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Conserved domains on  [gi|48735185|gb|AAH71619|]
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EEF1A1 protein [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
1-439 0e+00

elongation factor 1- alpha; Provisional


:

Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 868.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLA-------------------- 140
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAftlgvkqmivcinkmddktv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  141 -YSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGwkvtrkdgnasgTTLLEALDCILPPTR 219
Cdd:PTZ00141 161 nYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  220 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 299
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  300 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 379
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  380 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 439
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-439 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 868.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLA-------------------- 140
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAftlgvkqmivcinkmddktv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  141 -YSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGwkvtrkdgnasgTTLLEALDCILPPTR 219
Cdd:PTZ00141 161 nYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  220 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 299
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  300 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 379
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  380 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 439
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-423 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: 654.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:TIGR00483   1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagisKNGQTREHALLA-------------------Y 141
Cdd:TIGR00483  81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLArtlginqlivainkmdsvnY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   142 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPT 221
Cdd:TIGR00483 157 DEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEKPT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   222 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRR 301
Cdd:TIGR00483 225 DKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   302 GNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIV 381
Cdd:TIGR00483 305 GDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIV 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 48735185   382 DMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 423
Cdd:TIGR00483 384 KFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-424 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: 643.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:COG5256   1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLA-------------------Y 141
Cdd:COG5256  81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLArtlginqlivavnkmdavnY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 142 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPT 221
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEKPV 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 222 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRR 301
Cdd:COG5256 222 DKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 302 GNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIV 381
Cdd:COG5256 302 GDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIV 380
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 48735185 382 DMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKA 424
Cdd:COG5256 381 KIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
9-217 2.07e-138

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: 395.32  E-value: 2.07e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLA---------------------YSQKRYE 147
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLArtlgvkqlivavnkmddvtvnWSQERYD 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 148 EIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWkvtrkdgnasgtTLLEALDCILPP 217
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 ...
5-217 2.19e-68

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: 215.47  E-value: 2.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185     5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSK 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAY----------------SQKRYEE 148
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARqlgvpiivfinkmdrvDGAELEE 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   149 IVKEVS-TYIKKIGYNPDTVAFVPISGWNGDNMlepsanmpwfkgwkvtrkdgnasgTTLLEALDCILPP 217
Cdd:pfam00009 142 VVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-439 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 868.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PTZ00141   1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLA-------------------- 140
Cdd:PTZ00141  81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAftlgvkqmivcinkmddktv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  141 -YSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGwkvtrkdgnasgTTLLEALDCILPPTR 219
Cdd:PTZ00141 161 nYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  220 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 299
Cdd:PTZ00141 229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  300 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 379
Cdd:PTZ00141 309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  380 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKaagAGKVTKSAQKAQK 439
Cdd:PTZ00141 389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKK---EGSGTKAAAKAKK 445
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
1-436 0e+00

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 676.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:PLN00043   1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLA-------------------- 140
Cdd:PLN00043  81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAftlgvkqmicccnkmdattp 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  141 -YSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGwkvtrkdgnasgTTLLEALDCILPPTR 219
Cdd:PLN00043 161 kYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  220 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 299
Cdd:PLN00043 229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  300 RRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAA 379
Cdd:PLN00043 309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 48735185  380 IVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQK 436
Cdd:PLN00043 389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-423 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: 654.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185     1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:TIGR00483   1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagisKNGQTREHALLA-------------------Y 141
Cdd:TIGR00483  81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLArtlginqlivainkmdsvnY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   142 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPT 221
Cdd:TIGR00483 157 DEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEKPT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   222 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRR 301
Cdd:TIGR00483 225 DKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   302 GNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIV 381
Cdd:TIGR00483 305 GDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIV 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 48735185   382 DMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 423
Cdd:TIGR00483 384 KFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPT 425
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-424 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: 643.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKF 80
Cdd:COG5256   1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  81 ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLA-------------------Y 141
Cdd:COG5256  81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLArtlginqlivavnkmdavnY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 142 SQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPT 221
Cdd:COG5256 154 SEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEKPV 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 222 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRR 301
Cdd:COG5256 222 DKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 302 GNVAGDSKNdPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIV 381
Cdd:COG5256 302 GDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIV 380
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 48735185 382 DMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKA 424
Cdd:COG5256 381 KIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
3-423 0e+00

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 635.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PRK12317   2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKNGQTREHALLA-------------------YSQ 143
Cdd:PRK12317  82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLArtlginqlivainkmdavnYDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  144 KRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRPTDK 223
Cdd:PRK12317 157 KRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPTDK 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  224 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 303
Cdd:PRK12317 225 PLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  304 VAGdSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDM 383
Cdd:PRK12317 305 VCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKI 383
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 48735185  384 VPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKK 423
Cdd:PRK12317 384 KPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPA 423
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
9-217 2.07e-138

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: 395.32  E-value: 2.07e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLA---------------------YSQKRYE 147
Cdd:cd01883  81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLArtlgvkqlivavnkmddvtvnWSQERYD 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 148 EIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWkvtrkdgnasgtTLLEALDCILPP 217
Cdd:cd01883 161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
4-426 7.90e-82

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: 258.48  E-value: 7.90e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   4 EKTHINIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFE 81
Cdd:COG2895  14 NKDLLRFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  82 TSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLA------------------- 140
Cdd:COG2895  92 TPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDArkGVLE---------QTRRHSYIAsllgirhvvvavnkmdlvd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 141 YSQKRYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCILPPTRP 220
Cdd:COG2895 163 YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAEDR 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 221 TDKPLRLPLQDVYKiggigtvP-------VGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGF---- 289
Cdd:COG2895 229 NDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtled 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 290 NVknvsvkDVRRGNVAGDSkNDPPMEAAGFTAQVIILN-HPGQISAGYapVLDCHTAHIACKFAELKEKIDRRSGKKLEd 368
Cdd:COG2895 302 EI------DISRGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHEA- 371
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 369 gPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVIKAVDKKAAG 426
Cdd:COG2895 372 -ADSLELNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGALRRAAN 430
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
314-417 3.09e-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: 3.09e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 314 MEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVES 393
Cdd:cd03705   1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
                        90       100
                ....*....|....*....|....
gi 48735185 394 FSDYPPLGRFAVRDMRQTVAVGVI 417
Cdd:cd03705  81 FSEYPPLGRFAVRDMRQTVAVGVI 104
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
5-217 2.19e-68

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: 215.47  E-value: 2.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185     5 KTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSK 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALLAY----------------SQKRYEE 148
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARqlgvpiivfinkmdrvDGAELEE 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   149 IVKEVS-TYIKKIGYNPDTVAFVPISGWNGDNMlepsanmpwfkgwkvtrkdgnasgTTLLEALDCILPP 217
Cdd:pfam00009 142 VVEEVSrELLEKYGEDGEFVPVVPGSALKGEGV------------------------QTLLDALDEYLPS 187
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
221-311 1.46e-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: 194.33  E-value: 1.46e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 221 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVR 300
Cdd:cd03693   1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
                        90
                ....*....|.
gi 48735185 301 RGNVAGDSKND 311
Cdd:cd03693  81 RGDVAGDSKND 91
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
14-417 5.01e-50

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: 174.87  E-value: 5.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGK--GSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:TIGR02034   7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    92 APGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLA-------------------YSQKRYEEIVKE 152
Cdd:TIGR02034  87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIAsllgirhvvlavnkmdlvdYDEEVFENIKKD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   153 VSTYIKKIGynPDTVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPLRLPLQDV 232
Cdd:TIGR02034 160 YLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQYV 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   233 YKI-----GGIGTVPVGRVetgvlKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVRRGN--VA 305
Cdd:TIGR02034 226 NRPnldfrGYAGTIASGSV-----HVGDEVVVLPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGDllAA 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   306 GDSkndPPMEAAGFTAQVIIL-NHPgqISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEdgPKFLKSGDAAIVDMV 384
Cdd:TIGR02034 299 ADS---APEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGA--AKSLELNEIGRVNLS 371
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 48735185   385 PGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVI 417
Cdd:TIGR02034 372 LDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
14-441 1.27e-49

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 178.20  E-value: 1.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMG--KGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:PRK05506  31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   92 APGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLA-------------------YSQKRYEEIV 150
Cdd:PRK05506 111 TPGHEQYTRNMVTGASTADLAIILVDArkGVLT---------QTRRHSFIAsllgirhvvlavnkmdlvdYDQEVFDEIV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  151 KEVSTYIKKIGYNpdTVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPLRLPLQ 230
Cdd:PRK05506 182 ADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQ 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  231 DVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVgfnvkNVSVKD---VRRG 302
Cdd:PRK05506 248 YVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  303 NVAGDSkNDPPMEAAGFTAQVIILN----HPGqisAGYapVLDCHTAHIACKFAELKEKIDRRSgkkLEDGP-KFLKSGD 377
Cdd:PRK05506 318 DMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDVNT---LERLAaKTLELNE 388
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48735185  378 AAIVDMVPGKPMCVESFSDYPPLGRFAV--RDMRQTVAVGVIKAVDKKAAG----AGKVTK---SAQKAQKAK 441
Cdd:PRK05506 389 IGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIDFALRRATNvhwqASDVSRearAARKGQKPA 461
PRK12736 PRK12736
elongation factor Tu; Reviewed
1-422 1.45e-49

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 173.21  E-value: 1.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLiykcggidkrtiekfEKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12736   1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTAAI---------------TKVLAERGLNQAKDYDSIDAAPEEKERGITINT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYS------------- 142
Cdd:PRK12736  66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQvgvpylvvflnkv 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  143 -QKRYEEIVK----EVSTYIKKIGYNPDTVAFVPISGW---NGDNMLEPSANmpwfkgwkvtrkdgnasgtTLLEALDCI 214
Cdd:PRK12736 139 dLVDDEELLElvemEVRELLSEYDFPGDDIPVIRGSALkalEGDPKWEDAIM-------------------ELMDAVDEY 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  215 LP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVnVTTEVKSVEMHHEALSEALPGDNVGFN 290
Cdd:PRK12736 200 IPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVL 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  291 VKNVSVKDVRRGNVAGDSKNDPPmeAAGFTAQVIILN------HPGqISAGYAPVLDCHTAhiackfaelkekiDRRSGK 364
Cdd:PRK12736 279 LRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYILTkeeggrHTP-FFNNYRPQFYFRTT-------------DVTGSI 342
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 48735185  365 KLEDGPKFLKSGDAAIVDMVPGKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAVDK 422
Cdd:PRK12736 343 ELPEGTEMVMPGDNVTITVELIHPIAMEQGL------KFAIREGGRTVGAGTVTEILD 394
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
9-214 1.55e-49

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: 167.36  E-value: 1.55e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAAEMGKgsFKYAWVLDKLKAERERGITIDISLWKFETSKY 85
Cdd:cd04166   1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREHALLA-------------------YSQK 144
Cdd:cd04166  79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDArkGVLE---------QTRRHSYIAsllgirhvvvavnkmdlvdYDEE 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 145 RYEEIVKEVSTYIKKIGYNPdtVAFVPISGWNGDNMLEPSANMPWFKgwkvtrkdgnasGTTLLEALDCI 214
Cdd:cd04166 150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV 205
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
1-304 1.79e-49

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: 173.03  E-value: 1.79e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050   1 MAKEkfertKPHVNIGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAKAKAYDQIDKAPEEKERGITINT 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAysqkRY--------- 146
Cdd:COG0050  66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLA----RQvgvpyivvf 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 147 ---------EEIVK----EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEALD 212
Cdd:COG0050 135 lnkcdmvddEELLElvemEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKiLE------------LMDAVD 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 213 CILP-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPvNVTTEVKSVEMHHEALSEALPGDNVG 288
Cdd:COG0050 200 SYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVG 278
                       330
                ....*....|....*.
gi 48735185 289 FNVKNVSVKDVRRGNV 304
Cdd:COG0050 279 LLLRGIKREDVERGQV 294
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-304 6.85e-49

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 171.53  E-value: 6.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFK-YAWVlDKLKAERERGITID 74
Cdd:PRK00049   1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGAEAKaYDQI-DKAPEEKARGITIN 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   75 ISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLA----------YSQK 144
Cdd:PRK00049  65 TAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLArqvgvpyivvFLNK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  145 ----RYEEIVK----EVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEALDCIL 215
Cdd:PRK00049 138 cdmvDDEELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKiLE------------LMDAVDSYI 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  216 P-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHEALSEALPGDNVGFNV 291
Cdd:PRK00049 203 PtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGALL 281
                        330
                 ....*....|...
gi 48735185  292 KNVSVKDVRRGNV 304
Cdd:PRK00049 282 RGIKREDVERGQV 294
PRK12735 PRK12735
elongation factor Tu; Reviewed
1-304 2.87e-47

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 166.94  E-value: 2.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKE-----KTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735   1 MAKEkfertKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   76 SLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAySQKRYEEIV----- 150
Cdd:PRK12735  66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLA-RQVGVPYIVvflnk 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  151 --------------KEVSTYIKKIGYNPDTVAFVPISGWNGdnmLEPSANMPWFKG-WKvtrkdgnasgttLLEALDCIL 215
Cdd:PRK12735 138 cdmvddeellelveMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEAKiLE------------LMDAVDSYI 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  216 P-PTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHEALSEALPGDNVGFNV 291
Cdd:PRK12735 203 PePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVGVLL 281
                        330
                 ....*....|...
gi 48735185  292 KNVSVKDVRRGNV 304
Cdd:PRK12735 282 RGTKREDVERGQV 294
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
9-182 1.19e-46

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: 159.00  E-value: 1.19e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaaemgkgsfkyaWVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEfeagiskNGQTREHALLA----------------YSQKRYEEIVKE 152
Cdd:cd00881  66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAlagglpiivavnkidrVGEEDFDEVLRE 138
                       170       180       190
                ....*....|....*....|....*....|...
gi 48735185 153 VSTYIKKIGY---NPDTVAFVPISGWNGDNMLE 182
Cdd:cd00881 139 IKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
PLN03126 PLN03126
Elongation factor Tu; Provisional
3-420 2.62e-46

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 166.71  E-value: 2.62e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaaemgkgsfkyawvLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03126  77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLA--------------YSQKRYEE 148
Cdd:PLN03126 142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAkqvgvpnmvvflnkQDQVDDEE 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  149 IVK----EVSTYIKKIGYNPDTvafVPISGWNGDNMLEPSANMPwfkgwKVTRKDGNASGTT--LLEALDCILP-PTRPT 221
Cdd:PLN03126 215 LLElvelEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQRQT 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  222 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 299
Cdd:PLN03126 287 DLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADI 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  300 RRGNVAGDSKNDPPMEAagFTAQVIILNHP--GQIS---AGYAPVLDCHTAHIACKFAELKEKIDRRSgkkledgpKFLK 374
Cdd:PLN03126 367 QRGMVLAKPGSITPHTK--FEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKDEES--------KMVM 436
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 48735185  375 SGDAA--IVDMVpgKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 420
Cdd:PLN03126 437 PGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
tufA CHL00071
elongation factor Tu
3-417 8.99e-46

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 163.59  E-value: 8.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    3 KEKTHINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeAAEMGKGSFKYAWVlDKLKAERERGITIDISLWKFET 82
Cdd:CHL00071   8 RKKPHVNIGTIGHVDHGKTTLTAAITMTL--------------AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYET 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAY--------------SQKRYEE 148
Cdd:CHL00071  73 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKqvgvpnivvflnkeDQVDDEE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  149 IV----KEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANM-----PWFKgwKVtrkdgnasgTTLLEALDCILP-PT 218
Cdd:CHL00071 146 LLelveLEVRELLSKYDFPGDDIPIVSGSALLALEALTENPKIkrgenKWVD--KI---------YNLMDAVDSYIPtPE 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  219 RPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHEALSEALPGDNVGFNVKNVSV 296
Cdd:CHL00071 215 RDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETktTTVTGLEMFQKTLDEGLAGDNVGILLRGIQK 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  297 KDVRRGNVAGDSKNDPPMeaAGFTAQVIILN------HPGqISAGYAPVLDCHTAHIACKFaelkekidrrsgkkledgp 370
Cdd:CHL00071 295 EDIERGMVLAKPGTITPH--TKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKI------------------- 352
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 48735185  371 KFLKSGDAAIVDMV-PGK--PMCVESFSdypPLG-----RFAVRDMRQTVAVGVI 417
Cdd:CHL00071 353 ESFTADDGSKTEMVmPGDriKMTVELIY---PIAiekgmRFAIREGGRTVGAGVV 404
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
14-324 3.73e-45

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 163.16  E-value: 3.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   14 GHVDSGKSTTTGHLIYkcggiDKRTIekFEKEAAEMGKGSFK---------YAWVLDKLKAERERGITIDISLWKFETSK 84
Cdd:PRK05124  34 GSVDDGKSTLIGRLLH-----DTKQI--YEDQLASLHNDSKRhgtqgekldLALLVDGLQAEREQGITIDVAYRYFSTEK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   85 YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHA-------------------LLAYSQKR 145
Cdd:PRK05124 107 RKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSfiatllgikhlvvavnkmdLVDYSEEV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  146 YEEIVKEVSTYIKKIGYNPDtVAFVPISGWNGDNMLEPSANMPWFkgwkvtrkdgnaSGTTLLEALDCILPPTRPTDKPL 225
Cdd:PRK05124 180 FERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  226 RLPLQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVR 300
Cdd:PRK05124 247 RFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--DIS 319
                        330       340
                 ....*....|....*....|....
gi 48735185  301 RGNVAGDSKNDPPMeAAGFTAQVI 324
Cdd:PRK05124 320 RGDLLVAADEALQA-VQHASADVV 342
PLN03127 PLN03127
Elongation factor Tu; Provisional
3-420 4.02e-43

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 157.29  E-value: 4.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:PLN03127  57 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------KVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYET 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAysqkryeeivkevstyiKKIGY 162
Cdd:PLN03127 122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLA-----------------RQVGV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  163 nPDTVAFV-PISGWNGDNMLE---------------PSANMPWFKGWKVT----RKD--GNASGTTLLEALDCILP-PTR 219
Cdd:PLN03127 178 -PSLVVFLnKVDVVDDEELLElvemelrellsfykfPGDEIPIIRGSALSalqgTNDeiGKNAILKLMDAVDEYIPePVR 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  220 PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAP-VNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVS 295
Cdd:PLN03127 257 VLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLK 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  296 VKDVRRGNVAgdSKNDPPMEAAGFTAQVIILN------HPGQISaGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDG 369
Cdd:PLN03127 337 REDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFS-NYRPQFYLRTADVTGKV-------------ELPEG 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 48735185  370 PKFLKSGDAAIVDMVPGKPMCVEsfsdypPLGRFAVRDMRQTVAVGVIKAV 420
Cdd:PLN03127 401 VKMVMPGDNVTAVFELISPVPLE------PGQRFALREGGRTVGAGVVSKV 445
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
3-420 2.76e-42

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: 153.78  E-value: 2.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185     3 KEKTHINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFET 82
Cdd:TIGR00485   8 RTKPHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYET 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAysqkryeeivkevstyiKKIGY 162
Cdd:TIGR00485  73 ETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLA-----------------RQVGV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   163 nPDTVAFV-PISGWNGDNMLE---------------PSANMPWFKGWKVTRKDGNASGTT----LLEALDCILP-PTRPT 221
Cdd:TIGR00485 129 -PYIVVFLnKCDMVDDEELLElvemevrellsqydfPGDDTPIIRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREI 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   222 DKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTE--VKSVEMHHEALSEALPGDNVGFNVKNVSVKDV 299
Cdd:TIGR00485 208 DKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKttVTGVEMFRKELDEGRAGDNVGLLLRGIKREEI 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   300 RRGNVAGDSKNDPPMEAagFTAQVIILN------HPGQISaGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGPKFL 373
Cdd:TIGR00485 288 ERGMVLAKPGSIKPHTK--FEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDVTGTI-------------ELPEGVEMV 351
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 48735185   374 KSGD--AAIVDMVpgKPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 420
Cdd:TIGR00485 352 MPGDnvKMTVELI--SPIALEQGM------RFAIREGGRTVGAGVVSKI 392
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
312-420 9.36e-36

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: 9.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   312 PPMEAAGFTAQVIILNH-----PGQISAGYAPVLDCHTAHIACKFAELKEKIDrrSGKKLEDgPKFLKSGDAAIVDMVPG 386
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 48735185   387 KPMCVESFSdypplgRFAVRDMRQTVAVGVIKAV 420
Cdd:pfam03143  78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
8-304 1.96e-31

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: 126.95  E-value: 1.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFE-TSKYY 86
Cdd:COG3276   1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLGFAYLPlPDGRR 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVGEfeagiskngQTREH-ALLAYSQKRY------------EEIVK 151
Cdd:COG3276  53 LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAAdeGVMP---------QTREHlAILDLLGIKRgivvltkadlvdEEWLE 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 152 EVSTYIKkigynpdtvAFVPISGWNGDNMLEPSAnmpwfkgwkvtrkdgnASGT---TLLEALDCIL--PPTRPTDKPLR 226
Cdd:COG3276 124 LVEEEIR---------ELLAGTFLEDAPIVPVSA----------------VTGEgidELRAALDALAaaVPARDADGPFR 178
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48735185 227 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 304
Cdd:COG3276 179 LPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDV 256
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
316-417 4.99e-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: 4.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 316 AAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKleDGPKFLKSGDAAIVDMVPGKPMCVESFS 395
Cdd:cd01513   3 VWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGK 80
                        90       100
                ....*....|....*....|..
gi 48735185 396 DYPPLGRFAVRDMRQTVAVGVI 417
Cdd:cd01513  81 EFPTLGRFALRDGGRTVGAGLI 102
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
8-302 7.17e-27

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: 113.04  E-value: 7.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185     8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISLWKFETSKYYV 87
Cdd:TIGR00475   1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREHALLAYS-------------QKRYEEIVKEVS 154
Cdd:TIGR00475  53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDA-----DEGVMT--QTGEHLAVLDLlgiphtivvitkaDRVNEEEIKRTE 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   155 TYIKKIgynpdtvafvpisgwngdnmLEPSANMPWFKGWKVTRKDGNASG------TTLLEALDcilppTRPTDKPLRLP 228
Cdd:TIGR00475 126 MFMKQI--------------------LNSYIFLKNAKIFKTSAKTGQGIGelkkelKNLLESLD-----IKRIQKPLRMA 180
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48735185   229 LQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRG 302
Cdd:TIGR00475 181 IDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRG 254
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
6-140 1.26e-26

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: 105.74  E-value: 1.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   6 THINIVVIGHVDSGKSTTTGHLIYKCggidkrtiekfekeaAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKY 85
Cdd:cd01884   1 PHVNVGTIGHVDHGKTTLTAAITKVL---------------AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANR 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 48735185  86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLA 140
Cdd:cd01884  66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLA 113
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
319-417 7.19e-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: 7.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 319 FTAQVIILNHPGQI-SAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDY 397
Cdd:cd03704   6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
                        90       100
                ....*....|....*....|
gi 48735185 398 PPLGRFAVRDMRQTVAVGVI 417
Cdd:cd03704  86 PQLGRFTLRDEGKTIAIGKV 105
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
319-420 4.18e-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: 4.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 319 FTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYP 398
Cdd:cd04093   8 FEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPLETFKDNK 87
                        90       100
                ....*....|....*....|..
gi 48735185 399 PLGRFAVRDMRQTVAVGVIKAV 420
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 ...
225-304 5.58e-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: 81.16  E-value: 5.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 225 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNvsVKDVRRGNV 304
Cdd:cd01342   1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
10-136 8.75e-18

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: 80.34  E-value: 8.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDISL--WKFETSKYyV 87
Cdd:cd04171   2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLGFayLDLPDGKR-L 52
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 48735185  88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefEAGISKngQTREH 136
Cdd:cd04171  53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREH 94
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
227-304 4.89e-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: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 227 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN--VTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 304
Cdd:cd03697   3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKetLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
225-304 1.56e-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: 1.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 225 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 304
Cdd:cd03696   1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
239-304 1.08e-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: 68.83  E-value: 1.08e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48735185   239 GTVPVGRVETGVLKPGMVVTFAPVNV-----TTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 304
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
9-134 4.14e-14

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: 71.50  E-value: 4.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaemgkGSfkyawV------LDKLKAERERGITIDISLWKFET 82
Cdd:cd04168   1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 48735185  83 SKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTR 134
Cdd:cd04168  62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAveGV---------QAQTR 106
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
9-120 5.53e-14

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: 70.72  E-value: 5.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAaemgkGSFKYawvLDKLKAERERGITID---ISLwKFETSK- 84
Cdd:cd01885   2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 48735185  85 ------YYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GV 120
Cdd:cd01885  66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDAveGV 109
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
224-307 8.71e-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: 8.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 224 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 303
Cdd:cd16267   1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80

                ....
gi 48735185 304 VAGD 307
Cdd:cd16267  81 ILCD 84
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
9-140 1.36e-13

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: 68.71  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMgkgsfkYAWVLDKLKAERERGITID---ISL-WKFETSK 84
Cdd:cd01890   2 NFSIIAHIDHGKSTLADRLLELTGTVSER----------EM------KEQVLDSMDLERERGITIKaqaVRLfYKAKDGE 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 48735185  85 YYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGVGeFEAgiskngQTREHALLA 140
Cdd:cd01890  66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLA 115
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
7-302 5.78e-13

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 70.82  E-value: 5.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaaEMGkgsfkyAWVLDKLKAERERGITID---ISL-WKFE 81
Cdd:COG0481   5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER----------EMK------EQVLDSMDLERERGITIKaqaVRLnYKAK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  82 TSKYYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAA--GVgefEAgiskngQTREHALLAYSQK------- 144
Cdd:COG0481  69 DGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDAsqGV---EA------QTLANVYLALENDleiipvi 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 145 --------RYEEIVKEVstyIKKIGYNPDTVafVPISGWNGDNMLEpsanmpwfkgwkvtrkdgnasgttLLEAL-DCIL 215
Cdd:COG0481 133 nkidlpsaDPERVKQEI---EDIIGIDASDA--ILVSAKTGIGIEE------------------------ILEAIvERIP 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 216 PPTRPTDKPLRlPL-----QDVYKiggiGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSV-----EMHH-EALSealPG 284
Cdd:COG0481 184 PPKGDPDAPLQ-ALifdswYDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvftpKMTPvDELS---AG 255
                       330       340
                ....*....|....*....|.
gi 48735185 285 DnVGF---NVKNvsVKDVRRG 302
Cdd:COG0481 256 E-VGYiiaGIKD--VRDARVG 273
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
9-120 9.33e-13

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: 9.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:COG0480  11 NIGIVAHIDAGKTTLTERILFYTGAIHR--IGEVHDGNTVM-----------DWMPEEQERGITITSAATTCEWKGHKIN 77
                        90       100       110
                ....*....|....*....|....*....|....
gi 48735185  89 IIDAPGHRDFIKNMITGTSQADCAVLIV--AAGV 120
Cdd:COG0480  78 IIDTPGHVDFTGEVERSLRVLDGAVVVFdaVAGV 111
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
224-304 3.19e-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: 62.12  E-value: 3.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 224 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGN 303
Cdd:cd04089   1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78

                .
gi 48735185 304 V 304
Cdd:cd04089  79 V 79
PRK13351 PRK13351
elongation factor G-like protein;
9-121 5.06e-11

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 64.59  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAaemgkgsfkyawvlDKLKAERERGITIDISL----WKfets 83
Cdd:PRK13351  10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 48735185   84 KYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVG 121
Cdd:PRK13351  72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG 109
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
9-98 5.39e-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: 5.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtIEKFEKEAAEMgkgsfkyawvlDKLKAERERGITID---ISL-WKfetsK 84
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIHK--IGEVHGGGATM-----------DWMEQERERGITIQsaaTTCfWK----D 63
                        90
                ....*....|....
gi 48735185  85 YYVTIIDAPGHRDF 98
Cdd:cd01886  64 HRINIIDTPGHVDF 77
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
9-191 5.77e-11

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: 61.46  E-value: 5.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAAEMGKGsfkyawVLDKLKAERERGITIdisLWKfETSKYY-- 86
Cdd:cd01891   4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEAGISkngQTR---EHALLAY------------SQ 143
Cdd:cd01891  65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDA----SEGPMP---QTRfvlKKALEAGlkpivvinkidrPD 131
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 48735185 144 KRYEEIVKEVSTYIKKIGYNPDTVAFvPI------SGWNGDNMLEPSANM-PWFK 191
Cdd:cd01891 132 ARPEEVVDEVFDLFLELNATDEQLDF-PIvyasakNGWASLNLDDPSEDLdPLFE 185
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
8-139 7.67e-11

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: 61.23  E-value: 7.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   8 INIVVIGHVDSGKSTTTghliykcggidkRTIEKFEKEAAemgkgsfkyawvLDKLKAERERGITIDISLWKF------- 80
Cdd:cd01889   1 VNVGLLGHVDSGKTSLA------------KALSEIASTAA------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 48735185  81 -------ETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGefeagisKNGQTREHALL 139
Cdd:cd01889  57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVI 115
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
224-307 8.40e-11

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: 8.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 224 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMH-HEALSEALPGDNVGFNVKNVSVKDVRRG 302
Cdd:cd03698   1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79

                ....*
gi 48735185 303 NVAGD 307
Cdd:cd03698  80 DILSS 84
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
12-121 1.00e-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: 1.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYAwVLDKLKAERERGITIDISLWKFETSKYYVTII 90
Cdd:cd04169   7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
                        90       100       110
                ....*....|....*....|....*....|.
gi 48735185  91 DAPGHRDFIKNMITGTSQADCAVLIVAAGVG 121
Cdd:cd04169  77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
8-314 1.18e-10

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 62.95  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaaemgkgsfkyaWVlDKLKAERERGITI-----DISLWK--- 79
Cdd:PRK04000  10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKcpd 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   80 FETSKYYVT------------------IIDAPGHRDFIKNMITGTSQADCAVLIVAAgvgefeagiskN-----GQTREH 136
Cdd:PRK04000  62 CEEPEAYTTepkcpncgsetellrrvsFVDAPGHETLMATMLSGAALMDGAILVIAA-----------NepcpqPQTKEH 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  137 aLLAY------------------SQKR----YEEIVKEVSTyikkigynpdTVA----FVPISGWNGDNMlepsanmpwf 190
Cdd:PRK04000 131 -LMALdiigiknivivqnkidlvSKERalenYEQIKEFVKG----------TVAenapIIPVSALHKVNI---------- 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  191 kgwkvtrkDgnasgtTLLEALDCILP-PTRPTDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKP 253
Cdd:PRK04000 190 --------D------ALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRP 255
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48735185  254 GMVVTFAP----VNVTTEVKSVEMHHEALSEALPGDNVGFNVK---NVSVKDVRRGNVAGDSKNDPPM 314
Cdd:PRK04000 256 GIKVEEGGktkwEPITTKIVSLRAGGEKVEEARPGGLVGVGTKldpSLTKADALAGSVAGKPGTLPPV 323
PRK10218 PRK10218
translational GTPase TypA;
9-258 1.36e-10

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 63.19  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKeaaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSKYYVT 88
Cdd:PRK10218   7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA-ETQER--------------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEagiskngQTREHALLAYSQKrYEEIVkeVSTYIKKIGYNPDTVA 168
Cdd:PRK10218  72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYG-LKPIV--VINKVDRPGARPDWVV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  169 ------FVPISGwnGDNMLE-PSANMPWFKGWK-VTRKDGNASGTTLLEAL-DCILPPTRPTDKPLRLPLQDVYKIGGIG 239
Cdd:PRK10218 142 dqvfdlFVNLDA--TDEQLDfPIVYASALNGIAgLDHEDMAEDMTPLYQAIvDHVPAPDVDLDGPFQMQISQLDYNSYVG 219
                        250
                 ....*....|....*....
gi 48735185  240 TVPVGRVETGVLKPGMVVT 258
Cdd:PRK10218 220 VIGIGRIKRGKVKPNQQVT 238
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
9-118 1.49e-10

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: 61.46  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaaemgkGSFkyawVLDKLKAERERGITIDISLWKFETSKYYV 87
Cdd:cd04170   1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
                        90       100       110
                ....*....|....*....|....*....|.
gi 48735185  88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAA 118
Cdd:cd04170  67 NLIDTPGYADFVGETLSALRAVDAALIVVEA 97
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
13-120 1.85e-10

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 62.84  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAaemgkgsfkyawVLDKLKAERERGITIDISLWKFETSKYYVTIID 91
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
                         90       100       110
                 ....*....|....*....|....*....|.
gi 48735185   92 APGHRDFIKNMITGTSQADCAVLIVAA--GV 120
Cdd:PRK12740  67 TPGHVDFTGEVERALRVLDGAVVVVCAvgGV 97
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
9-116 5.87e-10

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: 58.82  E-value: 5.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKcggidkrtIEKFEKEAAEMGKgSFKYawvLDKLKAERERGITID---ISLwKFETSK- 84
Cdd:cd04167   2 NVCIAGHLHHGKTSLLDMLIEQ--------THKRTPSVKLGWK-PLRY---TDTRKDEQERGISIKsnpISL-VLEDSKg 68
                        90       100       110
                ....*....|....*....|....*....|....
gi 48735185  85 --YYVTIIDAPGHRDFIKNMITGTSQADCAVLIV 116
Cdd:cd04167  69 ksYLINIIDTPGHVNFMDEVAAALRLCDGVVLVV 102
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
231-304 2.37e-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: 54.15  E-value: 2.37e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48735185 231 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN----VTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNV 304
Cdd:cd03694   7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
9-258 6.76e-09

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 57.72  E-value: 6.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAAEMgkgsfkyawVLDKLKAERERGITIdisLWKfETSKYY-- 86
Cdd:COG1217   8 NIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK-NTAVRYkg 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgvgeFEagisknG---QTR---EHALlaySQK-------- 144
Cdd:COG1217  69 vkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELGlkpivvin 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 145 -------RYEEIVKEVSTYIKKIGYNPDTVAFvPI------SGWNGDNMLEPSANMpwfkgwkvtrkdgnasgTTLLEA- 210
Cdd:COG1217 130 kidrpdaRPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDL-----------------TPLFDTi 191
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 48735185 211 LDCILPPTRPTDKPLRlpLQ------DVYkIGGIGtvpVGRVETGVLKPGMVVT 258
Cdd:COG1217 192 LEHVPAPEVDPDGPLQ--MLvtnldySDY-VGRIA---IGRIFRGTIKKGQQVA 239
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-98 1.02e-08

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 57.37  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAAEmgkgsfkyAWVLDKLKAERERGITID---ISL 77
Cdd:PTZ00416  13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNAGD--------ARFTDTRADEQERGITIKstgISL 77
                         90       100
                 ....*....|....*....|....*...
gi 48735185   78 ---WKFETSK----YYVTIIDAPGHRDF 98
Cdd:PTZ00416  78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
PRK07560 PRK07560
elongation factor EF-2; Reviewed
3-98 1.16e-08

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 57.18  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    3 KEKTHI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeAAEmgkgsfkyAWVLDKLKAERERGITID---ISLW 78
Cdd:PRK07560  15 KNPEQIrNIGIIAHIDHGKTTLSDNLLAGAGMISEEL-------AGE--------QLALDFDEEEQARGITIKaanVSMV 79
                         90       100
                 ....*....|....*....|.
gi 48735185   79 -KFETSKYYVTIIDAPGHRDF 98
Cdd:PRK07560  80 hEYEGKEYLINLIDTPGHVDF 100
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
10-139 1.21e-08

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 56.98  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDI--SLWKFETSKYyV 87
Cdd:PRK10512   3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 48735185   88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAA--GVgefeagiskNGQTREH-ALL 139
Cdd:PRK10512  54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACddGV---------MAQTREHlAIL 99
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
225-304 8.39e-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: 8.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 225 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKN-VsvkDVRRGN 303
Cdd:cd03695   1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77

                .
gi 48735185 304 V 304
Cdd:cd03695  78 L 78
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
1-98 1.32e-07

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 53.96  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185    1 MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfEKEAAemgkGSFKYAwvlDKLKAERERGITID---ISL 77
Cdd:PLN00116  13 MDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGII--------AQEVA----GDVRMT---DTRADEAERGITIKstgISL 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 48735185   78 W-------------KFETSKYYVTIIDAPGHRDF 98
Cdd:PLN00116  78 YyemtdeslkdfkgERDGNEYLINLIDSPGHVDF 111
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
373-408 6.71e-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: 6.71e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 48735185 373 LKSGDAAIVDMVpGKPMCVESFSDYPPLGRFAVRDM 408
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 ...
319-383 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: 42.89  E-value: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48735185 319 FTAQVIILNHPGQISAGYAPVLDCHTAHIACKFaelkEKIDRrsgkkledgpKFLKSGDAAIVDM 383
Cdd:cd03708   6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDK----------EVLRTGDRALVRF 56
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
10-180 7.26e-05

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


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 43.23  E-value: 7.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaaemgkgsfkyawVLDKLK----AERE-RGITIDISLWKFETSK 84
Cdd:cd01887   3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185  85 YY--VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAA--GVGEfeagiskngQTRE---HALLA--------------YS 142
Cdd:cd01887  47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAAddGVMP---------QTIEainHAKAAnvpiivainkidkpYG 116
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 48735185 143 QKRYEEIVKEVstyIKKIGYNPD----TVAFVPISGWNGDNM 180
Cdd:cd01887 117 TEADPERVKNE---LSELGLVGEewggDVSIVPISAKTGEGI 155
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
230-304 2.36e-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: 2.36e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48735185 230 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfAPVNVTTeVKSVEMHHEALSEALPGDNVGFNVKNVSvkDVRRGNV 304
Cdd:cd16265   6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKGVAL-IRAIEREHRKVDFAVAGDEVALILEGKI--KVKEGDV 75
prfC PRK00741
peptide chain release factor 3; Provisional
12-98 5.09e-04

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 42.43  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185   12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAAEM-GKGSFKYA---WvldkLKAERERGITIDISLWKFETSKYYV 87
Cdd:PRK00741  15 IISHPDAGKTTLTEKLLLFGGAI---------QEAGTVkGRKSGRHAtsdW----MEMEKQRGISVTSSVMQFPYRDCLI 81
                         90
                 ....*....|.
gi 48735185   88 TIIDAPGHRDF 98
Cdd:PRK00741  82 NLLDTPGHEDF 92
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
319-417 4.43e-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: 36.44  E-value: 4.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48735185 319 FTAQVIILN------HPGqISAGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDGPKFLKSGDAAIVDMVPGKPMCVE 392
Cdd:cd03706   6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRI-------------DLPEGKEMVMPGEDTSVKLTLLKPMVLE 71
                        90       100
                ....*....|....*....|....*
gi 48735185 393 sfsdypPLGRFAVRDMRQTVAVGVI 417
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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