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Conserved domains on  [gi|4503471|ref|NP_001393|]
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elongation factor 1-alpha 1 [Homo sapiens]

Protein Classification

elongation factor 1-alpha( domain architecture ID 11488101)

elongation factor 1-alpha promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-460 0e+00

elongation factor 1- alpha; Provisional


:

Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 911.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   161 PYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   321 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 460
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-460 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 911.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   161 PYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   321 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 460
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-444 0e+00

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: 687.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:TIGR00483   1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagisKNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483  81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    161 pYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    321 RRGNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 4503471    401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 444
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-445 0e+00

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: 682.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:COG5256   1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256  81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  161 pYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  321 RRGNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:COG5256 300 KRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 4503471  401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKA 445
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
9-238 1.48e-159

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: 449.63  E-value: 1.48e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYE 168
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  169 EIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWkvtrkdgnasgtTLLEALDCILPP 238
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
5-238 2.71e-77

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: 238.96  E-value: 2.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSK 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGVKqLIVGVNKMDSTeppySQ 164
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503471    165 KRYEEIVKEVS-TYIKKIGYNPDTVAFVPISGWNGDNMlepsanmpwfkgwkvtrkdgnasgTTLLEALDCILPP 238
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-460 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 911.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   161 PYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:PTZ00141 161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYK------------GPTLLEALDTLEPPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   321 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 460
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
1-457 0e+00

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 714.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PLN00043   1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEP 160
Cdd:PLN00043  81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   161 PYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGwkvtrkdgnasgTTLLEALDCILPPTR 240
Cdd:PLN00043 161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   321 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 4503471   401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQK 457
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-444 0e+00

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: 687.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:TIGR00483   1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagisKNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483  81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    161 pYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    321 RRGNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 4503471    401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 444
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-445 0e+00

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: 682.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:COG5256   1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAYTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256  81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  161 pYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTR 240
Cdd:COG5256 153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  241 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 320
Cdd:COG5256 220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  321 RRGNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 400
Cdd:COG5256 300 KRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 4503471  401 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKA 445
Cdd:COG5256 379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
3-444 0e+00

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 674.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PRK12317   2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEppY 162
Cdd:PRK12317  82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   163 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPT 242
Cdd:PRK12317 155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   243 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRR 322
Cdd:PRK12317 223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   323 GNVAGdSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIV 402
Cdd:PRK12317 303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 4503471   403 DMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 444
Cdd:PRK12317 382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPA 423
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
9-238 1.48e-159

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: 449.63  E-value: 1.48e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYE 168
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  169 EIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWkvtrkdgnasgtTLLEALDCILPP 238
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
4-447 1.82e-93

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: 289.29  E-value: 1.82e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    4 EKTHINIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFE 81
Cdd:COG2895  14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   82 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTE 159
Cdd:COG2895  92 TPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDArkGVLE---------QTRRHSYIASLLGIRHVVVAVNKMDLVD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  160 ppYSQKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPT 239
Cdd:COG2895 163 --YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  240 RPTDKPLRLPLQDVYKiggigtvP-------VGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGF-- 310
Cdd:COG2895 227 DRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtl 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  311 --NVknvsvkDVRRGNVAGDSkNDPPMEAAGFTAQVIILN-HPGQISAGYapVLDCHTAHIACKFAELKEKIDRRSGKKL 387
Cdd:COG2895 300 edEI------DISRGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHE 370
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503471  388 EdgPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVIKAVDKKAAG 447
Cdd:COG2895 371 A--ADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGALRRAAN 430
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
5-238 2.71e-77

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: 238.96  E-value: 2.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSK 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGVKqLIVGVNKMDSTeppySQ 164
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503471    165 KRYEEIVKEVS-TYIKKIGYNPDTVAFVPISGWNGDNMlepsanmpwfkgwkvtrkdgnasgTTLLEALDCILPP 238
Cdd:pfam00009 137 AELEEVVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
335-438 5.41e-74

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: 227.46  E-value: 5.41e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  335 MEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVES 414
Cdd:cd03705   1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
                        90       100
                ....*....|....*....|....
gi 4503471  415 FSDYPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705  81 FSEYPPLGRFAVRDMRQTVAVGVI 104
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
9-235 3.30e-61

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: 198.56  E-value: 3.30e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAAEMGKgsFKYAWVLDKLKAERERGITIDISLWKFETSKY 85
Cdd:cd04166   1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYS 163
Cdd:cd04166  79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDArkGVLE---------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YD 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503471  164 QKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCI 235
Cdd:cd04166 148 EEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
242-332 4.34e-61

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: 193.94  E-value: 4.34e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 321
Cdd:cd03693   1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
                        90
                ....*....|.
gi 4503471  322 RGNVAGDSKND 332
Cdd:cd03693  81 RGDVAGDSKND 91
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
14-438 5.29e-61

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: 204.14  E-value: 5.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGK--GSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:TIGR02034   7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     92 APGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYSQKRYEEIV 171
Cdd:TIGR02034  87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    172 KEVSTYIKKIGynPDTVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPLRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    252 DVYKI-----GGIGTVPVGRVetgvlKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVRRGN-- 324
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSV-----HVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDll 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    325 VAGDSkndPPMEAAGFTAQVIIL-NHPgqISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEdgPKFLKSGDAAIVD 403
Cdd:TIGR02034 297 AAADS---APEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGA--AKSLELNEIGRVN 369
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 4503471    404 MVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 370 LSLDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
14-462 5.31e-59

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 204.39  E-value: 5.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMG--KGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:PRK05506  31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    92 APGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYSQKRYEE 169
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDArkGVLT---------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   170 IVKEVSTYIKKIGYNpdTVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPLRLP 249
Cdd:PRK05506 180 IVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   250 LQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVgfnvkNVSVKD---VR 321
Cdd:PRK05506 246 VQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidIS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   322 RGNVAGDSkNDPPMEAAGFTAQVIILN----HPGqisAGYapVLDCHTAHIACKFAELKEKIDRRSgkkLEDGP-KFLKS 396
Cdd:PRK05506 316 RGDMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAaKTLEL 386
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503471   397 GDAAIVDMVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVIKAVDKKAAG----AGKVTK---SAQKAQKAK 462
Cdd:PRK05506 387 NEIGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIDFALRRATNvhwqASDVSRearAARKGQKPA 461
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
1-325 9.31e-58

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: 195.37  E-value: 9.31e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050   1 MAKEkfertKPHVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:COG0050  66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  156 DSTEPPYSQKRYEEIVKE-VSTYikkiGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEALD 233
Cdd:COG0050 139 DMVDDEELLELVEMEVRElLSKY----GFPGDDTPIIRGSALKA---LEGDPDPEWEKKiLE------------LMDAVD 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  234 CILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPvNVTTEVKSVEMHHEALSEALPGDNVG 309
Cdd:COG0050 200 SYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVG 278
                       330
                ....*....|....*.
gi 4503471  310 FNVKNVSVKDVRRGNV 325
Cdd:COG0050 279 LLLRGIKREDVERGQV 294
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
14-345 5.75e-57

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 195.52  E-value: 5.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    14 GHVDSGKSTTTGHLIYkcggiDKRTIekFEKEAAEMGKGSFK---------YAWVLDKLKAERERGITIDISLWKFETSK 84
Cdd:PRK05124  34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppYSQ 164
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   165 KRYEEIVKEVSTYIKKIGYNPDtVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDK 244
Cdd:PRK05124 178 EVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   245 PLRLPLQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkD 319
Cdd:PRK05124 245 PFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--D 317
                        330       340
                 ....*....|....*....|....*.
gi 4503471   320 VRRGNVAGDSKNDPPMeAAGFTAQVI 345
Cdd:PRK05124 318 ISRGDLLVAADEALQA-VQHASADVV 342
PRK12736 PRK12736
elongation factor Tu; Reviewed
1-443 1.54e-56

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 192.08  E-value: 1.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLiykcggidkrtiekfEKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12736   1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:PRK12736  66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   156 DSTEPPYSQKRYEEIVKE-VSTYikkiGYNPDTVAFVPISGW---NGDNMLEPSANmpwfkgwkvtrkdgnasgtTLLEA 231
Cdd:PRK12736 139 DLVDDEELLELVEMEVRElLSEY----DFPGDDIPVIRGSALkalEGDPKWEDAIM-------------------ELMDA 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   232 LDCILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVnVTTEVKSVEMHHEALSEALPGDN 307
Cdd:PRK12736 196 VDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDN 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   308 VGFNVKNVSVKDVRRGNVAGDSKNDPPmeAAGFTAQVIILN------HPGqISAGYAPVLDCHTAhiackfaelkekiDR 381
Cdd:PRK12736 275 VGVLLRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYILTkeeggrHTP-FFNNYRPQFYFRTT-------------DV 338
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503471   382 RSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAVDK 443
Cdd:PRK12736 339 TGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGL------KFAIREGGRTVGAGTVTEILD 394
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-325 8.35e-56

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 190.40  E-value: 8.35e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFK-YAWVlDKLKAERERGITID 74
Cdd:PRK00049   1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITIN 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    75 ISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNK 154
Cdd:PRK00049  65 TAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   155 MDSTEPPysqkryE--EIVK-EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLE 230
Cdd:PRK00049 138 CDMVDDE------EllELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLE------------LMD 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   231 ALDCILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHEALSEALPGD 306
Cdd:PRK00049 197 AVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGD 275
                        330
                 ....*....|....*....
gi 4503471   307 NVGFNVKNVSVKDVRRGNV 325
Cdd:PRK00049 276 NVGALLRGIKREDVERGQV 294
PRK12735 PRK12735
elongation factor Tu; Reviewed
1-325 1.51e-53

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 184.27  E-value: 1.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735   1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKM 155
Cdd:PRK12735  66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   156 DSTEPPysqkryE--EIVK-EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEA 231
Cdd:PRK12735 139 DMVDDE------EllELVEmEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLE------------LMDA 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   232 LDCILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHEALSEALPGDN 307
Cdd:PRK12735 198 VDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDN 276
                        330
                 ....*....|....*...
gi 4503471   308 VGFNVKNVSVKDVRRGNV 325
Cdd:PRK12735 277 VGVLLRGTKREDVERGQV 294
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
9-203 2.26e-53

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: 177.10  E-value: 2.26e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaaemgkgsfkyaWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLAyTLGVKQLIVGVNKMDSTeppySQKRYE 168
Cdd:cd00881  66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIA-LAGGLPIIVAVNKIDRV----GEEDFD 133
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4503471  169 EIVKEVSTYIKKIGY---NPDTVAFVPISGWNGDNMLE 203
Cdd:cd00881 134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
PLN03126 PLN03126
Elongation factor Tu; Provisional
3-441 3.62e-52

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 182.89  E-value: 3.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03126  77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEppy 162
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   163 SQKRYEEIVKEVSTYIKKIGYNPDTvafVPISGWNGDNMLEPSANMPwfkgwKVTRKDGNASGTT--LLEALDCILP-PT 239
Cdd:PLN03126 212 DEELLELVELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQ 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   240 RPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHEALSEALPGDNVGFNVKNVSV 317
Cdd:PLN03126 284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQK 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   318 KDVRRGNVAGDSKNDPPMEAagFTAQVIILNHP--GQIS---AGYAPVLDCHTAHIACKFAELKEKIDRRSgkkledgpK 392
Cdd:PLN03126 364 ADIQRGMVLAKPGSITPHTK--FEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------K 433
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4503471   393 FLKSGDAA--IVDMVpgKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 441
Cdd:PLN03126 434 MVMPGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
tufA CHL00071
elongation factor Tu
3-438 4.13e-52

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 180.92  E-value: 4.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAWVlDKLKAERERGITIDISLWKFET 82
Cdd:CHL00071   8 RKKPHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYET 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPy 162
Cdd:CHL00071  73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKEDQVDDE- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   163 sqKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANM-----PWFKgwKVtrkdgnasgTTLLEALDCILP 237
Cdd:CHL00071 145 --ELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgenKWVD--KI---------YNLMDAVDSYIP 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   238 -PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHEALSEALPGDNVGFNVKN 314
Cdd:CHL00071 212 tPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETktTTVTGLEMFQKTLDEGLAGDNVGILLRG 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   315 VSVKDVRRGNVAGDSKNDPPMeaAGFTAQVIILN------HPGqISAGYAPVLDCHTAHIACKFaelkekidrrsgkkle 388
Cdd:CHL00071 292 IQKEDIERGMVLAKPGTITPH--TKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKI---------------- 352
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503471   389 dgpKFLKSGDAAIVDMV-PGK--PMCVESFSdypPLG-----RFAVRDMRQTVAVGVI 438
Cdd:CHL00071 353 ---ESFTADDGSKTEMVmPGDriKMTVELIY---PIAiekgmRFAIREGGRTVGAGVV 404
PLN03127 PLN03127
Elongation factor Tu; Provisional
3-441 1.62e-51

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 180.41  E-value: 1.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03127  57 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYET 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPY 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   163 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNmlepsanmpwfkgwkvtRKDGNASGTTLLEALDCILP-PTRP 241
Cdd:PLN03127 195 LLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGTN-----------------DEIGKNAILKLMDAVDEYIPePVRV 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAP-VNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSV 317
Cdd:PLN03127 258 LDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKR 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   318 KDVRRGNVAgdSKNDPPMEAAGFTAQVIILN------HPGQISaGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGP 391
Cdd:PLN03127 338 EDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFS-NYRPQFYLRTADVTGKV-------------ELPEGV 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 4503471   392 KFLKSGDAAIVDMVPGKPMCVEsfsdypPLGRFAVRDMRQTVAVGVIKAV 441
Cdd:PLN03127 402 KMVMPGDNVTAVFELISPVPLE------PGQRFALREGGRTVGAGVVSKV 445
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
3-441 2.44e-49

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: 173.04  E-value: 2.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:TIGR00485   8 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYET 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPY 162
Cdd:TIGR00485  73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMVDDEE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    163 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnASGTTLLEALDCILP-PTRP 241
Cdd:TIGR00485 146 LLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWE-------------------AKILELMDAVDEYIPtPERE 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTE--VKSVEMHHEALSEALPGDNVGFNVKNVSVKD 319
Cdd:TIGR00485 207 IDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKttVTGVEMFRKELDEGRAGDNVGLLLRGIKREE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    320 VRRGNVAGDSKNDPPMEAagFTAQVIILN------HPGQISaGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGPKF 393
Cdd:TIGR00485 287 IERGMVLAKPGSIKPHTK--FEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDVTGTI-------------ELPEGVEM 350
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 4503471    394 LKSGD--AAIVDMVpgKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 441
Cdd:TIGR00485 351 VMPGDnvKMTVELI--SPIALEQGM------RFAIREGGRTVGAGVVSKI 392
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
8-325 3.30e-37

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: 143.90  E-value: 3.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFE-TSKYY 86
Cdd:COG3276   1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLGFAYLPlPDGRR 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREH-ALLAyTLGVKQLIVGVNKMDSTEPPys 163
Cdd:COG3276  53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAdeGVMP---------QTREHlAILD-LLGIKRGIVVLTKADLVDEE-- 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  164 qkRYEEIVKEVSTYIKkiGYNPDTVAFVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnasgttLLEALDCIL--PPTRP 241
Cdd:COG3276 121 --WLELVEEEIRELLA--GTFLEDAPIVPVSAVTGEGIDE------------------------LRAALDALAaaVPARD 172
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 321
Cdd:COG3276 173 ADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIE 252

                ....
gi 4503471  322 RGNV 325
Cdd:COG3276 253 RGDV 256
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
333-441 1.45e-35

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: 127.38  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    333 PPMEAAGFTAQVIILNH-----PGQISAGYAPVLDCHTAHIACKFAELKEKIDrrSGKKLEDgPKFLKSGDAAIVDMVPG 407
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 4503471    408 KPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 441
Cdd:pfam03143  78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
8-323 1.76e-33

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 133.07  E-value: 1.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFETSKYYV 87
Cdd:TIGR00475   1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDSTEppysqkry 167
Cdd:TIGR00475  53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDA-----DEGVMT--QTGEHLAVLDLLGIPHTIVVITKADRVN-------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    168 EEIVKEVSTYIKKIgynpdtvafvpisgwngdnmLEPSANMPWFKGWKVTRKDGNASG------TTLLEALDcilppTRP 241
Cdd:TIGR00475 118 EEEIKRTEMFMKQI--------------------LNSYIFLKNAKIFKTSAKTGQGIGelkkelKNLLESLD-----IKR 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 321
Cdd:TIGR00475 173 IQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLK 252

                  ..
gi 4503471    322 RG 323
Cdd:TIGR00475 253 RG 254
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
6-238 2.84e-33

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: 124.23  E-value: 2.84e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    6 THINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKY 85
Cdd:cd01884   1 PHVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANR 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVGVNKMDSTEPPysqk 165
Cdd:cd01884  66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVDDE---- 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503471  166 ryE--EIVK-EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKgwKVtrkdgnasgTTLLEALDCILPP 238
Cdd:cd01884 135 --EllELVEmEVRELLSKYGFDGDDTPIVRGSALKA---LEGDDPNKWVD--KI---------LELLDALDSYIPT 194
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
337-438 7.29e-31

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: 114.80  E-value: 7.29e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  337 AAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKleDGPKFLKSGDAAIVDMVPGKPMCVESFS 416
Cdd:cd01513   3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGK 80
                        90       100
                ....*....|....*....|..
gi 4503471  417 DYPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513  81 EFPTLGRFALRDGGRTVGAGLI 102
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
340-438 8.58e-26

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: 101.09  E-value: 8.58e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  340 FTAQVIILNHPGQI-SAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDY 418
Cdd:cd03704   6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
                        90       100
                ....*....|....*....|
gi 4503471  419 PPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03704  86 PQLGRFTLRDEGKTIAIGKV 105
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
10-199 6.98e-25

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: 100.37  E-value: 6.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETSKYyV 87
Cdd:cd04171   2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFayLDLPDGKR-L 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYTLGVKQLIVGVNKMDSTEPPysqkRY 167
Cdd:cd04171  53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVDED----RL 121
                       170       180       190
                ....*....|....*....|....*....|..
gi 4503471  168 EEIVKEVSTYIKKIGYNPDTVafVPISGWNGD 199
Cdd:cd04171 122 ELVEEEILELLAGTFLADAPI--FPVSSVTGE 151
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
340-441 4.89e-19

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: 82.21  E-value: 4.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  340 FTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYP 419
Cdd:cd04093   8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKDNK 87
                        90       100
                ....*....|....*....|..
gi 4503471  420 PLGRFAVRDMRQTVAVGVIKAV 441
Cdd:cd04093  88 ELGRFVLRRGGETIAAGIVTEI 109
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
246-325 6.88e-19

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: 80.77  E-value: 6.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNvsVKDVRRGNV 325
Cdd:cd01342   1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
9-238 1.73e-17

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 81.12  E-value: 1.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAaemgkGSFKYawvLDKLKAERERGITID---ISLwKFETSK- 84
Cdd:cd01885   2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   85 ------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTreHALL--AYTLGVKQLIVgVNK 154
Cdd:cd01885  66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAveGVCV---------QT--ETVLrqALEERVKPVLV-INK 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  155 MD------STEPPYSQKRYEEIVKEVSTYIKKIG---YNPDTVAFVPISGwngdNMLEPSAnmpwFKGWKVTRKDGNASG 225
Cdd:cd01885 134 IDrlilelKLSPEEAYQRLLRIVEDVNAIIETYApeeFKQEKWKFSPQKG----NVAFGSA----LDGWGFTIIKFADIY 205
                       250
                ....*....|...
gi 4503471  226 TTLLEALDCILPP 238
Cdd:cd01885 206 AVLEMVVKHLPSP 218
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
8-335 1.10e-16

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 81.82  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DISLWK--- 79
Cdd:PRK04000  10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKcpd 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    80 FETSKYYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN-----GQTREH 136
Cdd:PRK04000  62 CEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAA-----------NepcpqPQTKEH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   137 ALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTyikkigynpdTVA----FVPISGWNGDNMlepsanmpwfk 212
Cdd:PRK04000 131 LMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKG----------TVAenapIIPVSALHKVNI----------- 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   213 gwkvtrkDgnasgtTLLEALDCILP-PTRPTDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKPG 275
Cdd:PRK04000 190 -------D------ALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPG 256
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503471   276 MVVTFAP----VNVTTEVKSVEMHHEALSEALPGDNVGFNVK---NVSVKDVRRGNVAGDSKNDPPM 335
Cdd:PRK04000 257 IKVEEGGktkwEPITTKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPPV 323
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
7-323 2.18e-16

Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 81.60  E-value: 2.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMGkgsfkyAWVLDKLKAERERGITID---ISL-WKFE 81
Cdd:COG0481   5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   82 TSKYYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAA--GVgefEAgiskngQTREHALLAYTLGVKQLIVg 151
Cdd:COG0481  69 DGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDAsqGV---EA------QTLANVYLALENDLEIIPV- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  152 VNKMD--STEPpysqkryEEIVKEVstyIKKIGYNPDTVafVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnasgttLL 229
Cdd:COG0481 132 INKIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSAKTGIGIEE------------------------IL 175
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  230 EAL-DCILPPTRPTDKPLRlPL-----QDVYKiggiGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSV-----EMHH-E 297
Cdd:COG0481 176 EAIvERIPPPKGDPDAPLQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvftpKMTPvD 250
                       330       340
                ....*....|....*....|....*....
gi 4503471  298 ALSealPGDnVGF---NVKNvsVKDVRRG 323
Cdd:COG0481 251 ELS---AGE-VGYiiaGIKD--VRDARVG 273
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
9-156 3.37e-16

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: 77.66  E-value: 3.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaemgkGSfkyawV------LDKLKAERERGITIDISLWKFET 82
Cdd:cd04168   1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503471   83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTRE--HALLAYTLGVkqlIVGVNKMD 156
Cdd:cd04168  62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAveGV---------QAQTRIlfRLLRKLNIPT---IIFVNKID 127
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
248-325 5.94e-16

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 72.94  E-value: 5.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  248 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN--VTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:cd03697   3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKetLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
9-198 1.04e-15

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 74.88  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMgkgsfkYAWVLDKLKAERERGITID---ISL-WKFETSK 84
Cdd:cd01890   2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EM------KEQVLDSMDLERERGITIKaqaVRLfYKAKDGE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   85 YYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGVGeFEAgiskngQTREHALLAYTLGVKQLIVgVNKMD--STE 159
Cdd:cd01890  66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDlpAAD 135
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 4503471  160 PPYSQKRYEEIvkevstyikkIGYNPDTVafVPISGWNG 198
Cdd:cd01890 136 PDRVKQEIEDV----------LGLDASEA--ILVSAKTG 162
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
246-325 1.70e-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: 71.40  E-value: 1.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:cd03696   1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
260-325 1.30e-14

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: 68.45  E-value: 1.30e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503471    260 GTVPVGRVETGVLKPGMVVTFAPVNV-----TTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
9-212 2.90e-14

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 71.09  E-value: 2.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAAEMGKGsfkyawVLDKLKAERERGITIdisLWKfETSKYY-- 86
Cdd:cd01891   4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEAGISkngQTR---EHALLAytlGVKqLIVGVNKM 155
Cdd:cd01891  65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDA----SEGPMP---QTRfvlKKALEA---GLK-PIVVINKI 127
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503471  156 DSteppySQKRYEEIVKEVSTYIKKIGYNPDTVAFvPI------SGWNGDNMLEPSANM-PWFK 212
Cdd:cd01891 128 DR-----PDARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLdPLFE 185
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
8-203 4.01e-14

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


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 70.76  E-value: 4.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    8 INIVVIGHVDSGKSTTTGHLiykcGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DISLWKFET 82
Cdd:cd01888   1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   83 SKYY----------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN-----GQTRE 135
Cdd:cd01888  53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSE 121
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503471  136 HALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKevstYIKkiGYNPDTVAFVPIS---GWNGDNMLE 203
Cdd:cd01888 122 HLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVK--GTIAENAPIIPISaqlKYNIDVLCE 186
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
8-194 6.15e-14

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 eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 70.09  E-value: 6.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    8 INIVVIGHVDSGKSTTTghliykcggidkRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDISLWKF------- 80
Cdd:cd01889   1 VNVGLLGHVDSGKTSLA------------KALSEIASTAA------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   81 -------ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAYTLGvKQLIVGVN 153
Cdd:cd01889  57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4503471  154 KMDSTePPYSQKRYEEIVKEV--STYIKKIGYNpdtVAFVPIS 194
Cdd:cd01889 129 KIDLI-PEEERKRKIEKMKKRlqKTLEKTRLKD---SPIIPVS 167
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
245-328 9.96e-14

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 66.38  E-value: 9.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  245 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 324
Cdd:cd16267   1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80

                ....
gi 4503471  325 VAGD 328
Cdd:cd16267  81 ILCD 84
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
10-324 2.34e-13

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 72.01  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--SLWKFETSKYyV 87
Cdd:PRK10512   3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTREH-ALLAYTlGVKQLIVGVNKMDSTEPPYSQ 164
Cdd:PRK10512  54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACddGV---------MAQTREHlAILQLT-GNPMLTVALTKADRVDEARIA 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   165 KRYEEIVKEVSTYikkigynpdtvafvpisGWNGDNMLEPSANmpwfkgwkvtrkdgnaSGT---TLLEALDCILPPTRP 241
Cdd:PRK10512 124 EVRRQVKAVLREY-----------------GFAEAKLFVTAAT----------------EGRgidALREHLLQLPEREHA 170
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   242 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVK-NVSVKDV 320
Cdd:PRK10512 171 AQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQI 250

                 ....
gi 4503471   321 RRGN 324
Cdd:PRK10512 251 NRGD 254
PRK10218 PRK10218
translational GTPase TypA;
9-279 5.57e-13

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 70.89  E-value: 5.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKeaaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:PRK10218   7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYTLGVKQLIVgVNKMDSteppySQKRYE 168
Cdd:PRK10218  72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDR-----PGARPD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   169 EIVKEVSTYIKKIGYNPDTVAFvPI---SGWNGDNMLEpsanmpwfkgwkvtRKDGNASGTTLLEAL-DCILPPTRPTDK 244
Cdd:PRK10218 139 WVVDQVFDLFVNLDATDEQLDF-PIvyaSALNGIAGLD--------------HEDMAEDMTPLYQAIvDHVPAPDVDLDG 203
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 4503471   245 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVT 279
Cdd:PRK10218 204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
9-120 1.03e-12

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


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 70.07  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:COG0480  11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAATTCEWKGHKIN 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 4503471   89 IIDAPGHRDFIKNMITGTSQADCAVLIV--AAGV 120
Cdd:COG0480  78 IIDTPGHVDFTGEVERSLRVLDGAVVVFdaVAGV 111
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
9-211 2.32e-12

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: 66.14  E-value: 2.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKcggidkrtIEKFEKEAAEMGKgSFKYawvLDKLKAERERGITID---ISLwKFETSK- 84
Cdd:cd04167   2 NVCIAGHLHHGKTSLLDMLIEQ--------THKRTPSVKLGWK-PLRY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   85 --YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVgefeaGISKNG-QTREHALLaytLGVKQLIVgVNKMDS--TE 159
Cdd:cd04167  69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTeRLIRHAIQ---EGLPMVLV-INKIDRliLE 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503471  160 ---PP---YSQKRYeeIVKEVSTYIKKIGyNPDTVAFVPISGwngdNMLEPSANMPWF 211
Cdd:cd04167 140 lklPPtdaYYKLRH--TIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
PRK13351 PRK13351
elongation factor G-like protein;
9-156 2.60e-12

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 68.82  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAaemgkgsfkyawvlDKLKAERERGITIDISL----WKfets 83
Cdd:PRK13351  10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503471    84 KYYVTIIDAPGHRDFiknmitgTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVgVNKMD 156
Cdd:PRK13351  72 NHRINLIDTPGHIDF-------TGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIF-INKMD 136
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
9-279 2.70e-12

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 68.89  E-value: 2.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAAEMgkgsfkyawVLDKLKAERERGITIdisLWKfETSKYY-- 86
Cdd:COG1217   8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK-NTAVRYkg 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEagisknG---QTR---EHALlayTLGVKqLIVGV 152
Cdd:COG1217  69 vkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGLK-PIVVI 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  153 NKMDsteppysqK---RYEEIVKEVSTYIKKIGYNPDTVAFvPI------SGWNGDNMLEPSANMpwfkgwkvtrkdgna 223
Cdd:COG1217 129 NKID--------RpdaRPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDL--------------- 184
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503471  224 sgTTLLEA-LDCILPPTRPTDKPLRlpLQ------DVYkIGGIGtvpVGRVETGVLKPGMVVT 279
Cdd:COG1217 185 --TPLFDTiLEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVA 239
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
245-325 4.13e-12

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 61.73  E-value: 4.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  245 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 324
Cdd:cd04089   1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78

                .
gi 4503471  325 V 325
Cdd:cd04089  79 V 79
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
9-156 4.80e-12

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 66.08  E-value: 4.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaaemgkGSFkyawVLDKLKAERERGITIDISLWKFETSKYYV 87
Cdd:cd04170   1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503471   88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISknGQTREHALLAYTLGVKQLIVgVNKMD 156
Cdd:cd04170  67 NLIDTPGYADFVGETLSALRAVDAALIVVEA-----QSGVE--VGTEKVWEFLDDAKLPRIIF-INKMD 127
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
13-156 7.98e-12

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 67.46  E-value: 7.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503471    92 APGHRDFIKNMITGTSQADCAVLIVAAgVGEFEAgiskngQTRehALLAYT--LGVKQLIVgVNKMD 156
Cdd:PRK12740  67 TPGHVDFTGEVERALRVLDGAVVVVCA-VGGVEP------QTE--TVWRQAekYGVPRIIF-VNKMD 123
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
9-98 5.66e-11

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 62.89  E-value: 5.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITID---ISL-WKfetsK 84
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IGEVHGGGATM-----------DWMEQERERGITIQsaaTTCfWK----D 63
                        90
                ....*....|....
gi 4503471   85 YYVTIIDAPGHRDF 98
Cdd:cd01886  64 HRINIIDTPGHVDF 77
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
12-121 1.04e-10

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 62.23  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYAwVLDKLKAERERGITIDISLWKFETSKYYVTII 90
Cdd:cd04169   7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
                        90       100       110
                ....*....|....*....|....*....|.
gi 4503471   91 DAPGHRDFIKNMITGTSQADCAVLIVAAGVG 121
Cdd:cd04169  77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
245-328 1.11e-10

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: 57.90  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  245 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMH-HEALSEALPGDNVGFNVKNVSVKDVRRG 323
Cdd:cd03698   1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79

                ....*
gi 4503471  324 NVAGD 328
Cdd:cd03698  80 DILSS 84
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
9-185 2.77e-10

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: 60.00  E-value: 2.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaaemGKGSFKYAwvLDKLKAERERGITIDISL----------- 77
Cdd:cd04165   1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTSSVSNdilgfdsdgev 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   78 --WK-----------FETSKYYVTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGvgefeAGIskNGQTREHALLAYT 142
Cdd:cd04165  64 vnYPdnhlgeldveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGAN-----AGI--IGMTKEHLGLALA 136
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4503471  143 LGVKQLIVgVNKMDSTEppysqkryEEIVKEVSTYIKKIGYNP 185
Cdd:cd04165 137 LKVPVFVV-VTKIDMTP--------ANVLQETLKDLKRLLKSP 170
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
10-201 2.16e-09

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: 56.33  E-value: 2.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDISLWKFETSK 84
Cdd:cd01887   3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   85 YY--VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLAYTlgvkQLIVGVNKMD 156
Cdd:cd01887  47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAAddGVMP---------QTIEainHAKAANV----PIIVAINKID 112
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 4503471  157 stEPPYSQKRYEEIVKEVSTYikkiGYNPD----TVAFVPISGWNGDNM 201
Cdd:cd01887 113 --KPYGTEADPERVKNELSEL----GLVGEewggDVSIVPISAKTGEGI 155
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
252-325 2.74e-09

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: 53.76  E-value: 2.74e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503471  252 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN----VTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 325
Cdd:cd03694   7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
PRK07560 PRK07560
elongation factor EF-2; Reviewed
3-190 5.26e-09

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 58.34  E-value: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     3 KEKTHI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeAAEmgkgsfkyAWVLDKLKAERERGITID---ISLW 78
Cdd:PRK07560  15 KNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKaanVSMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    79 -KFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQT--------REHallaytlgVKQ 147
Cdd:PRK07560  80 hEYEGKEYLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAveGVMP---------QTetvlrqalRER--------VKP 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503471   148 LIVgVNKMD------STEPPYSQKRYEEIVKEVSTYIKkiGYNPD-------------TVAF 190
Cdd:PRK07560 143 VLF-INKVDrlikelKLTPQEMQQRLLKIIKDVNKLIK--GMAPEefkekwkvdvedgTVAF 201
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-98 1.20e-08

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 57.37  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAAEmgkgsfkyAWVLDKLKAERERGITID---ISL 77
Cdd:PTZ00416  13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
                         90       100
                 ....*....|....*....|....*...
gi 4503471    78 ---WKFETSK----YYVTIIDAPGHRDF 98
Cdd:PTZ00416  78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
8-203 2.47e-08

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 56.17  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaaemgkgsfkyawvldKLKAERERGITIDI-----SLWKFE- 81
Cdd:PTZ00327  35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLgyanaKIYKCPk 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    82 ---------------------------TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN---- 130
Cdd:PTZ00327  87 cprptcyqsygsskpdnppcpgcghkmTLKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAA-----------Nescp 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503471   131 -GQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKkigynpDTVAFVPIS---GWNGDNMLE 203
Cdd:PTZ00327 156 qPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIA------DNAPIIPISaqlKYNIDVVLE 226
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
246-325 8.82e-08

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.49  E-value: 8.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKN-VsvkDVRRGN 324
Cdd:cd03695   1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77

                .
gi 4503471  325 V 325
Cdd:cd03695  78 L 78
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
1-98 1.46e-07

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 53.96  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfEKEAAemgkGSFKYAwvlDKLKAERERGITID---ISL 77
Cdd:PLN00116  13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGII--------AQEVA----GDVRMT---DTRADEAERGITIKstgISL 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 4503471    78 W-------------KFETSKYYVTIIDAPGHRDF 98
Cdd:PLN00116  78 YyemtdeslkdfkgERDGNEYLINLIDSPGHVDF 111
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
11-203 5.50e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.30  E-value: 5.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETSKYYVT 88
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   89 IIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGVGEFEAGIskngqTREHALLAYTLGVKQLIVGvNKMDsteppys 163
Cdd:cd00882  51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKID------- 117
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4503471  164 qKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLE 203
Cdd:cd00882 118 -LLEEREVEELLRLEELAKILG--VPVFEVSAKTGEGVDE 154
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
394-429 7.65e-06

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270018  Cd Length: 100  Bit Score: 44.53  E-value: 7.65e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 4503471  394 LKSGDAAIVDMVpGKPMCVESFSDYPPLGRFAVRDM 429
Cdd:cd13197  37 METKALLLSLKY-GCFMWQLGDADTCFQIHSLENKM 71
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
340-404 1.62e-05

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: 43.28  E-value: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503471  340 FTAQVIILNHPGQISAGYAPVLDCHTAHIACKFaelkEKIDRrsgkkledgpKFLKSGDAAIVDM 404
Cdd:cd03708   6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDK----------EVLRTGDRALVRF 56
infB CHL00189
translation initiation factor 2; Provisional
10-203 1.28e-04

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 44.44  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    10 IVVIGHVDSGKSTTtghliykcggIDK-RTIEKFEKEAAemgkgsfkyawvldklkaererGITIDIS----LWKFETSK 84
Cdd:CHL00189 247 VTILGHVDHGKTTL----------LDKiRKTQIAQKEAG----------------------GITQKIGayevEFEYKDEN 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTRE---HALLAYTlgvkQLIVGVNKMDSTepp 161
Cdd:CHL00189 295 QKIVFLDTPGHEAFSSMRSRGANVTDIAILIIAA-----DDGVKP--QTIEainYIQAANV----PIIVAINKIDKA--- 360
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4503471   162 ysQKRYEEIVKEVSTY---IKKIGynpDTVAFVPIS---GWNGDNMLE 203
Cdd:CHL00189 361 --NANTERIKQQLAKYnliPEKWG---GDTPMIPISasqGTNIDKLLE 403
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
251-325 2.58e-04

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


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 39.59  E-value: 2.58e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503471  251 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfAPVNVTTeVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVRRGNV 325
Cdd:cd16265   6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKGVAL-IRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
prfC PRK00741
peptide chain release factor 3; Provisional
12-98 5.46e-04

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 42.43  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471    12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYA---WvldkLKAERERGITIDISLWKFETSKYYV 87
Cdd:PRK00741  15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81
                         90
                 ....*....|.
gi 4503471    88 TIIDAPGHRDF 98
Cdd:PRK00741  82 NLLDTPGHEDF 92
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
8-203 1.02e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 39.66  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471      8 INIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfekeaaEMGKGSFKYAWVLdklkAERERGITidislwkfetskYYV 87
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT------------EYYPGTTRNYVTT----VIEEDGKT------------YKF 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471     88 TIIDAPGHRDFIKNMITGTSQADcAVLIVAAG---VGEFEAGISKNGQTREHALlayTLGVKQLIVGvNKMDsteppysq 164
Cdd:TIGR00231  54 NLLDTAGQEDYDAIRRLYYPQVE-RSLRVFDIvilVLDVEEILEKQTKEIIHHA---DSGVPIILVG-NKID-------- 120
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 4503471    165 KRYEEIVKEVSTYIKKIGYNPdtvaFVPISGWNGDNMLE 203
Cdd:TIGR00231 121 LKDADLKTHVASEFAKLNGEP----IIPLSAETGKNIDS 155
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
10-233 1.27e-03

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 41.15  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   10 IVVI-GHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDISLWKFETS 83
Cdd:COG0532   6 VVTVmGHVDHGKTS------------------------------------LLDAIRktnvAAGEaGGITQHIGAYQVETN 49
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471   84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLAytlGVKqLIVGVNKMDst 158
Cdd:COG0532  50 GGKITFLDTPGHEAFTAMRARGAQVTDIVILVVAAddGVMP---------QTIEainHAKAA---GVP-IIVAINKID-- 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  159 eppysqkryeeivkevstyikKIGYNPDTV------------------AFVPISGWNGDN-------------MLEPSAN 207
Cdd:COG0532 115 ---------------------KPGANPDRVkqelaehglvpeewggdtIFVPVSAKTGEGidellemillqaeVLELKAN 173
                       250       260
                ....*....|....*....|....*..
gi 4503471  208 mpwfkgwkvtrKDGNASGTTlLEA-LD 233
Cdd:COG0532 174 -----------PDRPARGTV-IEAkLD 188
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
340-438 5.55e-03

Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 294005 [Multi-domain]  Cd Length: 93  Bit Score: 36.05  E-value: 5.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503471  340 FTAQVIILN------HPGqISAGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGPKFLKSGDAAIVDMVPGKPMCVE 413
Cdd:cd03706   6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRI-------------DLPEGKEMVMPGEDTSVKLTLLKPMVLE 71
                        90       100
                ....*....|....*....|....*
gi 4503471  414 sfsdypPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03706  72 ------KGQRFTLREGGRTIGTGVV 90
 
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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