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Conserved domains on  [gi|442798721|gb|AGC75078|]
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elongation factor-like protein, partial [Sphaeroforma tapetis]

Protein Classification

translation elongation factor EF1A family protein( domain architecture ID 1004106)

translation elongation factor EF1A family protein belongs to the TRAFAC class translation factor GTPase superfamily, similar to Saccharomyces cerevisiae superkiller protein 7 and Schizosaccharomyces pombe eukaryotic peptide chain release factor GTP-binding subunit

CATH:  2.40.30.10|3.30.960.10
Gene Ontology:  GO:0003924|GO:0003746|GO:0005525
PubMed:  12853641|9242920
SCOP:  4004050|4002110

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TEF1 super family cl34957
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-309 1.34e-114

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


The actual alignment was detected with superfamily member COG5256:

Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 337.68  E-value: 1.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:COG5256   35 DEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAIL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:COG5256  115 VV--------SAKDG------VMGQTREHAFLARTLGINQLIVAVNKM--DAVNYSEKRYEEVKEEVSKLLKMVGYKVD- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLeNMVTIPPRTPDLAMRMPLSGAFKIKGVGDV 240
Cdd:COG5256  178 ---KIPFIPVSAWKGDNVVKKSDNMPWYNGP------------TLLEAL-DNLKEPEKPVDKPLRIPIQDVYSISGIGTV 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442798721 241 LTGRVEQGTVKPGDECVFLPTHTpstgcTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLnAKNMPRAGDV 309
Cdd:COG5256  242 PVGRVETGVLKVGDKVVFMPAGV-----VGEVKSIEMHHEELEQAEPGDNIGFNVRGV-EKNDIKRGDV 304
 
Name Accession Description Interval E-value
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-309 1.34e-114

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: 337.68  E-value: 1.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:COG5256   35 DEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAIL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:COG5256  115 VV--------SAKDG------VMGQTREHAFLARTLGINQLIVAVNKM--DAVNYSEKRYEEVKEEVSKLLKMVGYKVD- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLeNMVTIPPRTPDLAMRMPLSGAFKIKGVGDV 240
Cdd:COG5256  178 ---KIPFIPVSAWKGDNVVKKSDNMPWYNGP------------TLLEAL-DNLKEPEKPVDKPLRIPIQDVYSISGIGTV 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442798721 241 LTGRVEQGTVKPGDECVFLPTHTpstgcTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLnAKNMPRAGDV 309
Cdd:COG5256  242 PVGRVETGVLKVGDKVVFMPAGV-----VGEVKSIEMHHEELEQAEPGDNIGFNVRGV-EKNDIKRGDV 304
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-315 1.38e-114

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 338.26  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   2 EREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLM 81
Cdd:PTZ00141  36 KRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  82 VPSD-GNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:PTZ00141 116 VASTaGEFEAGISK--------DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPE- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLENMVtiPPRTP-DLAMRMPLSGAFKIKGVGD 239
Cdd:PTZ00141 187 ---KVPFIPISGWQGDNMIEKSDNMPWYKGP------------TLLEALDTLE--PPKRPvDKPLRLPLQDVYKIGGIGT 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442798721 240 VLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPR---AGDVmilKSD 315
Cdd:PTZ00141 250 VPVGRVETGILKPGMVVTFAP-----SGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRgyvASDS---KND 320
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-213 1.85e-100

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: 294.01  E-value: 1.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:cd01883   27 DKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVPSD-GNFSAAIakgnhkagEVQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKDEVVHMLTRVGWKKD 159
Cdd:cd01883  107 VVSARkGEFEAGF--------EKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPK 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442798721 160 fvakSVPVMPISGWCGDNLITKSDKMPWWKGadvlvgkekihvDCLLDCLENMV 213
Cdd:cd01883  179 ----DVPFIPISGFTGDNLIEKSENMPWYKG------------PTLLEALDSLE 216
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-309 1.12e-90

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: 276.74  E-value: 1.12e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721    1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:TIGR00483  35 DEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   81 MVpsdgnfsaaiaKGNHKAGEVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:TIGR00483 115 VV-----------AVGDGEFEVQPQTREHAFLARTLGINQLIVAINKM--DSVNYDEEEFEAIKKEVSNLIKKVGYNPD- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  161 vakSVPVMPISGWCGDNLITKSDKMPWWKGADVLVGkekihvdclLDCLEnmvtiPPRTP-DLAMRMPLSGAFKIKGVGD 239
Cdd:TIGR00483 181 ---TVPFIPISAWNGDNVIKKSENTPWYKGKTLLEA---------LDALE-----PPEKPtDKPLRIPIQDVYSITGVGT 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  240 VLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRaGDV 309
Cdd:TIGR00483 244 VPVGRVETGVLKPGDKVVFEP-----AGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRR-GDV 307
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 25-180 3.51e-41

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: 141.51  E-value: 3.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   25 YMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfsaAIAKGnhkageVQG 104
Cdd:pfam00009  43 GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVV--------DAVEG------VMP 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442798721  105 QTRQHALLINLLGVKqLIVGVNKMDCDVAkyglERYTEIKDEVVHMLTRvgwKKDFVAKSVPVMPISGWCGDNLIT 180
Cdd:pfam00009 109 QTREHLRLARQLGVP-IIVFINKMDRVDG----AELEEVVEEVSRELLE---KYGEDGEFVPVVPGSALKGEGVQT 176
 
Name Accession Description Interval E-value
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-309 1.34e-114

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: 337.68  E-value: 1.34e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:COG5256   35 DEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQADAAIL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:COG5256  115 VV--------SAKDG------VMGQTREHAFLARTLGINQLIVAVNKM--DAVNYSEKRYEEVKEEVSKLLKMVGYKVD- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLeNMVTIPPRTPDLAMRMPLSGAFKIKGVGDV 240
Cdd:COG5256  178 ---KIPFIPVSAWKGDNVVKKSDNMPWYNGP------------TLLEAL-DNLKEPEKPVDKPLRIPIQDVYSISGIGTV 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442798721 241 LTGRVEQGTVKPGDECVFLPTHTpstgcTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLnAKNMPRAGDV 309
Cdd:COG5256  242 PVGRVETGVLKVGDKVVFMPAGV-----VGEVKSIEMHHEELEQAEPGDNIGFNVRGV-EKNDIKRGDV 304
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-315 1.38e-114

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 338.26  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   2 EREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLM 81
Cdd:PTZ00141  36 KRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  82 VPSD-GNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:PTZ00141 116 VASTaGEFEAGISK--------DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPE- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLENMVtiPPRTP-DLAMRMPLSGAFKIKGVGD 239
Cdd:PTZ00141 187 ---KVPFIPISGWQGDNMIEKSDNMPWYKGP------------TLLEALDTLE--PPKRPvDKPLRLPLQDVYKIGGIGT 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442798721 240 VLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPR---AGDVmilKSD 315
Cdd:PTZ00141 250 VPVGRVETGILKPGMVVTFAP-----SGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRgyvASDS---KND 320
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-309 5.94e-112

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 330.73  E-value: 5.94e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:PRK12317  34 DEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQADAAVL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVpsdgnfSAAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:PRK12317 114 VV------AADDAGG------VMPQTREHVFLARTLGINQLIVAINKM--DAVNYDEKRYEEVKEEVSKLLKMVGYKPD- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGadvlvgkekihvDCLLDCLeNMVTIPPRTPDLAMRMPLSGAFKIKGVGDV 240
Cdd:PRK12317 179 ---DIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEAL-DNLKPPEKPTDKPLRIPIQDVYSISGVGTV 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442798721 241 LTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLnAKNMPRAGDV 309
Cdd:PRK12317 243 PVGRVETGVLKVGDKVVFMP-----AGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGV-GKKDIKRGDV 305
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-213 1.85e-100

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: 294.01  E-value: 1.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:cd01883   27 DKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQADVAVL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVPSD-GNFSAAIakgnhkagEVQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKDEVVHMLTRVGWKKD 159
Cdd:cd01883  107 VVSARkGEFEAGF--------EKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPK 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442798721 160 fvakSVPVMPISGWCGDNLITKSDKMPWWKGadvlvgkekihvDCLLDCLENMV 213
Cdd:cd01883  179 ----DVPFIPISGFTGDNLIEKSENMPWYKG------------PTLLEALDSLE 216
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-309 1.12e-90

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: 276.74  E-value: 1.12e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721    1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:TIGR00483  35 DEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADAAVL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   81 MVpsdgnfsaaiaKGNHKAGEVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:TIGR00483 115 VV-----------AVGDGEFEVQPQTREHAFLARTLGINQLIVAINKM--DSVNYDEEEFEAIKKEVSNLIKKVGYNPD- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  161 vakSVPVMPISGWCGDNLITKSDKMPWWKGADVLVGkekihvdclLDCLEnmvtiPPRTP-DLAMRMPLSGAFKIKGVGD 239
Cdd:TIGR00483 181 ---TVPFIPISAWNGDNVIKKSENTPWYKGKTLLEA---------LDALE-----PPEKPtDKPLRIPIQDVYSITGVGT 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  240 VLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRaGDV 309
Cdd:TIGR00483 244 VPVGRVETGVLKPGDKVVFEP-----AGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRR-GDV 307
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-306 2.38e-74

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 235.37  E-value: 2.38e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   2 EREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLM 81
Cdd:PLN00043  36 KRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  82 VPS-DGNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKDEVVHMLTRVGWKKDf 160
Cdd:PLN00043 116 IDStTGGFEAGISK--------DGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPD- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vakSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLENmVTIPPRTPDLAMRMPLSGAFKIKGVGDV 240
Cdd:PLN00043 187 ---KIPFVPISGFEGDNMIERSTNLDWYKGP------------TLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTV 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442798721 241 LTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRA 306
Cdd:PLN00043 251 PVGRVETGVIKPGMVVTFGP-----TGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRG 311
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-293 2.32e-59

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: 195.69  E-value: 2.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   1 PEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALL 80
Cdd:COG2895   45 FEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAIL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  81 MVpsDgnfsAaiAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWkkdf 160
Cdd:COG2895  125 LI--D----A--RKG------VLEQTRRHSYIASLLGIRHVVVAVNKM--DLVDYSEEVFEEIVADYRAFAAKLGL---- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 161 vaKSVPVMPISGWCGDNLITKSDKMPWWKGAdvlvgkekihvdCLLDCLENmVTIPPRTPDLAMRMPlsgafkikgVGDV 240
Cdd:COG2895  185 --EDITFIPISALKGDNVVERSENMPWYDGP------------TLLEHLET-VEVAEDRNDAPFRFP---------VQYV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798721 241 L---------TGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGL 293
Cdd:COG2895  241 NrpnldfrgyAGTIASGTVRVGDEVVVLP-----SGKTSTVKSIVTFDGDLEEAFAGQSVTL 297
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 16-204 1.07e-44

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: 151.18  E-value: 1.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  16 GKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsDGNfsaaiaKG 95
Cdd:cd04166   43 QGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLV--DAR------KG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  96 nhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGwkkdfvAKSVPVMPISGWCG 175
Cdd:cd04166  115 ------VLEQTRRHSYIASLLGIRHVVVAVNKM--DLVDYDEEVFEEIKADYLAFAASLG------IEDITFIPISALEG 180

                        170       180
                 ....*....|....*....|....*....
gi 442798721 176 DNLITKSDKMPWWKGADVLVGKEKIHVDC 204
Cdd:cd04166  181 DNVVSRSENMPWYKGPTLLEHLETVEIAS 209
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 27-297 9.41e-44

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: 154.15  E-value: 9.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGnfsaaiakgnhkageVQGQ 105
Cdd:COG0050   51 DKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSaTDG---------------PMPQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 106 TRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERyteIKDEVVHMLTrvgwKKDFVAKSVPVMPISGwcgdnliTK---S 182
Cdd:COG0050  116 TREHILLARQVGVPYIVVFLNKCDMVDDEELLEL---VEMEVRELLS----KYGFPGDDTPIIRGSA-------LKaleG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 183 DKMPWWKGAdvlvgkekihVDCLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD--ECVFLp 260
Cdd:COG0050  182 DPDPEWEKK----------ILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDevEIVGI- 250

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442798721 261 THTPSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKG 297
Cdd:COG0050  251 RDTQKTVVTG----VEMFRKLLDEGEAGDNVGLLLRG 283
PLN03127 PLN03127
Elongation factor Tu; Provisional
 18-310 1.33e-41

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 149.59  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  18 GSFAFAF-YMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPS-DGNFSaaiakg 95
Cdd:PLN03127  90 KAKAVAFdEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSApDGPMP------ 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  96 nhkagevqgQTRQHALLINLLGVKQLIVGVNKMDCdVAKYGLERYTEIkdEVVHMLTRVgwkkDFVAKSVPVMPISGWCG 175
Cdd:PLN03127 164 ---------QTKEHILLARQVGVPSLVVFLNKVDV-VDDEELLELVEM--ELRELLSFY----KFPGDEIPIIRGSALSA 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 176 dnlitksdkmpwWKGADVLVGKEKIHVdcLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDE 255
Cdd:PLN03127 228 ------------LQGTNDEIGKNAILK--LMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEE 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442798721 256 CVFL---PTHTPSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRaGDVM 310
Cdd:PLN03127 294 VEIVglrPGGPLKTTVTG----VEMFKKILDQGQAGDNVGLLLRGLKREDVQR-GQVI 346
PRK12736 PRK12736
elongation factor Tu; Reviewed
 27-305 1.65e-41

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 148.17  E-value: 1.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMV-PSDGnfsaaiakgnhkageVQGQ 105
Cdd:PRK12736  51 DAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVaATDG---------------PMPQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 106 TRQHALLINLLGVKQLIVGVNKmdCDVAkyGLERYTEIKD-EVVHMLTrvgwKKDFVAKSVPVMPISGwcgdnLITKSDK 184
Cdd:PRK12736 116 TREHILLARQVGVPYLVVFLNK--VDLV--DDEELLELVEmEVRELLS----EYDFPGDDIPVIRGSA-----LKALEGD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 185 MPWWKGadvlvgkekihVDCLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPTH-T 263
Cdd:PRK12736 183 PKWEDA-----------IMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKeT 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442798721 264 PSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPR 305
Cdd:PRK12736 252 QKTVVTG----VEMFRKLLDEGQAGDNVGVLLRGVDRDEVER 289
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 25-180 3.51e-41

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: 141.51  E-value: 3.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   25 YMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfsaAIAKGnhkageVQG 104
Cdd:pfam00009  43 GLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQADGAILVV--------DAVEG------VMP 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442798721  105 QTRQHALLINLLGVKqLIVGVNKMDCDVAkyglERYTEIKDEVVHMLTRvgwKKDFVAKSVPVMPISGWCGDNLIT 180
Cdd:pfam00009 109 QTREHLRLARQLGVP-IIVFINKMDRVDG----AELEEVVEEVSRELLE---KYGEDGEFVPVVPGSALKGEGVQT 176
PRK00049 PRK00049
elongation factor Tu; Reviewed
 27-297 4.76e-40

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 144.18  E-value: 4.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPS-DGnfsaaiakgnhkageVQGQ 105
Cdd:PRK00049  51 DKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAaDG---------------PMPQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 106 TRQHALLINLLGVKQLIVGVNKMDCdVAKYGLERYTEIkdEVVHMLTrvgwKKDFVAKSVPVMPISGWCGdnlITKSDKM 185
Cdd:PRK00049 116 TREHILLARQVGVPYIVVFLNKCDM-VDDEELLELVEM--EVRELLS----KYDFPGDDTPIIRGSALKA---LEGDDDE 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 186 PWwkgadvlvgKEKIHVdcLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC--VFLpTHT 263
Cdd:PRK00049 186 EW---------EKKILE--LMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVeiVGI-RDT 253

                        250       260       270
                 ....*....|....*....|....*....|....
gi 442798721 264 PSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKG 297
Cdd:PRK00049 254 QKTTVTG----VEMFRKLLDEGQAGDNVGALLRG 283
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 26-305 1.95e-39

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: 142.61  E-value: 1.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   26 MDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGnfsaaiakgnhkageVQG 104
Cdd:TIGR00485  50 IDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSaTDG---------------PMP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  105 QTRQHALLINLLGVKQLIVGVNKmdCDVAKyGLERYTEIKDEVVHMLTrvgwKKDFVAKSVPVMPisgwcGDNLITKSDK 184
Cdd:TIGR00485 115 QTREHILLARQVGVPYIVVFLNK--CDMVD-DEELLELVEMEVRELLS----QYDFPGDDTPIIR-----GSALKALEGD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  185 MPWwkgadvlvgKEKIHVdcLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPTH-T 263
Cdd:TIGR00485 183 AEW---------EAKILE--LMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKdT 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 442798721  264 PSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPR 305
Cdd:TIGR00485 252 RKTTVTG----VEMFRKELDEGRAGDNVGLLLRGIKREEIER 289
PLN03126 PLN03126
Elongation factor Tu; Provisional
 26-312 5.97e-39

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 143.22  E-value: 5.97e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  26 MDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGNFSaaiakgnhkagevqg 104
Cdd:PLN03126 119 IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSgADGPMP--------------- 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 105 QTRQHALLINLLGVKQLIVGVNKMDcDVAKYGLERYTEIkdEVVHMLTrvgwKKDFVAKSVPVMPISGWCGDNLITKSDK 184
Cdd:PLN03126 184 QTKEHILLAKQVGVPNMVVFLNKQD-QVDDEELLELVEL--EVRELLS----SYEFPGDDIPIISGSALLALEALMENPN 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 185 MPwwKGADVLVgkEKIHVdcLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD--ECVFLpTH 262
Cdd:PLN03126 257 IK--RGDNKWV--DKIYE--LMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGEtvDIVGL-RE 329

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442798721 263 TPSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRAgdvMIL 312
Cdd:PLN03126 330 TRSTTVTG----VEMFQKILDEALAGDNVGLLLRGIQKADIQRG---MVL 372
tufA CHL00071
elongation factor Tu
 27-312 1.27e-38

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 140.86  E-value: 1.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGNFSaaiakgnhkagevqgQ 105
Cdd:CHL00071  51 DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSaADGPMP---------------Q 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 106 TRQHALLINLLGVKQLIVGVNKMD-CDVAKYgLERyteIKDEVVHMLTrvgwKKDFVAKSVPVMPISGWCGDNLITKSDK 184
Cdd:CHL00071 116 TKEHILLAKQVGVPNIVVFLNKEDqVDDEEL-LEL---VELEVRELLS----KYDFPGDDIPIVSGSALLALEALTENPK 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 185 mpWWKGADVLVgkEKIHVdcLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD--ECVFLpTH 262
Cdd:CHL00071 188 --IKRGENKWV--DKIYN--LMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDtvEIVGL-RE 260

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442798721 263 TPSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRAgdvMIL 312
Cdd:CHL00071 261 TKTTTVTG----LEMFQKTLDEGLAGDNVGILLRGIQKEDIERG---MVL 303
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 22-293 1.30e-38

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 143.92  E-value: 1.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  22 FAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSdgnfsaaiAKGnhkage 101
Cdd:PRK05506  75 LALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDA--------RKG------ 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 102 VQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGwkkdfvAKSVPVMPISGWCGDNLITK 181
Cdd:PRK05506 141 VLTQTRRHSFIASLLGIRHVVLAVNKM--DLVDYDQEVFDEIVADYRAFAAKLG------LHDVTFIPISALKGDNVVTR 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 182 SDKMPWWKGADvlvgkekihvdcLLDCLENmVTIPPRTPDLAMRMPlsgafkikgVGDV---------LTGRVEQGTVKP 252
Cdd:PRK05506 213 SARMPWYEGPS------------LLEHLET-VEIASDRNLKDFRFP---------VQYVnrpnldfrgFAGTVASGVVRP 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442798721 253 GDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGL 293
Cdd:PRK05506 271 GDEVVVLP-----SGKTSRVKRIVTPDGDLDEAFAGQAVTL 306
PRK12735 PRK12735
elongation factor Tu; Reviewed
 27-297 1.38e-38

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 140.36  E-value: 1.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfSAAiakgnhkagevQG-- 104
Cdd:PRK12735  51 DNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVV------SAA-----------DGpm 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 105 -QTRQHALLINLLGVKQLIVGVNKMDCdVAKYGLERYTEIkdEVVHMLTrvgwKKDFVAKSVPVMPISGWCGDNlitkSD 183
Cdd:PRK12735 114 pQTREHILLARQVGVPYIVVFLNKCDM-VDDEELLELVEM--EVRELLS----KYDFPGDDTPIIRGSALKALE----GD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 184 KMPWWKGAdvlvgkekihVDCLLDCLENMVTIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC--VFLpT 261
Cdd:PRK12735 183 DDEEWEAK----------ILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVeiVGI-K 251

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442798721 262 HTPSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKG 297
Cdd:PRK12735 252 ETQKTTVTG----VEMFRKLLDEGQAGDNVGVLLRG 283
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 22-293 7.60e-38

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: 138.66  E-value: 7.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721   22 FAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSdgnfsaaiAKGnhkage 101
Cdd:TIGR02034  51 LALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDA--------RKG------ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  102 VQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVvhmltrVGWKKDFVAKSVPVMPISGWCGDNLITK 181
Cdd:TIGR02034 117 VLEQTRRHSYIASLLGIRHVVLAVNKM--DLVDYDEEVFENIKKDY------LAFAEQLGFRDVTFIPLSALKGDNVVSR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  182 SDKMPWWKGAdvlvgkekihvdCLLDCLENmVTIPPRTPDLAMRMPLSGAFK----IKGvgdvLTGRVEQGTVKPGDECV 257
Cdd:TIGR02034 189 SESMPWYSGP------------TLLEILET-VEVERDAQDLPLRFPVQYVNRpnldFRG----YAGTIASGSVHVGDEVV 251

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 442798721  258 FLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGL 293
Cdd:TIGR02034 252 VLP-----SGRSSRVARIVTFDGDLEQARAGQAVTL 282
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 221-315 2.90e-37

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: 128.07  E-value: 2.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 221 DLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNa 300
Cdd:cd03693    2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP-----AGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVS- 75

                         90
                 ....*....|....*
gi 442798721 301 KNMPRAGDVMILKSD 315
Cdd:cd03693   76 VKDIKRGDVAGDSKN 90
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 22-293 5.12e-36

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 135.04  E-value: 5.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  22 FAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsDGNfsaaiaKGnhkage 101
Cdd:PRK05124  78 LALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLI--DAR------KG------ 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 102 VQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGLERYTEIKDEVVHMLTRVGWKKDfvaksVPVMPISGWCGDNLITK 181
Cdd:PRK05124 144 VLDQTRRHSFIATLLGIKHLVVAVNKM--DLVDYSEEVFERIREDYLTFAEQLPGNLD-----IRFVPLSALEGDNVVSQ 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 182 SDKMPWWKGADvlvgkekihvdcLLDCLENmVTIPPRTPDLAMRMPlsgafkikgVGDVL---------TGRVEQGTVKP 252
Cdd:PRK05124 217 SESMPWYSGPT------------LLEVLET-VDIQRVVDAQPFRFP---------VQYVNrpnldfrgyAGTLASGVVKV 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 442798721 253 GDECVFLPthtpstgcTGKVFTVEmhhKQV------EAAFAGDNVGL 293
Cdd:PRK05124 275 GDRVKVLP--------SGKESNVA---RIVtfdgdlEEAFAGEAITL 310
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 27-309 7.15e-36

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: 136.20  E-value: 7.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIacttkEF-FTPT-----KHYTVIDAPGHRDFIKNMITGASQADVALLMVPSD-Gnfsaaiakgnhka 99
Cdd:COG3276   26 DRLKEEKKRGITI-----DLgFAYLplpdgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADeG------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 100 geVQGQTRQHALLINLLGVKQLIVGVNKmdCDVAkyGLERYTEIKDEVvhmltrvgwkKDFVAKSV----PVMPISGWCG 175
Cdd:COG3276   88 --VMPQTREHLAILDLLGIKRGIVVLTK--ADLV--DEEWLELVEEEI----------RELLAGTFledaPIVPVSAVTG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 176 DNLitksdkmpwwkgadvlvgkekihvDCLLDCLENMV-TIPPRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD 254
Cdd:COG3276  152 EGI------------------------DELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGD 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442798721 255 ECVFLPTHTPStgctgKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMPRaGDV 309
Cdd:COG3276  208 ELELLPSGKPV-----RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIER-GDV 256
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 25-176 8.26e-34

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: 122.40  E-value: 8.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  25 YMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSDgnfsaaiaKGnhkageVQG 104
Cdd:cd00881   36 FLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDAN--------EG------VEP 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798721 105 QTRQHaLLINLLGVKQLIVGVNKMDcdvaKYGLERYTEIKDEVVHMLTRVGWKKDFvAKSVPVMPISGWCGD 176
Cdd:cd00881  102 QTREH-LNIALAGGLPIIVAVNKID----RVGEEDFDEVLREIKELLKLIGFTFLK-GKDVPIIPISALTGE 167
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 27-129 1.47e-25

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: 100.74  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfsaAIAKGnhkageVQGQT 106
Cdd:cd01884   41 DKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVV--------SATDG------PMPQT 106

                         90       100
                 ....*....|....*....|...
gi 442798721 107 RQHALLINLLGVKQLIVGVNKMD 129
Cdd:cd01884  107 REHLLLARQVGVPYIVVFLNKAD 129
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 27-308 6.89e-18

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 83.95  E-value: 6.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTI----ActtkefFTPTKHYTV---IDAPGHRDFIKNMITGASQADVALLMVPSDGNfsaaiakgnhka 99
Cdd:PRK10512  26 DRLPEEKKRGMTIdlgyA------YWPQPDGRVlgfIDVPGHEKFLSNMLAGVGGIDHALLVVACDDG------------ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 100 geVQGQTRQHALLINLLGVKQLIVGVNKMDcdvaKYGLERYTEIKDEVVHMLTRVGWkkdfvaKSVPVMPISGWCGdnli 179
Cdd:PRK10512  88 --VMAQTREHLAILQLTGNPMLTVALTKAD----RVDEARIAEVRRQVKAVLREYGF------AEAKLFVTAATEG---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 180 tksdkmpwwKGADVLvgkekihvdclldcLENMVTIPPRTPDLAMRMPLS--GAFKIKGVGDVLTGRVEQGTVKPGDEcV 257
Cdd:PRK10512 152 ---------RGIDAL--------------REHLLQLPEREHAAQHRFRLAidRAFTVKGAGLVVTGTALSGEVKVGDT-L 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442798721 258 FLpthtpsTGCTGKVFTVEMH--HKQVEAAFAGDNVGLNIKGLNAKNMPRAGD 308
Cdd:PRK10512 208 WL------TGVNKPMRVRGLHaqNQPTEQAQAGQRIALNIAGDAEKEQINRGD 254
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 225-309 1.80e-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: 75.64  E-value: 1.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 225 RMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPTHTpstgcTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMP 304
Cdd:cd03696    2 RLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGK-----EVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELE 76


                 ....*
gi 442798721 305 RaGDV 309
Cdd:cd03696   77 R-GFV 80
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 27-129 1.17e-16

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: 76.10  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTIACTTKEFFTPT-KHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfsaAIAKGnhkageVQGQ 105
Cdd:cd04171   25 DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVV--------AADEG------IMPQ 90

                         90       100
                 ....*....|....*....|....
gi 442798721 106 TRQHALLINLLGVKQLIVGVNKMD 129
Cdd:cd04171   91 TREHLEILELLGIKKGLVVLTKAD 114
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 226-305 7.62e-16

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 71.40  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 226 MPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLP-THTPSTGCTGkvftVEMHHKQVEAAFAGDNVGLNIKGLNAKNMP 304
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGfKETLKTTVTG----IEMFRKTLDEAEAGDNVGVLLRGVKKEDVE 78


                 .
gi 442798721 305 R 305
Cdd:cd03697   79 R 79
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 27-255 1.30e-15

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 76.81  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  27 DRQKDERERGVTI----------ACTTKEfftPTKHYTV-------------------IDAPGHRDFIKNMITGASQADV 77
Cdd:PRK04000  35 DRHSEELKRGITIrlgyadatirKCPDCE---EPEAYTTepkcpncgsetellrrvsfVDAPGHETLMATMLSGAALMDG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  78 ALLMVpsdgnfsAAiakgNHKAGevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKDEVvhmltrvgwk 157
Cdd:PRK04000 112 AILVI-------AA----NEPCP--QPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFV---------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 158 KDFVAKSVPVMPISgwcgdnlitksdkmpwwkgadvlvGKEKIHVDCLLDCLENMVTIPPRTPDLAMRMPLSGAFKI--- 234
Cdd:PRK04000 169 KGTVAENAPIIPVS------------------------ALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVnkp 224

                        250       260
                 ....*....|....*....|....*.
gi 442798721 235 -----KGVGDVLTGRVEQGTVKPGDE 255
Cdd:PRK04000 225 gtppeKLKGGVIGGSLIQGVLKVGDE 250
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 16-218 7.62e-14

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


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 68.83  E-value: 7.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  16 GKGSFAFAF---YMDRQKDERERGVTI------------------------ACTTKEFFTPTK---HYTVIDAPGHRDFI 65
Cdd:cd01888   12 GKTTLVKALsgvWTVRHKEELKRNITIklgyanakiykcpncgcprpydtpECECPGCGGETKlvrHVSFVDCPGHEILM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  66 KNMITGASQADVALLMVpsDGNFSAAiakgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGLERYTEIKD 145
Cdd:cd01888   92 ATMLSGAAVMDGALLLI--AANEPCP-----------QPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798721 146 EVvhmltrvgwkKDFVAKSVPVMPISgwcgdnlitksdkmpwwkgadvlvGKEKIHVDCLLDCLENMVTIPPR 218
Cdd:cd01888  159 FV----------KGTIAENAPIIPIS------------------------AQLKYNIDVLCEYIVKKIPTPPR 197
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 225-299 2.04e-13

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: 64.59  E-value: 2.04e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442798721 225 RMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLN 299
Cdd:cd01342    2 VMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP-----KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK 71
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 238-310 3.47e-13

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: 63.82  E-value: 3.47e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798721  238 GDVLTGRVEQGTVKPGDECVFLPTHTPSTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNMpRAGDVM 310
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDI-RVGDTL 72
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 51-255 8.07e-11

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 62.33  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  51 KHYTVIDAPGHRDFIKNMITGASQADVALLMVPSDGNFSaaiakgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDC 130
Cdd:PTZ00327 117 RHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCP-------------QPQTSEHLAAVEIMKLKHIIILQNKIDL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 131 DVAKYGLERYTEIKDEVvhmltrvgwkKDFVAKSVPVMPISGwcgdnlitksdkmpwwkgadVLvgkeKIHVDCLLDCLE 210
Cdd:PTZ00327 184 VKEAQAQDQYEEIRNFV----------KGTIADNAPIIPISA--------------------QL----KYNIDVVLEYIC 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442798721 211 NMVTIPPRTPDLAMRMPLSGAFKIKGVGD--------VLTGRVEQGTVKPGDE 255
Cdd:PTZ00327 230 TQIPIPKRDLTSPPRMIVIRSFDVNKPGEdienlkggVAGGSILQGVLKVGDE 282
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 224-310 1.13e-09

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


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 54.06  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 224 MRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNM 303
Cdd:cd16267    2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMP-----SNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHL 76


                 ....*..
gi 442798721 304 pRAGDVM 310
Cdd:cd16267   77 -RVGSIL 82
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 32-145 2.07e-09

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: 56.86  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  32 ERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfSAaiakgnhKAGeVQGQTRqhaL 111
Cdd:cd04168   45 ERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVI------SA-------VEG-VQAQTR---I 107

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442798721 112 LINLLgvKQL----IVGVNKMdcDVAKYGLER-YTEIKD 145
Cdd:cd04168  108 LFRLL--RKLniptIIFVNKI--DRAGADLEKvYQEIKE 142
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 224-297 2.33e-09

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: 53.26  E-value: 2.33e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442798721 224 MRMPLSGAFKIKGVgdVLTGRVEQGTVKPGDECVFLPTHTPStgctgKVFTVEMHHKQVEAAFAGDNVGLNIKG 297
Cdd:cd04089    2 LRMPILDKYKDMGT--VVMGKVESGTIRKGQKLVLMPNKTKV-----EVTGIYIDEEEVDSAKPGENVKLKLKG 68
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 25-82 5.30e-06

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: 46.49  E-value: 5.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798721  25 YMDRQKDERERGVTIACTTKEFFTPTKHY-----TVIDAPGHRDFIKNMITGASQADVALLMV 82
Cdd:cd04167   40 YTDTRKDEQERGISIKSNPISLVLEDSKGksyliNIIDTPGHVNFMDEVAAALRLCDGVVLVV 102
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 230-310 6.19e-06

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: 43.44  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 230 GAFKIKGV-----GDVLTGRVEQGTVKPGDECVFLPTHtpstgctGKVFTVEMHHKQVEAAFAGDNVGLNIKG-LNAKNm 303
Cdd:cd16265    1 GKFRVEKVfkilgRQVLTGEVESGVIYVGYKVKGDKGV-------ALIRAIEREHRKVDFAVAGDEVALILEGkIKVKE- 72


                 ....*..
gi 442798721 304 praGDVM 310
Cdd:cd16265   73 ---GDVL 76
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 226-311 1.18e-05

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


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 42.98  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721 226 MPLSGAFKIKGVGDVLTGRVEQGTVKPGDECVFLPThtpSTGC--TGKVFTVEMHHKQVEAAFAGDNVGLNIKGLNAKNM 303
Cdd:cd03694    3 FQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPD---ADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79


                 ....*...
gi 442798721 304 PRaGDVMI 311
Cdd:cd03694   80 RK-GMVLV 86
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
26-129 1.52e-05

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 46.27  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  26 MDRQKDERERGVTI--ACTTkeFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSDgnfsaaiakgnhkaGEVQ 103
Cdd:PRK12740  35 MDFMPEERERGISItsAATT--CEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAV--------------GGVE 98

                         90       100
                 ....*....|....*....|....*.
gi 442798721 104 GQTRQHALLINLLGVKQLIVgVNKMD 129
Cdd:PRK12740  99 PQTETVWRQAEKYGVPRIIF-VNKMD 123
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 26-170 1.77e-05

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: 46.19  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  26 MDRQKDERERGVTI--ACTTkeFFTPTKHYTVIDAPGHRDFIKNMITGASQADVAlLMVpsdgnFSAaiakgnhKAGeVQ 103
Cdd:COG0480   49 MDWMPEEQERGITItsAATT--CEWKGHKINIIDTPGHVDFTGEVERSLRVLDGA-VVV-----FDA-------VAG-VE 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798721 104 GQT----RQhallINLLGVKQLIVgVNKMDCDVAKYgleryteikDEVVHMLtrvgwKKDFVAKSVPV-MPI 170
Cdd:COG0480  113 PQTetvwRQ----ADKYGVPRIVF-VNKMDREGADF---------DRVLEQL-----KERLGANPVPLqLPI 165
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 26-185 2.01e-05

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: 44.51  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  26 MDRQKDERERGVTI-ACTTKEFFTPTKhYTVIDAPGHRDF------IKNMITGasqadVALLMVPSDGnfsaaiakgnhk 98
Cdd:cd01891   40 MDSNDLERERGITIlAKNTAITYKDTK-INIIDTPGHADFggeverVLSMVDG-----VLLLVDASEG------------ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  99 ageVQGQTR---QHALLINLlgvkQLIVGVNKMDCDVAkygleRYTEIKDEVVHMLTRVGWKKDFVakSVPVMPIS---G 172
Cdd:cd01891  102 ---PMPQTRfvlKKALEAGL----KPIVVINKIDRPDA-----RPEEVVDEVFDLFLELNATDEQL--DFPIVYASaknG 167

                        170
                 ....*....|...
gi 442798721 173 WCGDNLITKSDKM 185
Cdd:cd01891  168 WASLNLDDPSEDL 180
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 243-293 2.38e-05

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: 41.78  E-value: 2.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442798721 243 GRVEQGTVKPGDECVFLPthtpsTGCTGKVFTVEMHHKQVEAAFAGDNVGL 293
Cdd:cd03695   20 GTIASGSIRVGDEVTVLP-----SGKTSRVKSIVTFDGELDSAGAGEAVTL 65
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 25-82 1.83e-04

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: 41.83  E-value: 1.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442798721  25 YMDRQKDERERGVTIA-------CTTKEFFTPTKHYTV--IDAPGHRDFIKNMITGASQADVALLMV 82
Cdd:cd01885   37 YLDTREDEQERGITIKssaislyFEYEEEKMDGNDYLInlIDSPGHVDFSSEVTAALRLTDGALVVV 103
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 26-64 5.90e-04

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: 40.94  E-value: 5.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 442798721  26 MDRQKDERERGVTI--ACTTkeFFTPTKHYTVIDAPGHRDF 64
Cdd:cd01886   39 MDWMEQERERGITIqsAATT--CFWKDHRINIIDTPGHVDF 77
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 25-64 3.01e-03

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: 37.90  E-value: 3.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 442798721  25 YMDRQKDERERGVTI---ACTTKEFFTPTKHYTV--IDAPGHRDF 64
Cdd:cd01890   36 VLDSMDLERERGITIkaqAVRLFYKAKDGEEYLLnlIDTPGHVDF 80
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 54-129 3.92e-03

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: 37.45  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798721  54 TVIDAPGHRDFiKNMIT-GASQADVALLMVpsdgnfsaAIAKGnhkageVQGQTR---QHALLINllgvKQLIVGVNKMD 129
Cdd:cd01887   52 TFIDTPGHEAF-TNMRArGASVTDIAILVV--------AADDG------VMPQTIeaiNHAKAAN----VPIIVAINKID 112
 
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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