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Conserved domains on  [gi|1049891811|gb|ANY92592|]
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elongation factor 1-alpha, partial [Osmia cyaneonitens]

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 ...
 1-346 0e+00

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: 639.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:PTZ00141   82 TPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVN 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGwtverkegkvegKCLIZALDAILPPT*P 160
Cdd:PTZ00141  162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:PTZ00141  230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:PTZ00141  310 RGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAI 389

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:PTZ00141  390 VKMVPTKPMCVEVFNEYPPLGRFAVR 415
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-346 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 639.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:PTZ00141   82 TPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVN 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGwtverkegkvegKCLIZALDAILPPT*P 160
Cdd:PTZ00141  162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:PTZ00141  230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:PTZ00141  310 RGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAI 389

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:PTZ00141  390 VKMVPTKPMCVEVFNEYPPLGRFAVR 415
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-346 2.05e-174

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: 490.60  E-value: 2.05e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVN*MDSTEpp 80
Cdd:COG5256    82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN-- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPPT*P 160
Cdd:COG5256   153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPT------------LLEALDNLKEPEKP 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:COG5256   221 VDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIK 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSkNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:COG5256   301 RGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAI 379

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:COG5256   380 VKIKPTKPLVIEKFKEFPQLGRFAIR 405
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-346 4.58e-172

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: 485.14  E-value: 4.58e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVN*MDSTEpp 80
Cdd:TIGR00483  82 TDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN-- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGwtverkegkvegKCLIZALDAILPPT*P 160
Cdd:TIGR00483 156 YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKP 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:TIGR00483 224 TDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIR 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSKNnPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:TIGR00483 304 RGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAI 382

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:TIGR00483 383 VKFKPTKPMVIEAVKEIPPLGRFAIR 408
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-157 8.09e-94

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: 278.61  E-value: 8.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:cd01883    74 TEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVN 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPP 157
Cdd:cd01883   154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPT------------LLEALDSLEPP 218
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-123 5.12e-37

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: 131.49  E-value: 5.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVN*MDSTepp 80
Cdd:pfam00009  66 TKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--- 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1049891811  81 ySETRFEEI*KEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEV 123
Cdd:pfam00009 135 -DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQTL 177
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-346 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 639.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:PTZ00141   82 TPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTVN 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGwtverkegkvegKCLIZALDAILPPT*P 160
Cdd:PTZ00141  162 YSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:PTZ00141  230 VDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:PTZ00141  310 RGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAI 389

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:PTZ00141  390 VKMVPTKPMCVEVFNEYPPLGRFAVR 415
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-346 1.08e-174

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 492.68  E-value: 1.08e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:PLN00043   82 TTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPPT*P 160
Cdd:PLN00043  162 YSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPT------------LLEALDQINEPKRP 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:PLN00043  230 SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLK 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:PLN00043  310 RGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGF 389

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:PLN00043  390 VKMIPTKPMVVETFSEYPPLGRFAVR 415
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-346 2.05e-174

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: 490.60  E-value: 2.05e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVN*MDSTEpp 80
Cdd:COG5256    82 TDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN-- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPPT*P 160
Cdd:COG5256   153 YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNGPT------------LLEALDNLKEPEKP 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:COG5256   221 VDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIK 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSkNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:COG5256   301 RGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAI 379

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:COG5256   380 VKIKPTKPLVIEKFKEFPQLGRFAIR 405
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-346 2.43e-172

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 485.59  E-value: 2.43e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEpp 80
Cdd:PRK12317   81 TDKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN-- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPPT*P 160
Cdd:PRK12317  154 YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNGPT------------LLEALDNLKPPEKP 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:PRK12317  222 TDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIK 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGdSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:PRK12317  302 RGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAI 380

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:PRK12317  381 VKIKPTKPLVIEKVKEIPQLGRFAIR 406
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-346 4.58e-172

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: 485.14  E-value: 4.58e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVN*MDSTEpp 80
Cdd:TIGR00483  82 TDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN-- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGwtverkegkvegKCLIZALDAILPPT*P 160
Cdd:TIGR00483 156 YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKP 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELR 240
Cdd:TIGR00483 224 TDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIR 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 241 RGYVAGDSKNnPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAI 320
Cdd:TIGR00483 304 RGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAI 382

                         330       340
                  ....*....|....*....|....*.
gi 1049891811 321 VTLVPSKPMCVEAFQEFPPLGRFAVR 346
Cdd:TIGR00483 383 VKFKPTKPMVIEAVKEIPPLGRFAIR 408
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-157 8.09e-94

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: 278.61  E-value: 8.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:cd01883    74 TEKYRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVN 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPP 157
Cdd:cd01883   154 WSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGPT------------LLEALDSLEPP 218
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 254-346 7.71e-63

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 195.10  E-value: 7.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 254 KGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAIVTLVPSKPMCVEA 333
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                          90
                  ....*....|...
gi 1049891811 334 FQEFPPLGRFAVR 346
Cdd:cd03705    81 FSEYPPLGRFAVR 93
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 8-343 1.79e-56

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: 189.53  E-value: 1.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   8 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppYSETRFE 87
Cdd:COG2895    99 IADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEVFE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  88 EI*KEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAILPPT*P******* 167
Cdd:COG2895   170 EIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYDGPT------------LLEHLETVEVAEDRNDAPFRF 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 168 ***DVYKiggigtvP-------VGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVK---SVSvk 237
Cdd:COG2895   236 PVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiDIS-- 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 238 elrRGYVAGDSkNNPPKGAADFTAQVIVLN-HPGQISNGYtpVLDCHTAHIACKFAEIKEKCDRRTGktTEQNPKAIKSG 316
Cdd:COG2895   307 ---RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTL--EHEAADSLELN 378

                         330       340
                  ....*....|....*....|....*..
gi 1049891811 317 DAAIVTLVPSKPMCVEAFQEFPPLGRF 343
Cdd:COG2895   379 DIGRVTLRLAEPIAFDPYADNRATGSF 405
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 171-251 2.09e-52

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: 168.14  E-value: 2.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 171 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYVAGDSKN 250
Cdd:cd03693    11 DVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGDVAGDSKN 90


                  .
gi 1049891811 251 N 251
Cdd:cd03693    91 D 91
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 8-154 3.17e-38

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: 135.39  E-value: 3.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   8 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppYSETRFE 87
Cdd:cd04166    82 IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEVFE 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1049891811  88 EI*KEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEVSSKMPWFKgwtverkegkveGKCLIZALDAI 154
Cdd:cd04166   153 EIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-123 5.12e-37

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: 131.49  E-value: 5.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVN*MDSTepp 80
Cdd:pfam00009  66 TKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--- 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1049891811  81 ySETRFEEI*KEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEV 123
Cdd:pfam00009 135 -DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQTL 177
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-343 2.02e-34

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: 130.19  E-value: 2.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEpp 80
Cdd:TIGR02034  77 TDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD-- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKKIGynPAAVAFVPISGWHGDNMLEVSSKMPWFKGWTVERKEGKVEGKCLIZALDAILPpt*p 160
Cdd:TIGR02034 148 YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWYSGPTLLEILETVEVERDAQDLPLRFP---- 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 161 **********dVYKI--------GGIGTVPVGRVEtgvlkPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVK 232
Cdd:TIGR02034 222 -----------VQYVnrpnldfrGYAGTIASGSVH-----VGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLD 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 233 SVSvkELRRG--YVAGDsknNPPKGAADFTAQVIVL-NHPgqISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQn 309
Cdd:TIGR02034 286 DEI--DISRGdlLAAAD---SAPEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA- 357

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1049891811 310 pKAIKSGDAAIVTLVPSKPMCVEAFQEFPPLGRF 343
Cdd:TIGR02034 358 -KSLELNEIGRVNLSLDEPIAFDPYAENRTTGAF 390
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 8-227 3.62e-32

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 125.41  E-value: 3.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   8 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppYSETRFE 87
Cdd:PRK05124  111 IADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEVFE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  88 EI*KEVSSYIKKIGYNPaAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAIlppt*p******* 167
Cdd:PRK05124  182 RIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYSGPT------------LLEVLETV------------- 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049891811 168 ***DVYKIGGIGTV--PV--------------GRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNV 227
Cdd:PRK05124  236 ---DIQRVVDAQPFrfPVqyvnrpnldfrgyaGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 8-264 9.99e-32

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 125.43  E-value: 9.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   8 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppYSETRFE 87
Cdd:PRK05506  108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFD 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  88 EI*KEVSSYIKKIGYnpAAVAFVPISGWHGDNMLEVSSKMPWFKGWTverkegkvegkcLIZALDAIlppt*p******* 167
Cdd:PRK05506  179 EIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWYEGPS------------LLEHLETV-------EIASDR 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 168 ***DVykiggigTVPV--------------GRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDnvgfnvkS 233
Cdd:PRK05506  238 NLKDF-------RFPVqyvnrpnldfrgfaGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQ-------A 303

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1049891811 234 VSVK-----ELRRGYVAGDSkNNPPKGAADFTAQVI 264
Cdd:PRK05506  304 VTLTladeiDISRGDMLARA-DNRPEVADQFDATVV 338
tufA CHL00071
elongation factor Tu
 9-267 8.16e-31

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 120.45  E-value: 8.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppySETRFEE 88
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVD---DEELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  89 I*KEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEVSSKMPwfkgwTVERKEGKVEGKC--LIZALDAILP-PT*P***** 165
Cdd:CHL00071  150 VELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKIynLMDAVDSYIPtPERDTDKPF 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 166 *****DVYKIGGIGTVPVGRVETGVLKPGMVVTFapAGL----TTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRR 241
Cdd:CHL00071  222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVEI--VGLretkTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIER 299

                         250       260
                  ....*....|....*....|....*.
gi 1049891811 242 GYVAgdSKNNPPKGAADFTAQVIVLN 267
Cdd:CHL00071  300 GMVL--AKPGTITPHTKFEAQVYILT 323
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 252-346 3.30e-29

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 108.51  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 252 PPKGAADFTAQVIVLNH-----PGQISNGYTPVLDCHTAHIACKFAEIKEKCDrrTGKTTEqNPKAIKSGDAAIVTLVPS 326
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|
gi 1049891811 327 KPMCVEAFQefpplgRFAVR 346
Cdd:pfam03143  78 KPIALEKGQ------RFAIR 91
PLN03126 PLN03126
Elongation factor Tu; Provisional
 9-346 4.38e-29

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 116.64  E-value: 4.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppySETRFEE 88
Cdd:PLN03126  149 VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLEL 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  89 I*KEVSSYIKKIGYNPAAVafvPISGWHGDNMLEVSSKMPwfkgwTVERKEGKVEGKC--LIZALDAILP-PT*P***** 165
Cdd:PLN03126  219 VELEVRELLSSYEFPGDDI---PIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQRQTDLPF 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 166 *****DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLT--TEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGY 243
Cdd:PLN03126  291 LLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGM 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 244 VAgdSKNNPPKGAADFTAQVIVLNHP--GQIS---NGYTPVLDCHTAHIACKFAEIKEKCDRRTgktteqnpKAIKSGDA 318
Cdd:PLN03126  371 VL--AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------KMVMPGDR 440

                         330       340
                  ....*....|....*....|....*...
gi 1049891811 319 AIVTLVPSKPMCVEAFQefpplgRFAVR 346
Cdd:PLN03126  441 VKMVVELIVPVACEQGM------RFAIR 462
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-346 4.79e-29

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 116.08  E-value: 4.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEPP 80
Cdd:PLN03127  121 TAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDE 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  81 YSETRFEEI*KEVSSYIKkigynpaavafvpisgWHGDNmlevsskMPWFKGWTVERKEGKVE--GKC----LIZALDAI 154
Cdd:PLN03127  194 ELLELVEMELRELLSFYK----------------FPGDE-------IPIIRGSALSALQGTNDeiGKNailkLMDAVDEY 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 155 LP-PT*P**********DVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAG-LTTEVKSVEMHHEALQEAVPGDNVGF 229
Cdd:PLN03127  251 IPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFKKILDQGQAGDNVGL 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 230 NVKSVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVLN------HPGQISNgYTPVLDCHTAHIackfaeikekcdrrTG 303
Cdd:PLN03127  331 LLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADV--------------TG 393

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1049891811 304 KTT-EQNPKAIKSGDAAIVTLVPSKPMCVEAFQefpplgRFAVR 346
Cdd:PLN03127  394 KVElPEGVKMVMPGDNVTAVFELISPVPLEPGQ------RFALR 431
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 9-266 7.56e-28

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: 112.17  E-value: 7.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEPPYsetRFEE 88
Cdd:COG0050    80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEE---LLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  89 I*KEVSSYIKKIGYNPAAVAFVPISGWhgdNMLEVSSKMPWfkgwtverkEGKVEGkcLIZALDAILP-PT*P******* 167
Cdd:COG0050   150 VEMEVRELLSKYGFPGDDTPIIRGSAL---KALEGDPDPEW---------EKKILE--LMDAVDSYIPePERDTDKPFLM 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 168 ***DVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAgLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:COG0050   216 PVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQV 294

                         250       260
                  ....*....|....*....|..
gi 1049891811 245 AgdSKNNPPKGAADFTAQVIVL 266
Cdd:COG0050   295 L--AKPGSITPHTKFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 9-266 1.07e-27

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 111.57  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppySETRFEE 88
Cdd:PRK12736   80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKVDLVD---DEELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  89 I*KEVSSYIKKIGYNPAAVAFVPISGWH---GDnmlevsskmpwfkgwtvERKEGKVEGkcLIZALDAILP-PT*P**** 164
Cdd:PRK12736  150 VEMEVRELLSEYDFPGDDIPVIRGSALKaleGD-----------------PKWEDAIME--LMDAVDEYIPtPERDTDKP 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 165 ******DVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAgLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRR 241
Cdd:PRK12736  211 FLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVER 289

                         250       260
                  ....*....|....*....|....*
gi 1049891811 242 GYVAgdSKNNPPKGAADFTAQVIVL 266
Cdd:PRK12736  290 GQVL--AKPGSIKPHTKFKAEVYIL 312
PRK00049 PRK00049
elongation factor Tu; Reviewed
 9-266 1.08e-26

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 108.74  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEppySETRFEE 88
Cdd:PRK00049   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVD---DEELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  89 I*KEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEVSSKMPWfkgwtverkEGKVEGkcLIZALDAILP-PT*P******* 167
Cdd:PRK00049  150 VEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEW---------EKKILE--LMDAVDSYIPtPERAIDKPFLM 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 168 ***DVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAGLTTeVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:PRK00049  216 PIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294

                         250       260
                  ....*....|....*....|..
gi 1049891811 245 AgdSKNNPPKGAADFTAQVIVL 266
Cdd:PRK00049  295 L--AKPGSITPHTKFEAEVYVL 314
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 9-266 1.65e-26

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: 108.33  E-value: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MD-STEPPYSETRFE 87
Cdd:TIGR00485  80 VDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEM 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  88 EI*KEVSSYikkigynpaavafvpisGWHGDNmlevsskMPWFKGWTVERKEGKVEGKC----LIZALDAILP-PT*P** 162
Cdd:TIGR00485 153 EVRELLSQY-----------------DFPGDD-------TPIIRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREID 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 163 ********DVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPAGLTTeVKSVEMHHEALQEAVPGDNVGFNVKSVSVKEL 239
Cdd:TIGR00485 209 KPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDNVGLLLRGIKREEI 287

                         250       260
                  ....*....|....*....|....*..
gi 1049891811 240 RRGYVAgdSKNNPPKGAADFTAQVIVL 266
Cdd:TIGR00485 288 ERGMVL--AKPGSIKPHTKFEAEVYVL 312
PRK12735 PRK12735
elongation factor Tu; Reviewed
 9-266 3.51e-26

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 107.62  E-value: 3.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MDSTEPPyseTRFEE 88
Cdd:PRK12735   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDE---ELLEL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  89 I*KEVSSYIKKIGYNpaavafvpisgwhGDNmlevsskMPWFKGWTVERKEGKVEGKC------LIZALDAILP-PT*P* 161
Cdd:PRK12735  150 VEMEVRELLSKYDFP-------------GDD-------TPIIRGSALKALEGDDDEEWeakileLMDAVDSYIPePERAI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 162 *********DVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPaGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKE 238
Cdd:PRK12735  210 DKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKE-TQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKRED 288

                         250       260
                  ....*....|....*....|....*...
gi 1049891811 239 LRRGYVAgdSKNNPPKGAADFTAQVIVL 266
Cdd:PRK12735  289 VERGQVL--AKPGSIKPHTKFEAEVYVL 314
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-122 2.09e-25

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: 100.83  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVKQLIVGVN*MDSTepp 80
Cdd:cd00881    59 WPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV--- 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1049891811  81 ySETRFEEI*KEVSSYIKKIGY---NPAAVAFVPISGWHGDNMLE 122
Cdd:cd00881   128 -GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 259-346 6.83e-25

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 96.69  E-value: 6.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 259 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKttEQNPKAIKSGDAAIVTLVPSKPMCVEAFQEFP 338
Cdd:cd01513     6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGKEFP 83


                  ....*...
gi 1049891811 339 PLGRFAVR 346
Cdd:cd01513    84 TLGRFALR 91
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 6-244 1.10e-24

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: 105.00  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   6 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtLGVKQLIVGVN*MDSTEPpyseT 84
Cdd:COG3276    53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-LGIKRGIVVLTKADLVDE----E 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  85 RFEEI*KEVSSYIKKigynpaavafvpiSGWHGDNMLEVSSKmpwfkgwtveRKEGKVEgkcLIZALDAILPPT*P**** 164
Cdd:COG3276   121 WLELVEEEIRELLAG-------------TFLEDAPIVPVSAV----------TGEGIDE---LRAALDALAAAVPA---- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 165 ******D---------VYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVS 235
Cdd:COG3276   171 ---RDADgpfrlpidrVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVE 247


                  ....*....
gi 1049891811 236 VKELRRGYV 244
Cdd:COG3276   248 KEEIERGDV 256
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 259-346 1.06e-19

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


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 82.99  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 259 FTAQVIVLNHPGQI-SNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAIVTLVPSKPMCVEAFQEF 337
Cdd:cd03704     6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85


                  ....*....
gi 1049891811 338 PPLGRFAVR 346
Cdd:cd03704    86 PQLGRFTLR 94
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 9-75 2.54e-18

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: 81.86  E-value: 2.54e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVN*MD 75
Cdd:cd01884    70 VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 171-244 1.93e-17

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: 75.76  E-value: 1.93e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049891811 171 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKsvSVKELRRGYV 244
Cdd:cd01342     7 KVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGIL--GVKDILTGDT 78
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 252-346 4.24e-16

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 72.96  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 252 PPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDRRTGKTTEQNPKAIKSGDAAIVTLVPSKPMCV 331
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80

                          90
                  ....*....|....*
gi 1049891811 332 EAFQEFPPLGRFAVR 346
Cdd:cd04093    81 ETFKDNKELGRFVLR 95
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 8-110 3.39e-15

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: 72.25  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   8 IIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLGVKQLIVGVN*MDSTEPPysetRFE 87
Cdd:cd04171    54 FIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RLE 122

                          90       100
                  ....*....|....*....|...
gi 1049891811  88 EI*KEVSSYIKKIGYNPAAVAFV 110
Cdd:cd04171   123 LVEEEILELLAGTFLADAPIFPV 145
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 179-244 4.83e-15

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 69.22  E-value: 4.83e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1049891811 179 GTVPVGRVETGVLKPGMVVTFAPAG-----LTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtgkkkIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 172-244 6.77e-15

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: 69.09  E-value: 6.77e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1049891811 172 VYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:cd03696     8 VFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 171-244 3.12e-14

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: 67.16  E-value: 3.12e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049891811 171 DVYKIGGIGTVPVGRVETGVLKPGMVVTFA--PAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:cd03697     7 DVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 171-244 1.90e-10

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


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 56.84  E-value: 1.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1049891811 171 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAG----LTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 171-227 7.64e-10

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: 54.83  E-value: 7.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1049891811 171 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNV 227
Cdd:cd16267     8 DVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNV 64
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 179-244 2.43e-07

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: 47.86  E-value: 2.43e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049891811 179 GTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKSVSVKELRRGYV 244
Cdd:cd04089    14 GTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFV 79
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 9-110 2.61e-07

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 52.36  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   9 IDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTlGVKQLIVGVN*MDSTEPPysetRFE 87
Cdd:PRK10512   56 IDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----RIA 123

                          90       100
                  ....*....|....*....|...
gi 1049891811  88 EI*KEVSSYIKKIGYnPAAVAFV 110
Cdd:PRK10512  124 EVRRQVKAVLREYGF-AEAKLFV 145
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 184-229 2.87e-07

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: 47.56  E-value: 2.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1049891811 184 GRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGF 229
Cdd:cd03695    20 GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 171-247 3.41e-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: 47.50  E-value: 3.41e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1049891811 171 DVYKiGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMH-HEALQEAVPGDNVGFNVKSVSVKELRRGYVAGD 247
Cdd:cd03698     8 DKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPGDILSS 84
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 6-253 2.43e-06

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 48.69  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   6 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAgiskngQTREHaLLAFT-LGVKQLIVGVN*MDSTEPPYSET 84
Cdd:PRK04000   87 VSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMALDiIGIKNIVIVQNKIDLVSKERALE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  85 RFEEI*KEVSSYIkkigynpAAVA-FVPISGWHGDNM----LEVSSKMPwfkgwTVERKEGKVEGKCLIZALDAILPPT* 159
Cdd:PRK04000  160 NYEQIKEFVKGTV-------AENApIIPVSALHKVNIdaliEAIEEEIP-----TPERDLDKPPRMYVARSFDVNKPGTP 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 160 P**********dvyKI-GGI--GTVPVGRVETG---VLKPGMVVTFAPAG----LTTEVKSVEMHHEALQEAVPGDNVGF 229
Cdd:PRK04000  228 PE------------KLkGGVigGSLIQGVLKVGdeiEIRPGIKVEEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVGV 295

                         250       260
                  ....*....|....*....|....*..
gi 1049891811 230 NVK---SVSVKELRRGYVAGDSKNNPP 253
Cdd:PRK04000  296 GTKldpSLTKADALAGSVAGKPGTLPP 322
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 6-120 1.18e-05

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 45.16  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   6 VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVGVN*MDstEPPY 81
Cdd:cd01887    51 ITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID--KPYG 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1049891811  82 SETRFEEI*KEVSSY---IKKIGYNpaaVAFVPISGWHGDNM 120
Cdd:cd01887   117 TEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 6-101 1.65e-05

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 45.36  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   6 VTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVgVN*MDSTeppySE 83
Cdd:cd04165    86 VTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALALKVPVFVV-VTKIDMT----PA 153

                          90
                  ....*....|....*...
gi 1049891811  84 TRFEEI*KEVSSYIKKIG 101
Cdd:cd04165   154 NVLQETLKDLKRLLKSPG 171
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 171-228 2.82e-05

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


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 41.90  E-value: 2.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049891811 171 DVYKIGGiGTVPVGRVETGVLKPGMVVTfAPAGlTTEVKSVEMHHEALQEAVPGDNVG 228
Cdd:cd16265     7 KVFKILG-RQVLTGEVESGVIYVGYKVK-GDKG-VALIRAIEREHRKVDFAVAGDEVA 61
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 259-304 2.00e-04

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


Pssm-ID: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 39.81  E-value: 2.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1049891811 259 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKCDrRTGK 304
Cdd:cd03708     6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVL-RTGD 50
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 4-130 6.17e-04

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 40.71  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   4 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--REhallAFTLGVKQLIVgVN*MDS--TE- 78
Cdd:cd04167    71 YLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH----AIQEGLPMVLV-INKIDRliLEl 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1049891811  79 --PP---YSETRfeEI*KEVSSYIKKIGyNPAAVAFVPISGwhgdNMLEVSSKMPWF 130
Cdd:cd04167   141 klPPtdaYYKLR--HTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-224 8.60e-04

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 41.14  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811   1 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTREHALLAFTLGVKQLIVGVN*MD 75
Cdd:PTZ00327  114 TLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------NescpqPQTSEHLAAVEIMKLKHIIILQNKID 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811  76 STEPPYSETRFEEI*KEVSSYIKKigynpaAVAFVPISGWHGDNM---LE-VSSKMPwfkgwtVERKEGKVEGK-CLIZA 150
Cdd:PTZ00327  183 LVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPISAQLKYNIdvvLEyICTQIP------IPKRDLTSPPRmIVIRS 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049891811 151 LDAILPPT*P**********dvykiggIGTVPVGRVETGVLK--------PGMVV-----TFAPAGLTTEVKSVEMHHEA 217
Cdd:PTZ00327  251 FDVNKPGEDIENL--------------KGGVAGGSILQGVLKvgdeieirPGIISkdsggEFTCRPIRTRIVSLFAENNE 316


                  ....*..
gi 1049891811 218 LQEAVPG 224
Cdd:PTZ00327  317 LQYAVPG 323
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 6-75 7.51e-03

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 37.60  E-value: 7.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049891811   6 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgvKQL----IVGVN*MD 75
Cdd:cd04168    66 VNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKID 127
 
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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