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Conserved domains on  [gi|1814598424|ref|XP_032528018|]
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elongation factor 1-alpha [Danaus plexippus plexippus]

Protein Classification

elongation factor 1-alpha( domain architecture ID 11488101)

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

Graphical summary

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List of domain hits

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

elongation factor 1- alpha; Provisional


:

Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 902.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141    1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141   81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 PYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKGwqierkegkaegKCLIEALDAILPPAR 240
Cdd:PTZ00141  161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:PTZ00141  229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:PTZ00141  309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKEaggGKVTKAAEKATK 460
Cdd:PTZ00141  389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKE---GSGTKAAAKAKK 445
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-460 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 902.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141    1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141   81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 PYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKGwqierkegkaegKCLIEALDAILPPAR 240
Cdd:PTZ00141  161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:PTZ00141  229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:PTZ00141  309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKEaggGKVTKAAEKATK 460
Cdd:PTZ00141  389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKE---GSGTKAAAKAKK 445
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-445 0e+00

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 678.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256     1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256    81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 pYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPAR 240
Cdd:COG5256   153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:COG5256   220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSkNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:COG5256   300 KRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKE 445
Cdd:COG5256   379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-445 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: 675.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483   1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483  81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 pYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPAR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSKnNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKE 445
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
9-238 1.23e-157

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: 445.01  E-value: 1.23e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKFYVT 88
Cdd:cd01883     1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSESRFE 168
Cdd:cd01883    81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 169 EIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKGWqierkegkaegkCLIEALDAILPP 238
Cdd:cd01883   161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
5-238 1.26e-74

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: 232.42  E-value: 1.26e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   5 KIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETAK 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  85 FYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySE 164
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 165 SRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEqstkmpwfkgwqierkegkaegkcLIEALDAILPP 238
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-460 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 902.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PTZ00141    1 MGKEKTHINLVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PTZ00141   81 ETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDDKTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 PYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKGwqierkegkaegKCLIEALDAILPPAR 240
Cdd:PTZ00141  161 NYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:PTZ00141  229 PVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:PTZ00141  309 KRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAA 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKEaggGKVTKAAEKATK 460
Cdd:PTZ00141  389 IVKMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVGVIKSVEKKE---GSGTKAAAKAKK 445
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
1-457 0e+00

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 699.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:PLN00043    1 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEP 160
Cdd:PLN00043   81 ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 PYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPAR 240
Cdd:PLN00043  161 KYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYK------------GPTLLEALDQINEPKR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:PLN00043  229 PSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:PLN00043  309 KRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAG 388
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKEAGGGKVTKAAEK 457
Cdd:PLN00043  389 FVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAK 445
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-445 0e+00

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 678.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:COG5256     1 MASEKPHLNLVVIGHVDHGKSTLVGRLLYETGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:COG5256    81 ETDKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVN- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 pYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPAR 240
Cdd:COG5256   153 -YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYN------------GPTLLEALDNLKEPEK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:COG5256   220 PVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSkNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:COG5256   300 KRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAA 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKE 445
Cdd:COG5256   379 IVKIKPTKPLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKPKK 423
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
1-445 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: 675.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKF 80
Cdd:TIGR00483   1 MAKEKEHINVAFIGHVDHGKSTTVGHLLYKCGAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagisKNGQTREHALLAFTLGVKQLIVGVNKMDSTEp 160
Cdd:TIGR00483  81 ETDKYEVTIVDCPGHRDFIKNMITGASQADAAVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVN- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 161 pYSESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPAR 240
Cdd:TIGR00483 156 -YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYK------------GKTLLEALDALEPPEK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 241 PTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKEL 320
Cdd:TIGR00483 223 PTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 321 RRGYVAGDSKnNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAA 400
Cdd:TIGR00483 303 RRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAA 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1814598424 401 IVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKE 445
Cdd:TIGR00483 382 IVKFKPTKPMVIEAVKEIPPLGRFAIRDMGQTVAAGMIIDVDPTK 426
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
3-445 0e+00

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 668.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   3 KEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFET 82
Cdd:PRK12317    2 KEKPHLNLAVIGHVDHGKSTLVGRLLYETGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  83 AKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEppY 162
Cdd:PRK12317   82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVN--Y 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 163 SESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPARPT 242
Cdd:PRK12317  155 DEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYN------------GPTLLEALDNLKPPEKPT 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 243 DKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRR 322
Cdd:PRK12317  223 DKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 323 GYVAGdSKNNPPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAAIV 402
Cdd:PRK12317  303 GDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIV 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1814598424 403 NLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKSVTHKE 445
Cdd:PRK12317  382 KIKPTKPLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKPAK 424
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
9-238 1.23e-157

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: 445.01  E-value: 1.23e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKFYVT 88
Cdd:cd01883     1 NLVVIGHVDAGKSTLTGHLLYKLGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSESRFE 168
Cdd:cd01883    81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 169 EIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEQSTKMPWFKGWqierkegkaegkCLIEALDAILPP 238
Cdd:cd01883   161 EIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
9-447 1.53e-96

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: 297.00  E-value: 1.53e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DKrtIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETA--K 84
Cdd:COG2895    19 RFITCGSVDDGKSTLIGRLLYDTKSIfeDQ--LAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPkrK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  85 FyvTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSE 164
Cdd:COG2895    97 F--IIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 165 SRFEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAILPPARPTDK 244
Cdd:COG2895   166 EVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAEDRNDA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 245 ALRLPLQDVYKiggigtvP-------VGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVK---N 314
Cdd:COG2895   232 PFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEdeiD 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 315 VSvkelrRGYVAGDSkNNPPKGAADFTAQVIVLN-HPGQISNGYtpVLDCHTAHIACKFAEIKEKVDRRSGksTEENPKS 393
Cdd:COG2895   305 IS-----RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTL--EHEAADS 374
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1814598424 394 IKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAV--RDMRQTVAVGVIKSVTHKEAG 447
Cdd:COG2895   375 LELNDIGRVTLRLAEPIAFDPYADNRATGSFILidRLTNATVGAGMIRGALRRAAN 430
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
5-238 1.26e-74

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: 232.42  E-value: 1.26e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   5 KIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETAK 84
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEA------------GLDNLPEERERGITIKSAAVSFETKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  85 FYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKqLIVGVNKMDSTeppySE 164
Cdd:pfam00009  69 YLINLIDTPGHVDFVKEVIRGLAQADGAILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DG 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 165 SRFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEqstkmpwfkgwqierkegkaegkcLIEALDAILPP 238
Cdd:pfam00009 137 AELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------------------------LLDALDEYLPS 187
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
335-438 9.65e-71

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: 219.37  E-value: 9.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 335 KGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAAIVNLVPSKPLCVEA 414
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80
                          90       100
                  ....*....|....*....|....
gi 1814598424 415 FQEFPPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03705    81 FSEYPPLGRFAVRDMRQTVAVGVI 104
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
14-438 1.08e-65

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: 216.47  E-value: 1.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGK--GSFKYAWVLDKLKAERERGITIDIALWKFETAKFYVTIID 91
Cdd:TIGR02034   7 GSVDDGKSTLIGRLLHDTKQIYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  92 APGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSESRFEEIK 171
Cdd:TIGR02034  87 TPGHEQYTRNMATGASTADLAVLLVDARKGVLE-------QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 172 KEVSSYIKKIGynPAAVAFVPISGWHGDNMLEQSTKMPWFkgwqierkegkaEGKCLIEALDAILPPARPTDKALRLPLQ 251
Cdd:TIGR02034 158 KDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY------------SGPTLLEILETVEVERDAQDLPLRFPVQ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 252 DVYKI-----GGIGTVPVGRVETGvlkpGTIVVfAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSvkELRRG--Y 324
Cdd:TIGR02034 224 YVNRPnldfrGYAGTIASGSVHVG----DEVVV-LPSGRSSRVARIVTFDGDLEQARAGQAVTLTLDDEI--DISRGdlL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 325 VAGDsknNPPKGAADFTAQVIVL-NHPgqISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEEnpKSIKSGDAAIVN 403
Cdd:TIGR02034 297 AAAD---SAPEVADQFAATLVWMaEEP--LLPGRSYDLKLGTRKVRASVAAIKHKVDVNTLEKGAA--KSLELNEIGRVN 369
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1814598424 404 LVPSKPLCVEAFQEFPPLGRFAV--RDMRQTVAVGVI 438
Cdd:TIGR02034 370 LSLDEPIAFDPYAENRTTGAFILidRLSNRTVGAGMI 406
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
14-463 1.10e-62

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 214.41  E-value: 1.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  14 GHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMG--KGSFKYAWVLDKLKAERERGITIDIALWKFETAKFYVTIID 91
Cdd:PRK05506   31 GSVDDGKSTLIGRLLYDSKMIFEDQLAALERDSKKVGtqGDEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVAD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  92 APGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSESRFEEIK 171
Cdd:PRK05506  111 TPGHEQYTRNMVTGASTADLAIILVDARKGVLT-------QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 172 KEVSSYIKKIGYnpAAVAFVPISGWHGDNMLEQSTKMPWFkgwqierkegkaEGKCLIEALDAILPPARPTDKALRLPLQ 251
Cdd:PRK05506  182 ADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQ 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 252 DVYKI-----GGIGTvpvgrVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKN---VSvkelrRG 323
Cdd:PRK05506  248 YVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADeidIS-----RG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 324 YVAGDSkNNPPKGAADFTAQVIVLN----HPGqisNGYtpVLDCHTAHIACKFAEIKEKVD-----RRSGKSTEENpksi 394
Cdd:PRK05506  318 DMLARA-DNRPEVADQFDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDvntleRLAAKTLELN---- 387
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 395 ksgDAAIVNLVPSKPLCVEAFQEFPPLGRFAV--RDMRQTVAVGVIKSVTHKEAG----GGKVTKAAEKATKGKK 463
Cdd:PRK05506  388 ---EIGRCNLSTDAPIAFDPYARNRTTGSFILidRLTNATVGAGMIDFALRRATNvhwqASDVSREARAARKGQK 459
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
9-240 3.99e-62

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: 200.87  E-value: 3.99e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGI--DK-RTIEKFEKEAQEMGKgsFKYAWVLDKLKAERERGITIDIALWKFETAKF 85
Cdd:cd04166     1 RFITCGSVDDGKSTLIGRLLYDSKSIfeDQlAALERSKSSGTQGEK--LDLALLVDGLQAEREQGITIDVAYRYFSTPKR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSES 165
Cdd:cd04166    79 KFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLE-------QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 166 RFEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEQSTKMPWFKgwqierkegkaeGKCLIEALDAIlPPAR 240
Cdd:cd04166   150 VFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETV-EIAS 209
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
242-332 3.09e-57

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: 183.93  E-value: 3.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 242 TDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELR 321
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80
                          90
                  ....*....|.
gi 1814598424 322 RGYVAGDSKNN 332
Cdd:cd03693    81 RGDVAGDSKND 91
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
9-203 1.91e-55

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: 182.49  E-value: 1.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFekeaqemgkgsfkyaWVLDKLKAERERGITIDIALWKFETAKFYVT 88
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE---------------TFLDTLKEERERGITIKTGVVEFEWPKRRIN 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEfeagiskNGQTREHALLAFtLGVKQLIVGVNKMDSTeppySESRFE 168
Cdd:cd00881    66 FIDTPGHEDFSKETVRGLAQADGALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFD 133
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1814598424 169 EIKKEVSSYIKKIGY---NPAAVAFVPISGWHGDNMLE 203
Cdd:cd00881   134 EVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
14-456 6.22e-55

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 190.12  E-value: 6.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  14 GHVDSGKSTTTGHLIYkcggiDKRTI-----EKFEKEAQEMGKGSFK--YAWVLDKLKAERERGITIDIALWKFETAKFY 86
Cdd:PRK05124   34 GSVDDGKSTLIGRLLH-----DTKQIyedqlASLHNDSKRHGTQGEKldLALLVDGLQAEREQGITIDVAYRYFSTEKRK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  87 VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppYSESR 166
Cdd:PRK05124  109 FIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLD-------QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 167 FEEIKKEVSSYIKKIGYNPaAVAFVPISGWHGDNMLEQSTKMPWFkgwqierkegkaEGKCLIEALDAILPPARPTDKAL 246
Cdd:PRK05124  180 FERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 247 RLPLQDVYKI-----GGIGTvpvgrVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKN---VSvk 318
Cdd:PRK05124  247 RFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDeidIS-- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 319 elrRGYVAGDSKNNPPKGAAdFTAQVIVLNH----PGQ-----ISNGYTPVldchtahiacKFAEIKEKVDRRSGK--ST 387
Cdd:PRK05124  320 ---RGDLLVAADEALQAVQH-ASADVVWMAEqplqPGQsydikIAGKKTRA----------RVDAIRYQVDINTLTqrEA 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814598424 388 EENPKSiksgDAAIVNLVPSKPLCVEAFQEFPPLGRFAV--RDMRQTVAVGVIKSVTHKEAGGGKVTKAAE 456
Cdd:PRK05124  386 ENLPLN----GIGLVELTFDEPLVLDPYQQNRVTGGFIFidRLTNVTVGAGMVREPLAQATAAPSEFSAFE 452
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
1-438 2.39e-54

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: 186.51  E-value: 2.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKI-----HINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKfekeaqemGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:COG0050     1 MAKEKFertkpHVNIGTIGHVDHGKTTLTA-------AITKVLAKK--------GGAKAKAYDQIDKAPEEKERGITINT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  76 ALWKFETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:COG0050    66 SHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 156 DSTEPPYSESRFE-EIKKEVSSYikkiGYNPAAVAFVPISGWhgdNMLEQSTKMPWFKgwQIERkegkaegkcLIEALDA 234
Cdd:COG0050   139 DMVDDEELLELVEmEVRELLSKY----GFPGDDTPIIRGSAL---KALEGDPDPEWEK--KILE---------LMDAVDS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 235 ILP-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---IVVFAPANITTeVKSVEMHHEALQEAVPGDNVGF 310
Cdd:COG0050   201 YIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDeveIVGIRDTQKTV-VTGVEMFRKLLDEGEAGDNVGL 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 311 NVKNVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVLN-------HPgqISNGYTPVLDCHTAHI--ACKFAEIKEKVdr 381
Cdd:COG0050   280 LLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVLSkeeggrhTP--FFNGYRPQFYFRTTDVtgVITLPEGVEMV-- 353
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1814598424 382 rsgksteeNPksiksGDAA--IVNLVpsKPLCVEAFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:COG0050   354 --------MP-----GDNVtmTVELI--TPIAMEEGL------RFAIREGGRTVGAGVV 391
tufA CHL00071
elongation factor Tu
1-438 3.63e-53

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 183.62  E-value: 3.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDI 75
Cdd:CHL00071    1 MAREKFerkkpHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDE---------------IDSAPEEKARGITINT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  76 ALWKFETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:CHL00071   66 AHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 156 DSTEppySESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEQSTKMPwfkgwQIERKEGKAEGKC--LIEALD 233
Cdd:CHL00071  139 DQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-----KIKRGENKWVDKIynLMDAVD 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 234 AILP-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPANITTeVKSVEMHHEALQEAVPGDNVG 309
Cdd:CHL00071  208 SYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGdtvEIVGLRETKTTT-VTGLEMFQKTLDEGLAGDNVG 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 310 FNVKNVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVLN------HPGqISNGYTPVLDCHTAHIACKFAEIKEkvdrrs 383
Cdd:CHL00071  287 ILLRGIQKEDIERGMVL--AKPGTITPHTKFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKIESFTA------ 357
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 384 gkSTEENPKSIKSGDAAIVNLVPSKPLCVEAFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:CHL00071  358 --DDGSKTEMVMPGDRIKMTVELIYPIAIEKGM------RFAIREGGRTVGAGVV 404
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-347 3.66e-53

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 183.47  E-value: 3.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKI-----HINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK00049    1 MAKEKFertkpHVNVGTIGHVDHGKTTLTA-------AITKVLAKKGGAEAK-------AYDQI-DKAPEEKARGITINT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  76 ALWKFETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK00049   66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 156 DSTEppySESRFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEQSTKMPWFKgwQIERkegkaegkcLIEALDAI 235
Cdd:PRK00049  139 DMVD---DEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEK--KILE---------LMDAVDSY 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 236 LP-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---IVVFAPANITTeVKSVEMHHEALQEAVPGDNVGFN 311
Cdd:PRK00049  202 IPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEeveIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVGAL 280
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1814598424 312 VKNVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVL 347
Cdd:PRK00049  281 LRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
PLN03126 PLN03126
Elongation factor Tu; Provisional
3-441 6.85e-53

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 184.82  E-value: 6.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   3 KEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKeaqemgkgsfkyawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03126   77 RKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDE---------------IDAAPEERARGITINTATVEYET 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  83 AKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppy 162
Cdd:PLN03126  142 ENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD--- 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 163 SESRFEEIKKEVSSYIKKIGYNPAAvafVPISGWHGDNMLEQSTKMPwfkgwQIERKEGKAEGKC--LIEALDAILP-PA 239
Cdd:PLN03126  212 DEELLELVELEVRELLSSYEFPGDD---IPIISGSALLALEALMENP-----NIKRGDNKWVDKIyeLMDAVDSYIPiPQ 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 240 RPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIV--VFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSV 317
Cdd:PLN03126  284 RQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdiVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQK 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 318 KELRRGYVAgdSKNNPPKGAADFTAQVIVLNHP--GQIS---NGYTPVLDCHTAHIACKFAEIKEKVDrrsgksteENPK 392
Cdd:PLN03126  364 ADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDKD--------EESK 433
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1814598424 393 SIKSGDAA--IVNLVpsKPLCVEAFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:PLN03126  434 MVMPGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
PLN03127 PLN03127
Elongation factor Tu; Provisional
3-441 2.99e-52

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 182.33  E-value: 2.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   3 KEKIHINIVVIGHVDSGKSTTTGhliykcggidkrTIEKFEKEAQEMGKGSFKYawvLDKLKAERERGITIDIALWKFET 82
Cdd:PLN03127   57 RTKPHVNVGTIGHVDHGKTTLTA------------AITKVLAEEGKAKAVAFDE---IDKAPEEKARGITIATAHVEYET 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  83 AKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEPPY 162
Cdd:PLN03127  122 AKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAPDGPMP-------QTKEHILLARQVGVPSLVVFLNKVDVVDDEE 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 163 SESRFEEIKKEVSSYIKkigynpaavafvpisgWHGDNmleqstkMPWFKGWQIERKEGKAE--GKC----LIEALDAIL 236
Cdd:PLN03127  195 LLELVEMELRELLSFYK----------------FPGDE-------IPIIRGSALSALQGTNDeiGKNailkLMDAVDEYI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 237 P-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAP-ANITTEVKSVEMHHEALQEAVPGDNVGFN 311
Cdd:PLN03127  252 PePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQGQAGDNVGLL 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 312 VKNVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVLN------HPGQISNgYTPVLDCHTAHIackfaeikekvdrrSGK 385
Cdd:PLN03127  332 LRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADV--------------TGK 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1814598424 386 ST-EENPKSIKSGDAAIVNLVPSKPLCVEAFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:PLN03127  395 VElPEGVKMVMPGDNVTAVFELISPVPLEPGQ------RFALREGGRTVGAGVVSKV 445
PRK12735 PRK12735
elongation factor Tu; Reviewed
1-347 2.60e-51

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 178.49  E-value: 2.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:PRK12735    1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------KVLAKKGGGEAKAYDQIDNAPEEKARGITINT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  76 ALWKFETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK12735   66 SHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 156 DSTEPPyseSRFEEIKKEVSSYIKKIGYNpaavafvpisgwhGDNmleqstkMPWFKGWQIERKEGKAEGKC------LI 229
Cdd:PRK12735  139 DMVDDE---ELLELVEMEVRELLSKYDFP-------------GDD-------TPIIRGSALKALEGDDDEEWeakileLM 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 230 EALDAILP-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPANITTeVKSVEMHHEALQEAVPG 305
Cdd:PRK12735  196 DAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAG 274
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1814598424 306 DNVGFNVKNVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVL 347
Cdd:PRK12735  275 DNVGVLLRGTKREDVERGQVL--AKPGSIKPHTKFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
1-441 3.35e-51

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 178.21  E-value: 3.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKE-----KIHINIVVIGHVDSGKSTTTGhliykcgGIDKRTIEKFEKEAQemgkgsfKYAWVlDKLKAERERGITIDI 75
Cdd:PRK12736    1 MAKEkfdrsKPHVNIGTIGHVDHGKTTLTA-------AITKVLAERGLNQAK-------DYDSI-DAAPEEKERGITINT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  76 ALWKFETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:PRK12736   66 AHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLARQVGVPYLVVFLNKV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 156 DSTEPPYSESRFE-EIKKEVSSYikkigynpaavafvpisGWHGDNmleqstkMPWFKGWQIERKEGKAEG----KCLIE 230
Cdd:PRK12736  139 DLVDDEELLELVEmEVRELLSEY-----------------DFPGDD-------IPVIRGSALKALEGDPKWedaiMELMD 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 231 ALDAILP-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGT---IVVFAPANITTeVKSVEMHHEALQEAVPGD 306
Cdd:PRK12736  195 AVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDeveIVGIKETQKTV-VTGVEMFRKLLDEGQAGD 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 307 NVGFNVKNVSVKELRRGYVAGDSKNNPPkgAADFTAQVIVLN------HPGQISNgYTPVLDCHTAHI--ACKFAEIKEK 378
Cdd:PRK12736  274 NVGVLLRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYILTkeeggrHTPFFNN-YRPQFYFRTTDVtgSIELPEGTEM 350
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814598424 379 VdrRSGKSTEenpksiksgdaAIVNLVpsKPLCVEafqefpPLGRFAVRDMRQTVAVGVIKSV 441
Cdd:PRK12736  351 V--MPGDNVT-----------ITVELI--HPIAME------QGLKFAIREGGRTVGAGTVTEI 392
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
1-442 2.18e-50

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: 176.12  E-value: 2.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKI-----HINIVVIGHVDSGKSTTTGHLIykcggidkrtiekfeKEAQEMGKGSFKYAWVLDKLKAERERGITIDI 75
Cdd:TIGR00485   1 MAKEKFertkpHVNVGTIGHVDHGKTTLTAAIT---------------TVLAKEGGAAARAYDQIDNAPEEKARGITINT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  76 ALWKFETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKM 155
Cdd:TIGR00485  66 AHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKC 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 156 D-STEPPYSESRFEEIKKEVSSYikkigynpaavafvpisGWHGDNmleqstkMPWFKGWQIERKEGKAEGKC----LIE 230
Cdd:TIGR00485 139 DmVDDEELLELVEMEVRELLSQY-----------------DFPGDD-------TPIIRGSALKALEGDAEWEAkileLMD 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 231 ALDAILP-PARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPANITTeVKSVEMHHEALQEAVPGD 306
Cdd:TIGR00485 195 AVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGD 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 307 NVGFNVKNVSVKELRRGYVAgdSKNNPPKGAADFTAQVIVLN------HPGQISnGYTPVLDCHTAHIackfaeikekvd 380
Cdd:TIGR00485 274 NVGLLLRGIKREEIERGMVL--AKPGSIKPHTKFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDV------------ 338
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814598424 381 rrSGKSTE-ENPKSIKSGDAAIVNLVPSKPLCVEAFQefpplgRFAVRDMRQTVAVGVIKSVT 442
Cdd:TIGR00485 339 --TGTIELpEGVEMVMPGDNVKMTVELISPIALEQGM------RFAIREGGRTVGAGVVSKIL 393
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
8-438 8.86e-43

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: 159.69  E-value: 8.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTttghLIYKCGGIDkrTiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETAKF 85
Cdd:COG3276     1 MIIGTAGHIDHGKTT----LVKALTGID--T----------------------DRLKEEKKRGITIDLgfAYLPLPDGRR 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  86 yVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREH-ALLAFtLGVKQLIVGVNKMDSTEPpyse 164
Cdd:COG3276    53 -LGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAA-----DEGVMP--QTREHlAILDL-LGIKRGIVVLTKADLVDE---- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 165 SRFEEIKKEVSSYIKKIGYNPAAVafVPISGWHGdnmleqstkmpwfkgwqierkEGKAEgkcLIEALDAIL--PPARPT 242
Cdd:COG3276   120 EWLELVEEEIRELLAGTFLEDAPI--VPVSAVTG---------------------EGIDE---LRAALDALAaaVPARDA 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 243 DKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRR 322
Cdd:COG3276   174 DGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIER 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 323 GYVAgdSKNNPPKGAADFTAQVIVLNHPGQ-ISNGyTPVLdCH--TAHIACKFAEIkekvdrrsgksteeNPKSIKSGDA 399
Cdd:COG3276   254 GDVL--AAPGALRPTDRIDVRLRLLPSAPRpLKHW-QRVH-LHhgTAEVLARVVLL--------------DREELAPGEE 315
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1814598424 400 AIVNLVPSKPLCVEAFQefpplgRFAVRDM--RQTVAVGVI 438
Cdd:COG3276   316 ALAQLRLEEPLVAARGD------RFILRDYspRRTIGGGRV 350
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
333-441 2.21e-35

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


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 127.00  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 333 PPKGAADFTAQVIVLNH-----PGQISNGYTPVLDCHTAHIACKFAEIKEKVDrrsGKSTEENPKSIKSGDAAIVNLVPS 407
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD---PGGVSENPEFVMPGDNVIVTVELI 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1814598424 408 KPLCVEAFQefpplgRFAVRDMRQTVAVGVIKSV 441
Cdd:pfam03143  78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
6-238 1.14e-33

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 125.39  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   6 IHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETAKF 85
Cdd:cd01884     1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEI---------------DKAPEEKARGITINTAHVEYETANR 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppySES 165
Cdd:cd01884    66 HYAHVDCPGHADYIKNMITGAAQMDGAILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKADMVD---DEE 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814598424 166 RFEEIKKEVSSYIKKIGYNPAAVAFVPISGWhgdNMLEQSTKMPWFKgwQIERkegkaegkcLIEALDAILPP 238
Cdd:cd01884   136 LLELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALEGDDPNKWVD--KILE---------LLDALDSYIPT 194
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
8-326 2.77e-32

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: 129.61  E-value: 2.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIALWKFETAKFYV 87
Cdd:TIGR00475   1 MIIATAGHVDHGKTT----LLKALTGIAA------------------------DRLPEEKKRGMTIDLGFAYFPLPDYRL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVGVNKMDSTEppysESRF 167
Cdd:TIGR00475  53 GFIDVPGHEKFISNAIAGGGGIDAALLVVDADEGVMT-------QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEI 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 168 EEIKKEVSSYIKKIGYNPAAVAFVpISGWHGDNMleqstkmpwfkgwqierKEGKAEGKCLIEALDailppARPTDKALR 247
Cdd:TIGR00475 122 KRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGI-----------------GELKKELKNLLESLD-----IKRIQKPLR 178
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814598424 248 LPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYVA 326
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLI 257
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
340-438 1.34e-29

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: 111.33  E-value: 1.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 340 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKstEENPKSIKSGDAAIVNLVPSKPLCVEAFQEFP 419
Cdd:cd01513     6 FDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLERGKEFP 83
                          90
                  ....*....|....*....
gi 1814598424 420 PLGRFAVRDMRQTVAVGVI 438
Cdd:cd01513    84 TLGRFALRDGGRTVGAGLI 102
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
10-191 1.16e-24

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: 99.99  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETAKfYV 87
Cdd:cd04171     2 IGTAGHIDHGKTT----LIKALTGIET------------------------DRLPEEKKRGITIDLgfAYLDLPDGK-RL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefEAGISKngQTREHALLAFTLGVKQLIVGVNKMDSTEppysESRF 167
Cdd:cd04171    53 GFIDVPGHEKFVKNMLAGAGGIDAVLLVVAA-----DEGIMP--QTREHLEILELLGIKKGLVVLTKADLVD----EDRL 121
                         170       180
                  ....*....|....*....|....
gi 1814598424 168 EEIKKEVSSYIKKIGYNPAAVAFV 191
Cdd:cd04171   122 ELVEEEILELLAGTFLADAPIFPV 145
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
340-438 6.57e-23

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: 93.00  E-value: 6.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 340 FTAQVIVLNHPGQI-SNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAAIVNLVPSKPLCVEAFQEF 418
Cdd:cd03704     6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85
                          90       100
                  ....*....|....*....|
gi 1814598424 419 PPLGRFAVRDMRQTVAVGVI 438
Cdd:cd03704    86 PQLGRFTLRDEGKTIAIGKV 105
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
246-325 6.77e-19

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 80.77  E-value: 6.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNvsVKELRRGYV 325
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
333-441 7.14e-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: 81.82  E-value: 7.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 333 PPKGAADFTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDRRSGKSTEENPKSIKSGDAAIVNLVPSKPLCV 412
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80
                          90       100
                  ....*....|....*....|....*....
gi 1814598424 413 EAFQEFPPLGRFAVRDMRQTVAVGVIKSV 441
Cdd:cd04093    81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
9-178 2.44e-18

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: 82.58  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFETAK 84
Cdd:cd01890     2 NFSIIAHIDHGKSTLADRLLELTGTVSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLfYKAKDGE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  85 FYV-TIIDAPGHRDFikNMITGTSQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD--STE 159
Cdd:cd01890    66 EYLlNLIDTPGHVDF--SYEVSRSLAACegALLVVDATQG-VEA------QTLANFYLALENNLEIIPV-INKIDlpAAD 135
                         170
                  ....*....|....*....
gi 1814598424 160 PpysesrfEEIKKEVSSYI 178
Cdd:cd01890   136 P-------DRVKQEIEDVL 147
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
246-325 3.13e-17

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: 76.41  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
7-316 2.16e-16

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 81.60  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   7 HI-NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfEKEAQemgkgsfkyawVLDKLKAERERGITID---IAL-WKFE 81
Cdd:COG0481     5 NIrNFSIIAHIDHGKSTLADRLLELTGTLSER-----EMKEQ-----------VLDSMDLERERGITIKaqaVRLnYKAK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  82 TAKFYV-TIIDAPGHRDFiknmitgT-----SQADC--AVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVN 153
Cdd:COG0481    69 DGETYQlNLIDTPGHVDF-------SyevsrSLAACegALLVVDASQG-VEA------QTLANVYLALENDLEIIPV-IN 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 154 KMD--STEPpysesrfEEIKKEVssyIKKIGYNPAAVafVPISGwhgdnmleqstkmpwfkgwqierKEGkaEGkclIEA 231
Cdd:COG0481   134 KIDlpSADP-------ERVKQEI---EDIIGIDASDA--ILVSA-----------------------KTG--IG---IEE 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 232 -LDAI---LPPARPTDKAlrlPLQ--------DVYKiggiGTVPVGRVETGVLKPGTIVVFAPANITTEVKSV---EMHH 296
Cdd:COG0481   174 iLEAIverIPPPKGDPDA---PLQalifdswyDSYR----GVVVYVRVFDGTLKKGDKIKMMSTGKEYEVDEVgvfTPKM 246
                         330       340
                  ....*....|....*....|...
gi 1814598424 297 EALQEAVPGDnVGF---NVKNVS 316
Cdd:COG0481   247 TPVDELSAGE-VGYiiaGIKDVR 268
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
10-323 1.39e-15

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 78.94  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  10 IVVIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDI--ALWKFETAKFyV 87
Cdd:PRK10512    3 IATAGHVDHGKTT----LLQAITGVNA------------------------DRLPEEKKRGMTIDLgyAYWPQPDGRV-L 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFeagisknGQTREH-ALLAFTlGVKQLIVGVNKMDSTEPPysesR 166
Cdd:PRK10512   54 GFIDVPGHEKFLSNMLAGVGGIDHALLVVACDDGVM-------AQTREHlAILQLT-GNPMLTVALTKADRVDEA----R 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 167 FEEIKKEVSSYIKKIgynpaavafvpisGWHGDNMLEQSTkmpwfkgwqierKEGKAegkclIEALDAIL----PPARPT 242
Cdd:PRK10512  122 IAEVRRQVKAVLREY-------------GFAEAKLFVTAA------------TEGRG-----IDALREHLlqlpEREHAA 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 243 DKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVK-NVSVKELR 321
Cdd:PRK10512  172 QHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAgDAEKEQIN 251

                  ..
gi 1814598424 322 RG 323
Cdd:PRK10512  252 RG 253
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
9-178 1.90e-15

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: 75.74  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfekeaqemgkGSfkyawV------LDKLKAERERGITIDIALWKFET 82
Cdd:cd04168     1 NIGILAHVDAGKTTLTESLLYTSGAIREL--------------GS-----VdkgttrTDSMELERQRGITIFSAVASFQW 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  83 AKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehaLLAFTLgvKQL----IVGVNKMDsT 158
Cdd:cd04168    62 EDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVISAVEG-------VQAQTR---ILFRLL--RKLniptIIFVNKID-R 128
                         170       180
                  ....*....|....*....|
gi 1814598424 159 EPPYSESRFEEIKKEVSSYI 178
Cdd:cd04168   129 AGADLEKVYQEIKEKLSPDI 148
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
248-325 2.10e-15

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: 71.01  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 248 LPLQDVYKIGGIGTVPVGRVETGVLKPG---TIVVFAPaNITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGdevEIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81

                  .
gi 1814598424 325 V 325
Cdd:cd03697    82 V 82
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
8-309 9.68e-15

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 75.66  E-value: 9.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTttghLIYKCGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:PRK04000   10 VNIGMVGHVDHGKTT----LVQALTGV-----------------------WT-DRHSEELKRGITIrlgyaDATIRKCPD 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  83 AKFY---------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAgiskngQTREHaLLAF 141
Cdd:PRK04000   62 CEEPeayttepkcpncgsetellrrVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCPQP------QTKEH-LMAL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 142 T-LGVKQLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIkkigynpAAVA-FVPISGWHGDNMleqstkmpwfkgwqierk 219
Cdd:PRK04000  135 DiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-------AENApIIPVSALHKVNI------------------ 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 220 egkaegKCLIEALDAILP-PARPTDKALRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VLKPGTIVVFAP 282
Cdd:PRK04000  190 ------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEIRPGIKVEEGG 263
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1814598424 283 AN----ITTEVKSVEMHHEALQEAVPGDNVG 309
Cdd:PRK04000  264 KTkwepITTKIVSLRAGGEKVEEARPGGLVG 294
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
260-325 1.21e-14

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


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 68.45  E-value: 1.21e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814598424 260 GTVPVGRVETGVLKPGTIVVFAPA-----NITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNgtgkkKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
8-194 2.06e-13

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: 68.55  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTttghliykcggIDKRTIEKFEKEAqemgkgsfkyawvLDKLKAERERGITIDIALWKF------- 80
Cdd:cd01889     1 VNVGLLGHVDSGKTS-----------LAKALSEIASTAA-------------FDKNPQSQERGITLDLGFSSFevdkpkh 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 -------ETAKFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGvKQLIVGVN 153
Cdd:cd01889    57 lednenpQIENYQITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKG-------IQTQTAECLVIGELLC-KPLIVVLN 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1814598424 154 KMDSTEPPYSESRFEEIKKEVSSYIKKIgyNPAAVAFVPIS 194
Cdd:cd01889   129 KIDLIPEEERKRKIEKMKKRLQKTLEKT--RLKDSPIIPVS 167
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
246-328 2.62e-13

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: 65.23  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd16267     2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGSI 81

                  ...
gi 1814598424 326 AGD 328
Cdd:cd16267    82 LCD 84
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
8-201 4.34e-13

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


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 67.68  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTTTGHLiykcGGIdkrtiekfekeaqemgkgsfkyaWVlDKLKAERERGITI-----DIALWKFET 82
Cdd:cd01888     1 INIGTIGHVAHGKTTLVKAL----SGV-----------------------WT-VRHKEELKRNITIklgyaNAKIYKCPN 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  83 AKFY----------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgefeagiskN-----GQTRE 135
Cdd:cd01888    53 CGCPrpydtpececpgcggetklvrhVSFVDCPGHEILMATMLSGAAVMDGALLLIAA-----------NepcpqPQTSE 121
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814598424 136 HALLAFTLGVKQLIVGVNKMDSTEPPYSESRFEEIKKevssYIKKIGYNPAAVafVPISGWHGDNM 201
Cdd:cd01888   122 HLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE----FVKGTIAENAPI--IPISAQLKYNI 181
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
9-174 9.18e-13

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: 66.85  E-value: 9.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGidkrtiekfEKEAQEMGKGsfkyawVLDKLKAERERGITIdiaLWKfETAKFY-- 86
Cdd:cd01891     4 NIAIIAHVDHGKTTLVDALLKQSGT---------FRENEEVGER------VMDSNDLERERGITI---LAK-NTAITYkd 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  87 --VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAGTGEFEagiskngQTR---EHALLAftlGVKqLIVGVNKM 155
Cdd:cd01891    65 tkINIIDTPGHADFggeverVLSM------VDGVLLLVDASEGPMP-------QTRfvlKKALEA---GLK-PIVVINKI 127
                         170
                  ....*....|....*....
gi 1814598424 156 DSteppySESRFEEIKKEV 174
Cdd:cd01891   128 DR-----PDARPEEVVDEV 141
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
9-156 9.58e-13

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: 67.26  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekFEKEAqemgkGSFKYawvLDKLKAERERGITID---IALwKFETAK- 84
Cdd:cd01885     2 NICIIAHVDHGKTTLSDSLLASAGII-------SEKLA-----GKARY---LDTREDEQERGITIKssaISL-YFEYEEe 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  85 ------FYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAgtgeFEaGISKngQTreHALL--AFTLGVKQLIVgVNKMD 156
Cdd:cd01885    66 kmdgndYLINLIDSPGHVDFSSEVTAALRLTDGALVVVDA----VE-GVCV--QT--ETVLrqALEERVKPVLV-INKID 135
PRK13351 PRK13351
elongation factor G-like protein;
9-156 4.87e-12

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 68.05  E-value: 4.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKFEKEAqemgkgsfkyawvlDKLKAERERGITIDIAL----WKfeta 83
Cdd:PRK13351   10 NIGILAHIDAGKTTLTERILFYTGKIHKMgEVEDGTTVT--------------DWMPQEQERGITIESAAtscdWD---- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814598424  84 KFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGeFEAgiskngQTREHALLAFTLGVKQLIVgVNKMD 156
Cdd:PRK13351   72 NHRINLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTG-VQP------QTETVWRQADRYGIPRLIF-INKMD 136
PRK10218 PRK10218
translational GTPase TypA;
9-274 7.65e-12

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 67.43  E-value: 7.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekEAQEMgkgsfkyawVLDKLKAERERGITIDIALWKFETAKFYVT 88
Cdd:PRK10218    7 NIAIIAHVDHGKTTLVDKLLQQSGTFDSRA------ETQER---------VMDSNDLEKERGITILAKNTAIKWNDYRIN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  89 IIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEagiskngQTREHALLAFTLGVKQLIVgVNKMD--STEPPYSESR 166
Cdd:PRK10218   72 IVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMP-------QTRFVTKKAFAYGLKPIVV-INKVDrpGARPDWVVDQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 167 FEEIKKEVSSYIKKIGYnPA--AVAFVPISGWHGDNMLEQSTkmPWFKGwqierkegkaegkclieALDAILPPARPTDK 244
Cdd:PRK10218  144 VFDLFVNLDATDEQLDF-PIvyASALNGIAGLDHEDMAEDMT--PLYQA-----------------IVDHVPAPDVDLDG 203
                         250       260       270
                  ....*....|....*....|....*....|
gi 1814598424 245 ALRLPLQDVYKIGGIGTVPVGRVETGVLKP 274
Cdd:PRK10218  204 PFQMQISQLDYNSYVGVIGIGRIKRGKVKP 233
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
9-121 8.89e-12

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


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 67.38  E-value: 8.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKrtiekfekeaqeMGK---GSFkyawVLDKLKAERERGITIDIALWKFETAKF 85
Cdd:COG0480    11 NIGIVAHIDAGKTTLTERILFYTGAIHR------------IGEvhdGNT----VMDWMPEEQERGITITSAATTCEWKGH 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1814598424  86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTG 121
Cdd:COG0480    75 KINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAG 110
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
9-156 1.94e-11

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: 64.15  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKR-TIEKfekeaqemgkGSFkyawVLDKLKAERERGITIDIALWKFETAKFYV 87
Cdd:cd04170     1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVED----------GNT----VSDYDPEEKKRKMSIETSVAPLEWNGHKI 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814598424  88 TIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREHALLAFTLGVKQLIVgVNKMD 156
Cdd:cd04170    67 NLIDTPGYADFVGETLSALRAVDAALIVVEAQSG-------VEVGTEKVWEFLDDAKLPRIIF-INKMD 127
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
13-156 3.62e-11

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 65.15  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  13 IGHVDSGKSTTTGHLIYKCGGIDKR-TIEkfEKEAqemgkgsfkyawVLDKLKAERERGITIDIALWKFETAKFYVTIID 91
Cdd:PRK12740    1 VGHSGAGKTTLTEAILFYTGAIHRIgEVE--DGTT------------TMDFMPEERERGISITSAATTCEWKGHKINLID 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814598424  92 APGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTRehALLAFT--LGVKQLIVgVNKMD 156
Cdd:PRK12740   67 TPGHVDFTGEVERALRVLDGAVVVVCAVGG-------VEPQTE--TVWRQAekYGVPRIIF-VNKMD 123
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
9-98 7.29e-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: 62.51  E-value: 7.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiEKFEKEAqemgkgsfkyawVLDKLKAERERGITIDIA----LWKfetaK 84
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERILYYTGRIHKIG-EVHGGGA------------TMDWMEQERERGITIQSAattcFWK----D 63
                          90
                  ....*....|....
gi 1814598424  85 FYVTIIDAPGHRDF 98
Cdd:cd01886    64 HRINIIDTPGHVDF 77
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
9-211 2.13e-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: 60.36  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKcggIDKRTIEKFEKEAQEmgkgsfKYawvLDKLKAERERGITI-----DIALWKFETA 83
Cdd:cd04167     2 NVCIAGHLHHGKTSLLDMLIEQ---THKRTPSVKLGWKPL------RY---TDTRKDEQERGISIksnpiSLVLEDSKGK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  84 KFYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTgefeaGISKNGQT--REhallAFTLGVKQLIVgVNKMDS--TE 159
Cdd:cd04167    70 SYLINIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVE-----GLTSVTERliRH----AIQEGLPMVLV-INKIDRliLE 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1814598424 160 ---PPYSESR-FEEIKKEVSSYIKKIGyNPAAVAFVPISGwhgdNMLEQSTKMPWF 211
Cdd:cd04167   140 lklPPTDAYYkLRHTIDEINNYIASFS-TTEGFLVSPELG----NVLFASSKFGFC 190
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
1-306 2.46e-10

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 62.73  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIhINIVVIGHVDSGKSTTTGHLIYKCGGIDKRtiekfeKEAQEMgkgsfkyawVLDKLKAERERGITIdiaLWKf 80
Cdd:COG1217     1 MMREDI-RNIAIIAHVDHGKTTLVDALLKQSGTFREN------QEVAER---------VMDSNDLERERGITI---LAK- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  81 ETAKFY----VTIIDAPGHRDF------IKNMitgtsqADCAVLIVAAgtgeFEagisknG---QTR---EHALlafTLG 144
Cdd:COG1217    61 NTAVRYkgvkINIVDTPGHADFggeverVLSM------VDGVLLLVDA----FE------GpmpQTRfvlKKAL---ELG 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 145 VKqLIVGVNKMDSteppySESRFEEIKKEVSSYIKKIGYNPAAVAFvPI------SGWHGDNMLEQSTKMpwfkgwqier 218
Cdd:COG1217   122 LK-PIVVINKIDR-----PDARPDEVVDEVFDLFIELGATDEQLDF-PVvyasarNGWASLDLDDPGEDL---------- 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 219 kegkaegKCLIEA-LDAILPPARPTDKalrlPLQ--------DVYkIGGIGtvpVGRVETGVLKPG-TIVVFAPANITTE 288
Cdd:COG1217   185 -------TPLFDTiLEHVPAPEVDPDG----PLQmlvtnldySDY-VGRIA---IGRIFRGTIKKGqQVALIKRDGKVEK 249
                         330       340
                  ....*....|....*....|....
gi 1814598424 289 VKSVEMH-HEALQ-----EAVPGD 306
Cdd:COG1217   250 GKITKLFgFEGLErveveEAEAGD 273
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
246-325 3.52e-10

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: 56.34  E-value: 3.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 246 LRLPLQDVYKigGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd04089     2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFV 79
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
252-325 3.98e-10

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


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 56.07  E-value: 3.98e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814598424 252 DVYKIGGIGTVPVGRVETGVLKPGTIVVFAPAN----ITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYV 325
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
9-182 7.50e-10

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


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 58.84  E-value: 7.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLiyKCGGIDKrtiekfekeaqemGKGSFKYAwvLDKLKAERERGIT---------------- 72
Cdd:cd04165     1 RVAVVGNVDAGKSTLLGVL--TQGELDN-------------GRGKARLN--LFRHKHEVESGRTssvsndilgfdsdgev 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  73 ----IDIALWK----FETAKFYVTIIDAPGHRDFIKNMITGTS--QADCAVLIVAAGTGEfeagiskNGQTREHALLAFT 142
Cdd:cd04165    64 vnypDNHLGELdveiCEKSSKVVTFIDLAGHERYLKTTVFGMTgyAPDYAMLVVGANAGI-------IGMTKEHLGLALA 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1814598424 143 LGVKQLIVgVNKMDSTeppySESRFEEIKKEVSSYIKKIG 182
Cdd:cd04165   137 LKVPVFVV-VTKIDMT----PANVLQETLKDLKRLLKSPG 171
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
246-328 1.05e-09

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: 54.81  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 246 LRLPLQDVYKiGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMH-HEALQEAVPGDNVGFNVKNVSVKELRRGY 324
Cdd:cd03698     2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPGD 80

                  ....
gi 1814598424 325 VAGD 328
Cdd:cd03698    81 ILSS 84
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
12-121 1.16e-09

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: 58.76  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  12 VIGHVDSGKSTTTGHLIYKCGGIdkrtiekfeKEAQEM-GKGSFKYAwVLDKLKAERERGITIDIALWKFETAKFYVTII 90
Cdd:cd04169     7 IISHPDAGKTTLTEKLLLFGGAI---------QEAGAVkARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLL 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1814598424  91 DAPGHRDFIKNMITGTSQADCAVLIVAAGTG 121
Cdd:cd04169    77 DTPGHEDFSEDTYRTLTAVDSAVMVIDAAKG 107
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
10-201 5.73e-09

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


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 55.17  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  10 IVVIGHVDSGKSTttghliykcggidkrtiekfekeaqemgkgsfkyawVLDKLK----AERE-RGITIDIALWKFETAK 84
Cdd:cd01887     3 VTVMGHVDHGKTT------------------------------------LLDKIRktnvAAGEaGGITQHIGAYQVPIDV 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  85 FY--VTIIDAPGHRDFiKNMIT-GTSQADCAVLIVAAGTGeFEAgiskngQTRE---HALLAFTlgvkQLIVGVNKMDst 158
Cdd:cd01887    47 KIpgITFIDTPGHEAF-TNMRArGASVTDIAILVVAADDG-VMP------QTIEainHAKAANV----PIIVAINKID-- 112
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1814598424 159 EPPYSESRFEEIKKEVSSY---IKKIGYNpaaVAFVPISGWHGDNM 201
Cdd:cd01887   113 KPYGTEADPERVKNELSELglvGEEWGGD---VSIVPISAKTGEGI 155
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
246-310 7.68e-09

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: 52.57  E-value: 7.68e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 246 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGF 310
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
8-305 2.48e-08

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 56.17  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTttghLIYKCGGIdkRTIekfekeaqemgkgsfkyawvldKLKAERERGITIDIAlwkFETAKFY- 86
Cdd:PTZ00327   35 INIGTIGHVAHGKST----VVKALSGV--KTV----------------------RFKREKVRNITIKLG---YANAKIYk 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  87 -----------------------------------VTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagiSKNG 131
Cdd:PTZ00327   84 cpkcprptcyqsygsskpdnppcpgcghkmtlkrhVSFVDCPGHDILMATMLNGAAVMDAALLLIAANES------CPQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 132 QTREHALLAFTLGVKQLIVGVNKMDSTEPPYSESRFEEIKKEVSSYIKKigynpaAVAFVPISGWHGDNM---LEQ-STK 207
Cdd:PTZ00327  158 QTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTIAD------NAPIIPISAQLKYNIdvvLEYiCTQ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 208 MPwfkgwqierkegkaegkclIEALDAILPP----ARPTDkaLRLPLQDVYKIggIGTVPVGRVETGVLK--------PG 275
Cdd:PTZ00327  232 IP-------------------IPKRDLTSPPrmivIRSFD--VNKPGEDIENL--KGGVAGGSILQGVLKvgdeieirPG 288
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1814598424 276 TIVVFAPANIT-----TEVKSVEMHHEALQEAVPG 305
Cdd:PTZ00327  289 IISKDSGGEFTcrpirTRIVSLFAENNELQYAVPG 323
PTZ00416 PTZ00416
elongation factor 2; Provisional
1-98 7.74e-08

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 55.05  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   1 MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDkrtiekfEKEAqemGKGSFkyawvLDKLKAERERGITID---IAL 77
Cdd:PTZ00416   13 MDNPDQIRNMSVIAHVDHGKSTLTDSLVCKAGIIS-------SKNA---GDARF-----TDTRADEQERGITIKstgISL 77
                          90       100
                  ....*....|....*....|....*...
gi 1814598424  78 ---WKFETAK----FYVTIIDAPGHRDF 98
Cdd:PTZ00416   78 yyeHDLEDGDdkqpFLINLIDSPGHVDF 105
PRK07560 PRK07560
elongation factor EF-2; Reviewed
9-98 3.93e-07

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 52.56  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIDKRTiekfekeaqeMGKgsfkyAWVLDKLKAERERGITIDIA----LWKFETAK 84
Cdd:PRK07560   22 NIGIIAHIDHGKTTLSDNLLAGAGMISEEL----------AGE-----QLALDFDEEEQARGITIKAAnvsmVHEYEGKE 86
                          90
                  ....*....|....
gi 1814598424  85 FYVTIIDAPGHRDF 98
Cdd:PRK07560   87 YLINLIDTPGHVDF 100
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
9-98 2.16e-06

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 50.11  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   9 NIVVIGHVDSGKSTTTGHLIYKCGGIdkrtiekfekeAQEMGKGsfkyAWVLDKLKAERERGITID---IALW------- 78
Cdd:PLN00116   21 NMSVIAHVDHGKSTLTDSLVAAAGII-----------AQEVAGD----VRMTDTRADEAERGITIKstgISLYyemtdes 85
                          90       100
                  ....*....|....*....|....*.
gi 1814598424  79 ------KFETAKFYVTIIDAPGHRDF 98
Cdd:PLN00116   86 lkdfkgERDGNEYLINLIDSPGHVDF 111
infB CHL00189
translation initiation factor 2; Provisional
10-201 6.40e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 45.59  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  10 IVVIGHVDSGKSTTtghliykcggIDKrtIEKFEKEAQEMGkgsfkyawvldklkaererGITIDIA----LWKFETAKF 85
Cdd:CHL00189  247 VTILGHVDHGKTTL----------LDK--IRKTQIAQKEAG-------------------GITQKIGayevEFEYKDENQ 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  86 YVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGefeagisKNGQTREhALLAFTLGVKQLIVGVNKMDSTeppysES 165
Cdd:CHL00189  296 KIVFLDTPGHEAFSSMRSRGANVTDIAILIIAADDG-------VKPQTIE-AINYIQAANVPIIVAINKIDKA-----NA 362
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1814598424 166 RFEEIKKEVSSY---IKKIGynpAAVAFVPISGWHGDNM 201
Cdd:CHL00189  363 NTERIKQQLAKYnliPEKWG---GDTPMIPISASQGTNI 398
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
8-203 8.80e-05

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 42.74  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424   8 INIVVIGHVDSGKSTTTGHLIYKcggidkrtiEKFEKEAQEmgkGSFKYAWVLdklkAERERGITIDIALWkfetakfyv 87
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGN---------KGSITEYYP---GTTRNYVTT----VIEEDGKTYKFNLL--------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  88 tiiDAPGHRDFIKNMITGTSQADcAVLIVAAGTG---EFEAGISKNGQTREHALlafTLGVKQLIVGvNKMDsteppyse 164
Cdd:TIGR00231  57 ---DTAGQEDYDAIRRLYYPQVE-RSLRVFDIVIlvlDVEEILEKQTKEIIHHA---DSGVPIILVG-NKID-------- 120
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1814598424 165 SRFEEIKKEVSSYIKKIGYNPaavaFVPISGWHGDNMLE 203
Cdd:TIGR00231 121 LKDADLKTHVASEFAKLNGEP----IIPLSAETGKNIDS 155
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
11-203 2.03e-04

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 41.67  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  11 VVIGHVDSGKSTTTGHLIYKcggidkrtiekfekeaqemgkgsfkyawvlDKLKAERERGITIDIAL--WKFETAKFYVT 88
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGG------------------------------EVGEVSDVPGTTRDPDVyvKELDKGKVKLV 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424  89 IIDAPGHRDFIKNMITGT-----SQADCAVLIVAAGTGEFEAGIskngqTREHALLAFTLGVKQLIVGvNKMDSTEPPys 163
Cdd:cd00882    51 LVDTPGLDEFGGLGREELarlllRGADLILLVVDSTDRESEEDA-----KLLILRRLRKEGIPIILVG-NKIDLLEER-- 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1814598424 164 esrfEEIKKEVSSYIKKIGYNPaavaFVPISGWHGDNMLE 203
Cdd:cd00882   123 ----EVEELLRLEELAKILGVP----VFEVSAKTGEGVDE 154
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
251-309 3.21e-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: 39.20  E-value: 3.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1814598424 251 QDVYKIGGiGTVPVGRVETGVLKPGTIVVfaPANITTEVKSVEMHHEALQEAVPGDNVG 309
Cdd:cd16265     6 EKVFKILG-RQVLTGEVESGVIYVGYKVK--GDKGVALIRAIEREHRKVDFAVAGDEVA 61
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
340-381 1.10e-03

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: 37.88  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1814598424 340 FTAQVIVLNHPGQISNGYTPVLDCHTAHIACKFAEIKEKVDR 381
Cdd:cd03708     6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARIISIDKEVLR 47
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
340-438 2.81e-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: 36.83  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 340 FTAQVIVLN------HPGqISNGYTPVLDCHTAHIACKFAEIKEKvdrrsgksteenpKSIKSGDAAIVNLVPSKPLCVE 413
Cdd:cd03706     6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRIDLPEGK-------------EMVMPGEDTSVKLTLLKPMVLE 71
                          90       100
                  ....*....|....*....|....*
gi 1814598424 414 AFQefpplgRFAVRDMRQTVAVGVI 438
Cdd:cd03706    72 KGQ------RFTLREGGRTIGTGVV 90
IF2_aeIF5B_IV cd16266
Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ...
264-317 4.93e-03

Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents the domain IV of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologs IF5B. IF2, the largest initiation factor is an essential GTP binding protein. In E. coli three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.


Pssm-ID: 293911 [Multi-domain]  Cd Length: 87  Bit Score: 35.98  E-value: 4.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1814598424 264 VG-RVETGVLKPGTIVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSV 317
Cdd:cd16266    19 VGvEVLEGTLKPGVPLIVPDGKDVGRVKSIQDNGENVKEAKKGQEVAVSIEGPTV 73
CysN_NoDQ_III cd04095
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ...
339-438 9.14e-03

Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. 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: 294010 [Multi-domain]  Cd Length: 103  Bit Score: 35.87  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814598424 339 DFTAQVIVLNH-PGQISNGYtpVLDCHTAHIACKFAEIKEKVDRRSGKstEENPKSIKSGDAAIVNLVPSKPLCVEAFQE 417
Cdd:cd04095     5 QFEATLVWMDEkPLQPGRRY--LLKHGTRTVRARVTEIDYRIDVNTLE--REPADTLALNDIGRVTLRLAEPLAFDPYAE 80
                          90       100
                  ....*....|....*....|....
gi 1814598424 418 FPPLGRFAVRDmRQ---TVAVGVI 438
Cdd:cd04095    81 NRATGSFILID-RLtnaTVAAGMI 103
 
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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