NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1180720478|gb|ARI47440|]
View 

translation elongation factor 1-alpha, partial [Suillus luteus]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-202 5.24e-128

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: 367.54  E-value: 5.24e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PTZ00141  109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 158
Cdd:PTZ00141  189 PFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVE 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1180720478 159 TGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:PTZ00141  257 TGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNV 300
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-202 5.24e-128

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 367.54  E-value: 5.24e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PTZ00141  109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 158
Cdd:PTZ00141  189 PFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVE 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1180720478 159 TGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:PTZ00141  257 TGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNV 300
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-202 9.18e-100

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 295.23  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:TIGR00483 109 ADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPF 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 160
Cdd:TIGR00483 185 IPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETG 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1180720478 161 VIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:TIGR00483 253 VLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNV 294
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-202 4.64e-98

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: 290.68  E-value: 4.64e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:COG5256   109 ADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 160
Cdd:COG5256   182 IPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETG 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1180720478 161 VIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:COG5256   250 VLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNV 291
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-129 2.25e-69

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: 210.81  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:cd01883   101 ADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDV 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYKGWtketkggvvkgkTLLDAIDAIEPPV 129
Cdd:cd01883   181 PFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-128 4.59e-21

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: 85.65  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGYNPKAVA 79
Cdd:pfam00009  93 ADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVP 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1180720478  80 FVPISGWHGDNMleespnmpwykgwtketkggvvkgKTLLDAIDAIEPP 128
Cdd:pfam00009 163 VVPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-202 5.24e-128

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 367.54  E-value: 5.24e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PTZ00141  109 ADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 158
Cdd:PTZ00141  189 PFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVE 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1180720478 159 TGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:PTZ00141  257 TGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNV 300
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-202 9.18e-100

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 295.23  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:TIGR00483 109 ADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPF 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 160
Cdd:TIGR00483 185 IPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETG 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1180720478 161 VIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:TIGR00483 253 VLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNV 294
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-202 4.64e-98

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: 290.68  E-value: 4.64e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:COG5256   109 ADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPF 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 160
Cdd:COG5256   182 IPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETG 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1180720478 161 VIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:COG5256   250 VLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNV 291
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-202 2.52e-97

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 289.68  E-value: 2.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:PLN00043  109 ADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKI 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 158
Cdd:PLN00043  189 PFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 256

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1180720478 159 TGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:PLN00043  257 TGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNV 300
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-202 2.30e-96

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 286.44  E-value: 2.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKAVAF 80
Cdd:PRK12317  108 ADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPF 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYKGwtketkggvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 160
Cdd:PRK12317  183 IPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETG 250

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1180720478 161 VIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:PRK12317  251 VLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNV 292
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-129 2.25e-69

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: 210.81  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSTFIKKVGYNPKAV 78
Cdd:cd01883   101 ADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDV 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYKGWtketkggvvkgkTLLDAIDAIEPPV 129
Cdd:cd01883   181 PFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-200 1.24e-51

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: 171.42  E-value: 1.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIaggtgefEA--GISKdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPkaV 78
Cdd:COG2895   119 ADLAILLI-------DArkGVLE--QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--I 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  79 AFVPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKiggigtvP----- 153
Cdd:COG2895   188 TFIPISALKGDNVVERSENMPWY------------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------Pnldfr 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1180720478 154 --VGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGF 200
Cdd:COG2895   249 gyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTL 297
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 132-202 3.45e-47

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: 150.03  E-value: 3.45e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180720478 132 SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNV 71
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-128 2.14e-32

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: 115.74  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPkaVAF 80
Cdd:cd04166   102 ADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITF 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPP 128
Cdd:cd04166   173 IPISALEGDNVVSRSENMPWY------------KGPTLLEHLETVEIA 208
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-198 2.26e-32

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 121.17  E-value: 2.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNPKaVAF 80
Cdd:PRK05124  131 CDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRF 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTvpvg 155
Cdd:PRK05124  203 VPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT---- 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1180720478 156 rVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNV 198
Cdd:PRK05124  267 -LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-198 2.35e-32

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 122.35  E-value: 2.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGYNpkAVAF 80
Cdd:PRK05506  128 ADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTF 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTvpvg 155
Cdd:PRK05506  199 IPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT---- 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1180720478 156 rVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNV 198
Cdd:PRK05506  263 -VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV 304
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-198 6.39e-31

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: 116.32  E-value: 6.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSTFIKKVGynPKAVAF 80
Cdd:TIGR02034 104 ADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTF 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNMPWYkgwtketkggvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTVPVG 155
Cdd:TIGR02034 175 IPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASG 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1180720478 156 RVETgvikaGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNV 198
Cdd:TIGR02034 243 SVHV-----GDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAV 280
tufA CHL00071
elongation factor Tu
 2-199 2.03e-25

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 101.57  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIIK-ETSTFIKKVGYNPKAVAF 80
Cdd:CHL00071  100 DGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPI 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  81 VPISGWHGDNMLEESPNmpwykgWTKETKGGVVKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVET 159
Cdd:CHL00071  171 VSGSALLALEALTENPK------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIER 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1180720478 160 GVIKAGMVVT---FAPSNVTTeVKSVEMHHEQLVEGLPGDNVG 199
Cdd:CHL00071  245 GTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVG 286
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 2-199 3.99e-25

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: 100.61  E-value: 3.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAGgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwsEDrfNEIIK----ETSTFIKKVGYN 74
Cdd:COG0050   100 DGAILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV---DD--EELLElvemEVRELLSKYGFP 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  75 PKAVAFVPISGWhgdNMLEESPNMPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVP 153
Cdd:COG0050   165 GDDTPIIRGSAL---KALEGDPDPEWEK-----------KILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVV 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1180720478 154 VGRVETGVIKAG---MVVTFAPSnVTTEVKSVEMHHEQLVEGLPGDNVG 199
Cdd:COG0050   231 TGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVG 278
PRK00049 PRK00049
elongation factor Tu; Reviewed
 2-199 1.66e-23

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 96.03  E-value: 1.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAGGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMDTtkwSEDRfnEIIK----ETSTFIKKVGYN 74
Cdd:PRK00049  100 DGAILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCDM---VDDE--ELLElvemEVRELLSKYDFP 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  75 PKAVAFVPISGWHGdnmLEESPNMPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVP 153
Cdd:PRK00049  165 GDDTPIIRGSALKA---LEGDDDEEWEK-----------KILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVV 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1180720478 154 VGRVETGVIKAG---MVVTFAPSNVTTeVKSVEMHHEQLVEGLPGDNVG 199
Cdd:PRK00049  231 TGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVG 278
PRK12736 PRK12736
elongation factor Tu; Reviewed
 2-199 2.87e-23

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 95.40  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIK-ETSTFIKKVGYNPKA 77
Cdd:PRK12736  100 DGAILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDD 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  78 VAFVPISGWHGdnmLEESPnmPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGR 156
Cdd:PRK12736  168 IPVIRGSALKA---LEGDP--KWED-----------AIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGR 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1180720478 157 VETGVIKAG---MVVTFAPSnVTTEVKSVEMHHEQLVEGLPGDNVG 199
Cdd:PRK12736  232 VERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVG 276
PLN03127 PLN03127
Elongation factor Tu; Provisional
 2-199 8.47e-22

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 91.81  E-value: 8.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIIKETSTFIKKVGYNPKAVA 79
Cdd:PLN03127  149 DGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYKFPGDEIPIIR 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  80 FVPISGWHGDNmleespnmpwykgwTKETKGGVVKgktLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 158
Cdd:PLN03127  222 GSALSALQGTN--------------DEIGKNAILK---LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVE 284

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1180720478 159 TGVIKAG---MVVTFAPS-NVTTEVKSVEMHHEQLVEGLPGDNVG 199
Cdd:PLN03127  285 QGTIKVGeevEIVGLRPGgPLKTTVTGVEMFKKILDQGQAGDNVG 329
PRK12735 PRK12735
elongation factor Tu; Reviewed
 2-199 4.44e-21

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 89.51  E-value: 4.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTKWSEdrFNEIIK-ETSTFIKKVGYNpka 77
Cdd:PRK12735  100 DGAILVVS----------AADGpmpQTREHILLARQVGVPYIVVFLNKCDMVDDEE--LLELVEmEVRELLSKYDFP--- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  78 vafvpisgwhGDNM----------LEESPNMPWYKgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKI 146
Cdd:PRK12735  165 ----------GDDTpiirgsalkaLEGDDDEEWEA-----------KILELMDAVDSyIPEPERAIDKPFLMPIEDVFSI 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1180720478 147 GGIGTVPVGRVETGVIKAG---MVVTFAPSNVTTeVKSVEMHHEQLVEGLPGDNVG 199
Cdd:PRK12735  224 SGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVG 278
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-128 4.59e-21

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: 85.65  E-value: 4.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-TFIKKVGYNPKAVA 79
Cdd:pfam00009  93 ADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVP 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1180720478  80 FVPISGWHGDNMleespnmpwykgwtketkggvvkgKTLLDAIDAIEPP 128
Cdd:pfam00009 163 VVPGSALKGEGV------------------------QTLLDALDEYLPS 187
PLN03126 PLN03126
Elongation factor Tu; Provisional
 2-199 1.20e-20

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 88.90  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKwSEDRFNEIIKETSTFIKKVGYNPKAVAFV 81
Cdd:PLN03126  169 DGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPII 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  82 PISGWHGDNMLEESPNMPwyKGWTKetkgGVVKGKTLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 160
Cdd:PLN03126  241 SGSALLALEALMENPNIK--RGDNK----WVDKIYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERG 314

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1180720478 161 VIKAGMVVTFAPSNVT--TEVKSVEMHHEQLVEGLPGDNVG 199
Cdd:PLN03126  315 TVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVG 355
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 2-199 6.46e-20

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: 86.37  E-value: 6.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIIKETSTFIKKVGYNPKAVA 79
Cdd:TIGR00485 100 DGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEEllELVEMEVRELLSQYDFPGDDTPIIR 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  80 FVPISGWHGDNMLEEspnmpwykgwtketkggvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 158
Cdd:TIGR00485 173 GSALKALEGDAEWEA-------------------KILELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVE 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1180720478 159 TGVIKAG---MVVTFAPSNVTTeVKSVEMHHEQLVEGLPGDNVG 199
Cdd:TIGR00485 234 RGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDNVG 276
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-201 1.85e-15

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


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 73.79  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   2 DCAILIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKA 77
Cdd:COG3276    76 DLVLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLED 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  78 VAFVPISGWHGDNmLEEspnmpwykgwtketkggvvkgktLLDAIDAI--EPPVRPSDKPLRLPLQDVYKIGGIGTVPVG 155
Cdd:COG3276   141 APIVPVSAVTGEG-IDE-----------------------LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTG 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1180720478 156 RVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFN 201
Cdd:COG3276   197 TLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALN 242
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 136-202 2.49e-14

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: 65.36  E-value: 2.49e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180720478 136 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGI 67
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-128 3.93e-14

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: 67.32  E-value: 3.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSTFIKKVGY---NPKA 77
Cdd:cd00881    86 ADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKD 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180720478  78 VAFVPISGWHGDNMLEespnmpwykgwtketkggvvkgktLLDAIDAIEPP 128
Cdd:cd00881   156 VPIIPISALTGEGIEE------------------------LLDAIVEHLPP 182
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-202 5.52e-14

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: 69.52  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478   1 ADCAILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGYNPKA 77
Cdd:TIGR00475  74 IDAALLVVD----------ADEGvmtQTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  78 VAFVpISGWHGDNMLEESPNMpwykgwtketkggvvkgKTLLDAIDAieppvRPSDKPLRLPLQDVYKIGGIGTVPVGRV 157
Cdd:TIGR00475 142 KIFK-TSAKTGQGIGELKKEL-----------------KNLLESLDI-----KRIQKPLRMAIDRAFKVKGAGTVVTGTA 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1180720478 158 ETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:TIGR00475 199 FSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNL 243
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 135-198 3.17e-12

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: 59.83  E-value: 3.17e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180720478 135 PLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNV 198
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNV 64
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 138-199 5.33e-12

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: 59.07  E-value: 5.33e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180720478 138 LPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFA--PSNVTTEVKSVEMHHEQLVEGLPGDNVG 199
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVG 66
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 136-202 3.22e-11

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


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 57.15  E-value: 3.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180720478 136 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNL 67
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 150-202 1.89e-09

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 52.27  E-value: 1.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1180720478 150 GTVPVGRVETGVIKAGMVVTFAP-----SNVTTEVKSVEMHHEQLVEGLPGDNVGFNV 202
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLIL 58
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 136-200 1.62e-08

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.87  E-value: 1.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180720478 136 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNVGF 200
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 135-198 2.46e-08

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: 49.41  E-value: 2.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1180720478 135 PLRLPLQDVYKigGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMHHEQLVEGLPGDNV 198
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENV 62
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 135-198 4.11e-07

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: 45.96  E-value: 4.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180720478 135 PLRLPLQDVYKiGGIGTVPVGRVETGVIKAGMVVTFAPSNVTTEVKSVEMH-HEQLVEGLPGDNV 198
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTV 64
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 2-48 1.58e-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: 43.73  E-value: 1.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1180720478   2 DCAILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 48
Cdd:cd01884    90 DGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 142-200 4.34e-05

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 40.67  E-value: 4.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180720478 142 DVYKIGGIGTVPVGRVETGVIKAGMVVTFAP----SNVTTEVKSVEMHHEQLVEGLPGDNVGF 200
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdadgKFRPVTVKSIHRNRQPVDRARAGQSASF 69
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-73 1.20e-03

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: 37.97  E-value: 1.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180720478   2 DCAILIIAGgtgefEAGISKdgQTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKKVGY 73
Cdd:cd04171    75 DAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLV--DEDRLELVEEEILELLAGTFL 137
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 24-199 1.76e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 38.29  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478  24 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSTFIKkvGYNPKAVAFVPISGWHGDNMleespnmpwykg 103
Cdd:PRK04000  126 QTKEHLMALDIIGIKNIVIVQNKIDLV--SKERALENYEQIKEFVK--GTVAENAPIIPVSALHKVNI------------ 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180720478 104 wtketkggvvkgKTLLDAIDA-IEPPVRPSDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VIKAGM 166
Cdd:PRK04000  190 ------------DALIEAIEEeIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGI 257

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1180720478 167 VVTFAPSN----VTTEVKSVEMHHEQLVEGLPGDNVG 199
Cdd:PRK04000  258 KVEEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVG 294
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH