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Conserved domains on  [gi|1151065125|gb|AQV08751|]
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elongation factor 1-alpha, partial [Sarcophaga hirtipes]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-159 9.71e-96

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: 283.56  E-value: 9.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   1 EAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLE 80
Cdd:PTZ00141  124 EAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIE 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065125  81 ASTNMPWFKgwkierkegnaeGKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:PTZ00141  204 KSDNMPWYK------------GPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP 270
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-159 9.71e-96

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 283.56  E-value: 9.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   1 EAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLE 80
Cdd:PTZ00141  124 EAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIE 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065125  81 ASTNMPWFKgwkierkegnaeGKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:PTZ00141  204 KSDNMPWYK------------GPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP 270
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 8-159 4.35e-74

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: 227.51  E-value: 4.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   8 GQTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEASTNMPW 87
Cdd:COG5256   124 GQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065125  88 FKGwkierkegnaegKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:COG5256   202 YNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMP 261
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-115 6.47e-62

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: 190.01  E-value: 6.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   1 EAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLE 80
Cdd:cd01883   116 EAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIE 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1151065125  81 ASTNMPWFKGWkierkegnaegkTLIDALDAILPP 115
Cdd:cd01883   196 KSENMPWYKGP------------TLLEALDSLEPP 218
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 9-156 4.28e-26

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: 101.68  E-value: 4.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGynPAAVAFVPISGWHGDNMLEASTNMPWF 88
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065125  89 kgwkierkegnaEGKTLIDALDAILPPTRPTEKPLRLPLQDVYKI-----GGIGTVPVGRVETGvlkpGTVVV 156
Cdd:TIGR02034 196 ------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVG----DEVVV 252
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 8-115 7.98e-18

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: 76.02  E-value: 7.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   8 GQTREHALLAFTLGVKqLIVGVNKMDSSeppySEARYEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMleastnmp 86
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV-------- 174

                          90       100
                  ....*....|....*....|....*....
gi 1151065125  87 wfkgwkierkegnaegKTLIDALDAILPP 115
Cdd:pfam00009 175 ----------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-159 9.71e-96

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 283.56  E-value: 9.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   1 EAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLE 80
Cdd:PTZ00141  124 EAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIE 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065125  81 ASTNMPWFKgwkierkegnaeGKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:PTZ00141  204 KSDNMPWYK------------GPTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP 270
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 8-159 4.35e-74

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: 227.51  E-value: 4.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   8 GQTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEASTNMPW 87
Cdd:COG5256   124 GQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065125  88 FKGwkierkegnaegKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:COG5256   202 YNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMP 261
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 8-159 3.75e-72

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 222.49  E-value: 3.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   8 GQTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEASTNMPW 87
Cdd:PRK12317  125 PQTREHVFLARTLGINQLIVAINKMDAVN--YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPW 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065125  88 FKGwkierkegnaegKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:PRK12317  203 YNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMP 262
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-159 9.90e-72

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 222.27  E-value: 9.90e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   1 EAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLE 80
Cdd:PLN00043  124 EAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIE 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065125  81 ASTNMPWFKgwkierkegnaeGKTLIDALDAILPPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:PLN00043  204 RSTNLDWYK------------GPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGP 270
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-115 6.47e-62

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: 190.01  E-value: 6.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   1 EAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLE 80
Cdd:cd01883   116 EAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIE 195

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1151065125  81 ASTNMPWFKGWkierkegnaegkTLIDALDAILPP 115
Cdd:cd01883   196 KSENMPWYKGP------------TLLEALDSLEPP 218
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 9-159 8.21e-42

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: 144.07  E-value: 8.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEASTNMPWF 88
Cdd:COG2895   135 QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065125  89 KgwkierkegnaeGKTLIDALDAILPPTRPTEKPLRLPLQDVYKiggigtvP-------VGRVETGVLKPGTVVVFAP 159
Cdd:COG2895   211 D------------GPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLP 269
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 9-112 1.67e-28

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: 104.19  E-value: 1.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEASTNMPWF 88
Cdd:cd04166   118 QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY 193

                          90       100
                  ....*....|....*....|....
gi 1151065125  89 KgwkierkegnaeGKTLIDALDAI 112
Cdd:cd04166   194 K------------GPTLLEHLETV 205
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 9-159 3.61e-26

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 103.09  E-value: 3.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYnpAAVAFVPISGWHGDNMLEASTNMPWF 88
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065125  89 kgwkierkegnaEGKTLIDALDAILPPTRPTEKPLRLPLQDVYKI-----GGIGTvpvgrVETGVLKPGTVVVFAP 159
Cdd:PRK05506  220 ------------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLP 278
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 9-159 3.65e-26

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 102.68  E-value: 3.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGYNPaAVAFVPISGWHGDNMLEASTNMPWF 88
Cdd:PRK05124  147 QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWY 223

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065125  89 kgwkierkegnaEGKTLIDALDAILPPTRPTEKPLRLPLQDVYKI-----GGIGTvpvgrVETGVLKPGTVVVFAP 159
Cdd:PRK05124  224 ------------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLP 282
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 9-156 4.28e-26

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: 101.68  E-value: 4.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppYSEARYEEIKKEVSSYIKKIGynPAAVAFVPISGWHGDNMLEASTNMPWF 88
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065125  89 kgwkierkegnaEGKTLIDALDAILPPTRPTEKPLRLPLQDVYKI-----GGIGTVPVGRVETGvlkpGTVVV 156
Cdd:TIGR02034 196 ------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVG----DEVVV 252
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 119-159 3.83e-25

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: 92.25  E-value: 3.83e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1151065125 119 TEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP 41
tufA CHL00071
elongation factor Tu
 9-155 3.14e-18

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 80.00  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppySEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEASTNMPwf 88
Cdd:CHL00071  115 QTKEHILLAKQVGVPNIVVFLNKEDQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-- 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125  89 kgwKIERKEGNAEGK--TLIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 155
Cdd:CHL00071  187 ---KIKRGENKWVDKiyNLMDAVDSYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTV 253
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 8-115 7.98e-18

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: 76.02  E-value: 7.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   8 GQTREHALLAFTLGVKqLIVGVNKMDSSeppySEARYEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMleastnmp 86
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV-------- 174

                          90       100
                  ....*....|....*....|....*....
gi 1151065125  87 wfkgwkierkegnaegKTLIDALDAILPP 115
Cdd:pfam00009 175 ----------------QTLLDALDEYLPS 187
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 9-152 8.53e-18

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 78.65  E-value: 8.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEPPY-SEARYEEIKKEVSSYikkiGYNPAAVAFVPISGWhgdNMLEASTNMPW 87
Cdd:COG0050   115 QTREHILLARQVGVPYIVVFLNKCDMVDDEElLELVEMEVRELLSKY----GFPGDDTPIIRGSAL---KALEGDPDPEW 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065125  88 FKgwKIERkegnaegktLIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG 152
Cdd:COG0050   188 EK--KILE---------LMDAVDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVG 242
PRK00049 PRK00049
elongation factor Tu; Reviewed
 9-155 5.26e-17

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 76.38  E-value: 5.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSE-PPYSEARYEEIKKEVSSYikkiGYNPAAVAFVPISGWHGdnmLEASTNMPW 87
Cdd:PRK00049  115 QTREHILLARQVGVPYIVVFLNKCDMVDdEELLELVEMEVRELLSKY----DFPGDDTPIIRGSALKA---LEGDDDEEW 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065125  88 FKgwKIERkegnaegktLIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 155
Cdd:PRK00049  188 EK--KILE---------LMDAVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEV 245
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 9-155 1.41e-16

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: 75.20  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMD-SSEPPYSEARYEEIKKEVSSYikkigynpaavafvpisGWHGDNMleastnmPW 87
Cdd:TIGR00485 115 QTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSQY-----------------DFPGDDT-------PI 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065125  88 FKGWKIERKEGNAEGKT----LIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 155
Cdd:TIGR00485 171 IRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEV 243
PRK12736 PRK12736
elongation factor Tu; Reviewed
 9-155 4.33e-16

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 73.83  E-value: 4.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMD-SSEPPYSEARYEEIKKEVSSYikkigynpaavafvpisGWHGDNMleastnmPW 87
Cdd:PRK12736  115 QTREHILLARQVGVPYLVVFLNKVDlVDDEELLELVEMEVRELLSEY-----------------DFPGDDI-------PV 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065125  88 FKGWKIERKEGNAEGKT----LIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 155
Cdd:PRK12736  171 IRGSALKALEGDPKWEDaimeLMDAVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEV 243
PLN03127 PLN03127
Elongation factor Tu; Provisional
 9-152 5.87e-16

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 73.71  E-value: 5.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKkigynpaavafvpisgWHGDNMleastnmPWF 88
Cdd:PLN03127  164 QTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYK----------------FPGDEI-------PII 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065125  89 KGWKIERKEGNAE--GKT----LIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG 152
Cdd:PLN03127  221 RGSALSALQGTNDeiGKNailkLMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVG 291
PRK12735 PRK12735
elongation factor Tu; Reviewed
 9-152 7.72e-16

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 73.33  E-value: 7.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDS-SEPPYSEARYEEIKKEVSSYikkigynpaavafvpisGWHGDNM--------- 78
Cdd:PRK12735  115 QTREHILLARQVGVPYIVVFLNKCDMvDDEELLELVEMEVRELLSKY-----------------DFPGDDTpiirgsalk 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065125  79 -LEASTNMPWFKgwKIERkegnaegktLIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG 152
Cdd:PRK12735  178 aLEGDDDEEWEA--KILE---------LMDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVG 242
PLN03126 PLN03126
Elongation factor Tu; Provisional
 9-155 3.51e-15

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 71.57  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppySEARYEEIKKEVSSYIKKIGYNPAAVafvPISGWHGDNMLEASTNMPwf 88
Cdd:PLN03126  184 QTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLELVELEVRELLSSYEFPGDDI---PIISGSALLALEALMENP-- 255

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125  89 kgwKIERKEGNAEGKT--LIDALDAILP-PTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVV 155
Cdd:PLN03126  256 ---NIKRGDNKWVDKIyeLMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETV 322
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 8-80 2.73e-10

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: 55.76  E-value: 2.73e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065125   8 GQTREHALLAFtLGVKQLIVGVNKMDSSeppySEARYEEIKKEVSSYIKKIGY---NPAAVAFVPISGWHGDNMLE 80
Cdd:cd00881   101 PQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 9-159 1.63e-09

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: 55.31  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREH-ALLAFtLGVKQLIVGVNKMDSSEPpyseARYEEIKKEVSSYIKKIGYNPAAVafVPISgwhgdnmleASTnmpw 87
Cdd:COG3276    91 QTREHlAILDL-LGIKRGIVVLTKADLVDE----EWLELVEEEIRELLAGTFLEDAPI--VPVS---------AVT---- 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065125  88 fkgwkierKEGNAEgktLIDALDAIL--PPTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:COG3276   151 --------GEGIDE---LRAALDALAaaVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLP 213
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 9-159 4.71e-09

selenocysteine-specific elongation factor SelB; 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-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 54.11  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppysEARYEEIKKEVSSYIKKIGYNPAAVAFVpISGWHGDNMLEASTNMpwf 88
Cdd:TIGR00475  90 QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL--- 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065125  89 kgwkierkegnaegKTLIDALDailppTRPTEKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:TIGR00475 162 --------------KNLLESLD-----IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLP 213
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 9-115 7.17e-07

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: 46.81  E-value: 7.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEppySEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWhgdNMLEASTNMPWF 88
Cdd:cd01884   105 QTREHLLLARQVGVPYIVVFLNKADMVD---DEELLELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWV 178

                          90       100
                  ....*....|....*....|....*..
gi 1151065125  89 KgwKIErkegnaegkTLIDALDAILPP 115
Cdd:cd01884   179 D--KIL---------ELLDALDSYIPT 194
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 122-159 5.59e-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: 42.12  E-value: 5.59e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1151065125 122 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMP 38
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 123-159 1.49e-05

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: 41.10  E-value: 1.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1151065125 123 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP 37
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 125-152 1.03e-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: 1.03e-04
                          10        20
                  ....*....|....*....|....*...
gi 1151065125 125 LPLQDVYKIGGIGTVPVGRVETGVLKPG 152
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVG 30
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 9-54 5.39e-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: 38.36  E-value: 5.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1151065125   9 QTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSY 54
Cdd:cd04171    90 QTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAGT 135
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 9-78 1.66e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 37.52  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065125   9 QTREHaLLAFT-LGVKQLIVGVNKMD--SSEppysEAR--YEEIKKEVSSYIkkigynpAAVA-FVPISGWHGDNM 78
Cdd:PRK04000  126 QTKEH-LMALDiIGIKNIVIVQNKIDlvSKE----RALenYEQIKEFVKGTV-------AENApIIPVSALHKVNI 189
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 122-159 4.48e-03

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: 34.38  E-value: 4.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1151065125 122 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMP 36
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 122-159 6.87e-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: 34.01  E-value: 6.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1151065125 122 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGTVVVFAP 159
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMP 37
 
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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