEKSDNMPWYK------------------GPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKP 262

                         170
                  ....*....|....*..
gi 1050145317 162 GMVVCFAPHGLTTEVKS 178
Cdd:PTZ00141  263 GMVVTFAPSGVTTEVKS 279
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-178 1.02e-75

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 233.44  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317   2 GEFEAGISKNGQTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDN 81
Cdd:PLN00043  121 GGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  82 MVTPSTNMPWFKgwtikrkngatkkeesltGITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKP 161
Cdd:PLN00043  201 MIERSTNLDWYK------------------GPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKP 262

                         170
                  ....*....|....*..
gi 1050145317 162 GMVVCFAPHGLTTEVKS 178
Cdd:PLN00043  263 GMVVTFGPTGLTTEVKS 279
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 12-178 1.54e-72

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: 224.43  E-value: 1.54e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  12 GQTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDNMVTPSTNMPW 91
Cdd:COG5256   124 GQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  92 FKGwtikrkngatkkeesltgITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHG 171
Cdd:COG5256   202 YNG------------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAG 263


                  ....*..
gi 1050145317 172 LTTEVKS 178
Cdd:COG5256   264 VVGEVKS 270
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 12-178 1.02e-70

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 219.80  E-value: 1.02e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  12 GQTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDNMVTPSTNMPW 91
Cdd:PRK12317  125 PQTREHVFLARTLGINQLIVAINKMDAVN--YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPW 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  92 FKGwtikrkngatkkeesltgITLLEAMDAIDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHG 171
Cdd:PRK12317  203 YNG------------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAG 264


                  ....*..
gi 1050145317 172 LTTEVKS 178
Cdd:PRK12317  265 VVGEVKS 271
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-125 4.65e-59

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: 183.46  E-value: 4.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317   1 VGEFEAGISKNGQTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGD 80
Cdd:cd01883   112 KGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGD 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1050145317  81 NMVTPSTNMPWFKGWtikrkngatkkeesltgiTLLEAMDAIDPP 125
Cdd:cd01883   192 NLIEKSENMPWYKGP------------------TLLEALDSLEPP 218
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 13-178 1.05e-39

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: 139.07  E-value: 1.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNPdtVAFVPISGWVGDNMVTPSTNMPWF 92
Cdd:COG2895   135 QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  93 KgwtikrkngatkkeesltGITLLEAMDAIDPPARPTEKPLRLPLQDVYKiggigtvP-------VGRVETGIIKPGMVV 165
Cdd:COG2895   211 D------------------GPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEV 265

                         170
                  ....*....|...
gi 1050145317 166 CFAPHGLTTEVKS 178
Cdd:COG2895   266 VVLPSGKTSTVKS 278
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 129-178 1.80e-30

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: 106.50  E-value: 1.80e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1050145317 129 TEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHGLTTEVKS 178
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKS 50
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 13-178 8.22e-27

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 105.00  E-value: 8.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNPDtVAFVPISGWVGDNMVTPSTNMPWF 92
Cdd:PRK05124  147 QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  93 KgwtikrkngatkkeesltGITLLEAMDAIDPPARPTEKPLRLPLQDVYKI-----GGIGTvpvgrVETGIIKPGMVVCF 167
Cdd:PRK05124  224 S------------------GPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKV 280

                         170
                  ....*....|.
gi 1050145317 168 APHGLTTEVKS 178
Cdd:PRK05124  281 LPSGKESNVAR 291
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 13-126 3.65e-24

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: 93.79  E-value: 3.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNPdtVAFVPISGWVGDNMVTPSTNMPWF 92
Cdd:cd04166   118 QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY 193

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1050145317  93 KgwtikrkngatkkeesltGITLLEAMDAIDPPA 126
Cdd:cd04166   194 K------------------GPTLLEHLETVEIAS 209
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 13-178 3.69e-24

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: 97.06  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGynPDTVAFVPISGWVGDNMVTPSTNMPWF 92
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  93 kgwtikrkngatkkeeslTGITLLEAMDAIDPPARPTEKPLRLPLQDVYKI-----GGIGTVPVGRVEtgiikPGMVVCF 167
Cdd:TIGR02034 196 ------------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVH-----VGDEVVV 252

                         170
                  ....*....|.
gi 1050145317 168 APHGLTTEVKS 178
Cdd:TIGR02034 253 LPSGRSSRVAR 263
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 13-178 1.45e-23

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 96.54  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppY*E*RYNEIKKEVSGY*KKVGYNpdTVAFVPISGWVGDNMVTPSTNMPWF 92
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  93 kgwtikrkngatkkeeslTGITLLEAMDAIDPPARPTEKPLRLPLQDVYKI-----GGIGTvpvgrVETGIIKPGMVVCF 167
Cdd:PRK05506  220 ------------------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVV 276

                         170
                  ....*....|.
gi 1050145317 168 APHGLTTEVKS 178
Cdd:PRK05506  277 LPSGKTSRVKR 287
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 13-162 1.18e-16

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: 76.34  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEPPY-*E*RYNEIKKEVSGY*kkvGYNPDTVAFVPISGwvgdnmvtpstnmpw 91
Cdd:COG0050   115 QTREHILLARQVGVPYIVVFLNKCDMVDDEElLELVEMEVRELLSKY----GFPGDDTPIIRGSA--------------- 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1050145317  92 fkgwtIKRKNGATKKEESLTGITLLEAMDA-IDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:COG0050   176 -----LKALEGDPDPEWEKKILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVG 242
PRK12736 PRK12736
elongation factor Tu; Reviewed
 13-162 1.52e-16

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 75.75  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAE-PPY*E*RYNEIKKEVSGY*kkvgynpdtvafvpisGWVGDnmvtpstNMPW 91
Cdd:PRK12736  115 QTREHILLARQVGVPYLVVFLNKVDLVDdEELLELVEMEVRELLSEY-----------------DFPGD-------DIPV 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1050145317  92 FKGWTIKRKNGATKKEESltgitLLEAMDAIDP----PARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:PRK12736  171 IRGSALKALEGDPKWEDA-----IMELMDAVDEyiptPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
PRK00049 PRK00049
elongation factor Tu; Reviewed
 13-162 1.90e-16

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 75.61  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAE-PPY*E*RYNEIKKEVSGY*kkvgynpdtvafvpisGWVGDNMvtpstnmPW 91
Cdd:PRK00049  115 QTREHILLARQVGVPYIVVFLNKCDMVDdEELLELVEMEVRELLSKY-----------------DFPGDDT-------PI 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1050145317  92 FKGWTIKRKNGATKKEESLTGITLLEAMDA-IDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:PRK00049  171 IRGSALKALEGDDDEEWEKKILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVG 242
PRK12735 PRK12735
elongation factor Tu; Reviewed
 13-162 2.97e-16

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 74.87  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEPP-Y*E*RYNEIKKEVSGY*kkvgynpdtvafvpisGWVGDNMvtpstnmPW 91
Cdd:PRK12735  115 QTREHILLARQVGVPYIVVFLNKCDMVDDEeLLELVEMEVRELLSKY-----------------DFPGDDT-------PI 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1050145317  92 FKGWTIKRKNGATKKEESLTGITLLEAMDA-IDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:PRK12735  171 IRGSALKALEGDDDEEWEAKILELMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVG 242
PLN03127 PLN03127
Elongation factor Tu; Provisional
 13-162 9.56e-16

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 73.71  E-value: 9.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAE-PPY*E*RYNEIKKEVSGY*kkvgynpdtvafvpisgwvgdnmvTPSTNMPW 91
Cdd:PLN03127  164 QTKEHILLARQVGVPSLVVFLNKVDVVDdEELLELVEMELRELLSFYK------------------------FPGDEIPI 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1050145317  92 FKGWTIKRKNGatkKEESLTGITLLEAMDAIDP----PARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:PLN03127  220 IRGSALSALQG---TNDEIGKNAILKLMDAVDEyipePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVG 291
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 12-84 2.66e-15

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: 69.86  E-value: 2.66e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050145317  12 GQTREHALLAYTLGVKqMIVGINKIDSAEppy*E*RYNEIKKEVSG-Y*KKVGYNPDTVAFVPISGWVGDNMVT 84
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRVD----GAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT 176
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 13-162 3.04e-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: 72.12  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSA-EPPY*E*RYNEIKKEVSGY*kkvgynpdtvafvpisGWVGDNMvtpstnmPW 91
Cdd:TIGR00485 115 QTREHILLARQVGVPYIVVFLNKCDMVdDEELLELVEMEVRELLSQY-----------------DFPGDDT-------PI 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1050145317  92 FKGWTIKRKNGATKKEESLtgITLLEAMDA-IDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:TIGR00485 171 IRGSALKALEGDAEWEAKI--LELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
tufA CHL00071
elongation factor Tu
 13-165 3.25e-15

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 72.30  E-value: 3.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEPPy*e*rynEI----KKEVSGY*KKVGYNPDTVAFVPISGWVGDNMVTPSTN 88
Cdd:CHL00071  115 QTKEHILLAKQVGVPNIVVFLNKEDQVDDE-------ELlelvELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPK 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  89 M-----PWFKgwTIkrkngatkkeesltgITLLEAMDA-IDPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPG 162
Cdd:CHL00071  188 IkrgenKWVD--KI---------------YNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVG 250


                  ...
gi 1050145317 163 MVV 165
Cdd:CHL00071  251 DTV 253
PLN03126 PLN03126
Elongation factor Tu; Provisional
 13-165 2.92e-12

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 63.87  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEppy*E*RYNEIKKEVSGY*KKVGYNPDTVAFVPISGWVGDNMVTpstnmpwf 92
Cdd:PLN03126  184 QTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEALM-------- 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050145317  93 kgwtikrKNGATKKEESLTGITLLEAMDAIDP----PARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVV 165
Cdd:PLN03126  253 -------ENPNIKRGDNKWVDKIYELMDAVDSyipiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV 322
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 13-178 9.16e-12

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: 62.24  E-value: 9.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  13 QTREH-ALLAyTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGy*kkvgynpdTV----AFVPISgwvgdnmvtpst 87
Cdd:COG3276    91 QTREHlAILD-LLGIKRGIVVLTKADLVDEEWLELVEEEIRELLAG----------TFledaPIVPVS------------ 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050145317  88 nmpwfkgwtikrkngATKKEesltGI-TLLEAMDAI--DPPARPTEKPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMV 164
Cdd:COG3276   148 ---------------AVTGE----GIdELRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDE 208

                         170
                  ....*....|....
gi 1050145317 165 VCFAPHGLTTEVKS 178
Cdd:COG3276   209 LELLPSGKPVRVRG 222
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 133-178 2.73e-08

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: 48.80  E-value: 2.73e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1050145317 133 LRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHGLTTEVKS 178
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTS 46
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 132-178 2.53e-06

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: 43.66  E-value: 2.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1050145317 132 PLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHGLTTEVKS 178
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKS 47
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 12-82 3.48e-06

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 44.98  E-value: 3.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050145317  12 GQTREHALLAyTLGVKQMIVGINKIDSAeppy*E*RYNEIKKEVSGY*KKVGY---NPDTVAFVPISGWVGDNM 82
Cdd:cd00881   101 PQTREHLNIA-LAGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGI 169
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 13-37 7.59e-05

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


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 41.42  E-value: 7.59e-05
                          10        20
                  ....*....|....*....|....*
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKID 37
Cdd:cd01884   105 QTREHLLLARQVGVPYIVVFLNKAD 129
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 135-165 1.16e-04

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: 39.04  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1050145317 135 LPLQDVYKIGGIGTVPVGRVETGIIKPGMVV 165
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEV 33
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 133-178 1.20e-04

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: 39.09  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1050145317 133 LRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVCFAPHGLTTEVKS 178
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKS 46
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 132-176 2.37e-04

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: 38.23  E-value: 2.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1050145317 132 PLRLPLQDVYKigGIGTVPVGRVETGIIKPGMVVCFAPHGLTTEV 176
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEV 43
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 13-58 2.84e-04

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 39.51  E-value: 2.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGY 58
Cdd:cd04171    90 QTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAGT 135
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 13-82 7.28e-04

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 38.40  E-value: 7.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGy*kkvgynpdTVA----FVPISGWVGDNM 82
Cdd:cd01888   118 QTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKEFVKG----------TIAenapIIPISAQLKYNI 181
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 13-75 8.38e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 39.06  E-value: 8.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050145317  13 QTREHALLAYTLGVKQMIVGINKIDSAEPPY*E*RYNEIKKEVSGy*kkvgynpdTVA----FVPIS 75
Cdd:PRK04000  126 QTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKG----------TVAenapIIPVS 182
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 132-177 1.42e-03

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: 36.33  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1050145317 132 PLRLPLQDVYKiGGIGTVPVGRVETGIIKPGMVVCFAPHGLTTEVK 177
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVK 45
 
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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