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Conserved domains on  [gi|442798715|gb|AGC75075|]
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elongation factor-like protein, partial [Sphaeroforma gastrica]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 2-320 1.97e-115

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 340.96  E-value: 1.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:PTZ00141  31 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVPSD-GNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVVHMLTRVG 160
Cdd:PTZ00141 111 VAILVVASTaGEFEAGISK--------DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 161 WKKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEhMVTIPVRTPDLAMRMPLSGAFKIK 240
Cdd:PTZ00141 183 YNPE----KVPFIPISGWQGDNMIEKSDNMPWYKGP------------TLLEALD-TLEPPKRPVDKPLRLPLQDVYKIG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 241 GVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPR---AGDVmil 317
Cdd:PTZ00141 246 GIGTVPVGRVETGILKPGMVVTFAP-----SGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRgyvASDS--- 317


                 ...
gi 442798715 318 KSD 320
Cdd:PTZ00141 318 KND 320
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-320 1.97e-115

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 340.96  E-value: 1.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:PTZ00141  31 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVPSD-GNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVVHMLTRVG 160
Cdd:PTZ00141 111 VAILVVASTaGEFEAGISK--------DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 161 WKKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEhMVTIPVRTPDLAMRMPLSGAFKIK 240
Cdd:PTZ00141 183 YNPE----KVPFIPISGWQGDNMIEKSDNMPWYKGP------------TLLEALD-TLEPPKRPVDKPLRLPLQDVYKIG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 241 GVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPR---AGDVmil 317
Cdd:PTZ00141 246 GIGTVPVGRVETGILKPGMVVTFAP-----SGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRgyvASDS--- 317


                 ...
gi 442798715 318 KSD 320
Cdd:PTZ00141 318 KND 320
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-314 4.88e-113

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: 334.21  E-value: 4.88e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:COG5256   31 TGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGW 161
Cdd:COG5256  111 AAILVV--------SAKDG------VMGQTREHAFLARTLGINQLIVAVNKM--DAVNYSEKRYEEVKEEVSKLLKMVGY 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 162 KKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEhMVTIPVRTPDLAMRMPLSGAFKIKG 241
Cdd:COG5256  175 KVD----KIPFIPVSAWKGDNVVKKSDNMPWYNGP------------TLLEALD-NLKEPEKPVDKPLRIPIQDVYSISG 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798715 242 VGDVLTGRVEQGTVKPGDECIFLPTHTpstgcTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLnAKNMPRAGDV 314
Cdd:COG5256  238 IGTVPVGRVETGVLKVGDKVVFMPAGV-----VGEVKSIEMHHEELEQAEPGDNIGFNVRGV-EKNDIKRGDV 304
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 2-218 1.05e-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: 295.17  E-value: 1.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:cd01883   23 LGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQAD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVPSD-GNFSAAIakgnhkagEVQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVVHMLTRVG 160
Cdd:cd01883  103 VAVLVVSARkGEFEAGF--------EKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVG 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442798715 161 WKKdfvaKSVPVMPISGWCGDNLITKSDKMAWWKGadvlvgkekihvDCLLDCLEHMV 218
Cdd:cd01883  175 YNP----KDVPFIPISGFTGDNLIEKSENMPWYKG------------PTLLEALDSLE 216
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 3-314 1.82e-91

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: 279.05  E-value: 1.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715    3 GGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADV 82
Cdd:TIGR00483  32 GAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   83 ALLMVpsdgnfsaaiaKGNHKAGEVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGWK 162
Cdd:TIGR00483 112 AVLVV-----------AVGDGEFEVQPQTREHAFLARTLGINQLIVAINKM--DSVNYDEEEFEAIKKEVSNLIKKVGYN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  163 KDfvakSVPVMPISGWCGDNLITKSDKMAWWKGADVLVGkekihvdclLDCLEHmvtiPVRTPDLAMRMPLSGAFKIKGV 242
Cdd:TIGR00483 179 PD----TVPFIPISAWNGDNVIKKSENTPWYKGKTLLEA---------LDALEP----PEKPTDKPLRIPIQDVYSITGV 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715  243 GDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRaGDV 314
Cdd:TIGR00483 242 GTVPVGRVETGVLKPGDKVVFEP-----AGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRR-GDV 307
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-185 3.07e-42

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: 144.59  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715    2 LGGIPEREMQKLKEEATrlgkgsfafafyMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:pfam00009  27 TGAISKRGEVKGEGEAG------------LDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQAD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   82 VALLMVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKqLIVGVNKMDCDvakyGIERYTEIKDEVVHMLTRvgw 161
Cdd:pfam00009  95 GAILVV--------DAVEG------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSRELLE--- 152

                         170       180
                  ....*....|....*....|....
gi 442798715  162 KKDFVAKSVPVMPISGWCGDNLIT 185
Cdd:pfam00009 153 KYGEDGEFVPVVPGSALKGEGVQT 176
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-320 1.97e-115

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 340.96  E-value: 1.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:PTZ00141  31 CGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVPSD-GNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVVHMLTRVG 160
Cdd:PTZ00141 111 VAILVVASTaGEFEAGISK--------DGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 161 WKKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEhMVTIPVRTPDLAMRMPLSGAFKIK 240
Cdd:PTZ00141 183 YNPE----KVPFIPISGWQGDNMIEKSDNMPWYKGP------------TLLEALD-TLEPPKRPVDKPLRLPLQDVYKIG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 241 GVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPR---AGDVmil 317
Cdd:PTZ00141 246 GIGTVPVGRVETGILKPGMVVTFAP-----SGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRgyvASDS--- 317


                 ...
gi 442798715 318 KSD 320
Cdd:PTZ00141 318 KND 320
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-314 4.88e-113

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: 334.21  E-value: 4.88e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:COG5256   31 TGAIDEHIIEKYEEEAEKKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIIDAPGHRDFVKNMITGASQAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGW 161
Cdd:COG5256  111 AAILVV--------SAKDG------VMGQTREHAFLARTLGINQLIVAVNKM--DAVNYSEKRYEEVKEEVSKLLKMVGY 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 162 KKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEhMVTIPVRTPDLAMRMPLSGAFKIKG 241
Cdd:COG5256  175 KVD----KIPFIPVSAWKGDNVVKKSDNMPWYNGP------------TLLEALD-NLKEPEKPVDKPLRIPIQDVYSISG 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798715 242 VGDVLTGRVEQGTVKPGDECIFLPTHTpstgcTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLnAKNMPRAGDV 314
Cdd:COG5256  238 IGTVPVGRVETGVLKVGDKVVFMPAGV-----VGEVKSIEMHHEELEQAEPGDNIGFNVRGV-EKNDIKRGDV 304
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-314 1.44e-110

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 327.65  E-value: 1.44e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:PRK12317  30 TGAIDEHIIEELREEAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNMITGASQAD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVpsdgnfSAAIAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGW 161
Cdd:PRK12317 110 AAVLVV------AADDAGG------VMPQTREHVFLARTLGINQLIVAINKM--DAVNYDEKRYEEVKEEVSKLLKMVGY 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 162 KKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGadvlvgkekihvDCLLDCLEhMVTIPVRTPDLAMRMPLSGAFKIKG 241
Cdd:PRK12317 176 KPD----DIPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALD-NLKPPEKPTDKPLRIPIQDVYSISG 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798715 242 VGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLnAKNMPRAGDV 314
Cdd:PRK12317 239 VGTVPVGRVETGVLKVGDKVVFMP-----AGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGV-GKKDIKRGDV 305
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 2-218 1.05e-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: 295.17  E-value: 1.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:cd01883   23 LGGVDKRTIEKYEKEAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNMITGASQAD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVPSD-GNFSAAIakgnhkagEVQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVVHMLTRVG 160
Cdd:cd01883  103 VAVLVVSARkGEFEAGF--------EKGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVG 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442798715 161 WKKdfvaKSVPVMPISGWCGDNLITKSDKMAWWKGadvlvgkekihvDCLLDCLEHMV 218
Cdd:cd01883  175 YNP----KDVPFIPISGFTGDNLIEKSENMPWYKG------------PTLLEALDSLE 216
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 3-314 1.82e-91

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: 279.05  E-value: 1.82e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715    3 GGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADV 82
Cdd:TIGR00483  32 GAIDEQTIEKFEKEAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNMITGASQADA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   83 ALLMVpsdgnfsaaiaKGNHKAGEVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGWK 162
Cdd:TIGR00483 112 AVLVV-----------AVGDGEFEVQPQTREHAFLARTLGINQLIVAINKM--DSVNYDEEEFEAIKKEVSNLIKKVGYN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  163 KDfvakSVPVMPISGWCGDNLITKSDKMAWWKGADVLVGkekihvdclLDCLEHmvtiPVRTPDLAMRMPLSGAFKIKGV 242
Cdd:TIGR00483 179 PD----TVPFIPISAWNGDNVIKKSENTPWYKGKTLLEA---------LDALEP----PEKPTDKPLRIPIQDVYSITGV 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715  243 GDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRaGDV 314
Cdd:TIGR00483 242 GTVPVGRVETGVLKPGDKVVFEP-----AGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRR-GDV 307
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-311 1.58e-76

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 241.53  E-value: 1.58e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   2 LGGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:PLN00043  31 LGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVPS-DGNFSAAIAKgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVVHMLTRVG 160
Cdd:PLN00043 111 CAVLIIDStTGGFEAGISK--------DGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 161 WKKDfvakSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEHmVTIPVRTPDLAMRMPLSGAFKIK 240
Cdd:PLN00043 183 YNPD----KIPFVPISGFEGDNMIERSTNLDWYKGP------------TLLEALDQ-INEPKRPSDKPLRLPLQDVYKIG 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442798715 241 GVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRA 311
Cdd:PLN00043 246 GIGTVPVGRVETGVIKPGMVVTFGP-----TGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRG 311
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 3-298 1.90e-56

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 188.76  E-value: 1.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   3 GGIPEREMQKLKEEATRLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADV 82
Cdd:COG2895   42 KSIFEDQLAALERDSKKRGTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  83 ALLMVpsDgnfsAaiAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGWk 162
Cdd:COG2895  122 AILLI--D----A--RKG------VLEQTRRHSYIASLLGIRHVVVAVNKM--DLVDYSEEVFEEIVADYRAFAAKLGL- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 163 kdfvaKSVPVMPISGWCGDNLITKSDKMAWWKGAdvlvgkekihvdCLLDCLEHmVTIPVRTPDLAMRMPlsgafkikgV 242
Cdd:COG2895  185 -----EDITFIPISALKGDNVVERSENMPWYDGP------------TLLEHLET-VEVAEDRNDAPFRFP---------V 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442798715 243 GDVL---------TGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGL 298
Cdd:COG2895  238 QYVNrpnldfrgyAGTIASGTVRVGDEVVVLP-----SGKTSTVKSIVTFDGDLEEAFAGQSVTL 297
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 3-209 4.70e-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: 150.03  E-value: 4.70e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   3 GGIPEREMQKLKEEAT-RLGKGSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:cd04166   24 KSIFEDQLAALERSKSsGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTAD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  82 VALLMVpsDGNfsaaiaKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGw 161
Cdd:cd04166  104 LAILLV--DAR------KG------VLEQTRRHSYIASLLGIRHVVVAVNKM--DLVDYDEEVFEEIKADYLAFAASLG- 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 442798715 162 kkdfvAKSVPVMPISGWCGDNLITKSDKMAWWKGADVLVGKEKIHVDC 209
Cdd:cd04166  167 -----IEDITFIPISALEGDNVVSRSENMPWYKGPTLLEHLETVEIAS 209
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 32-302 8.51e-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: 154.54  E-value: 8.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGnfsaaiakgnhkageVQGQ 110
Cdd:COG0050   51 DKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSaTDG---------------PMPQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 111 TRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERyteIKDEVVHMLTrvgwKKDFVAKSVPVMPISGwcgdnliTK---S 187
Cdd:COG0050  116 TREHILLARQVGVPYIVVFLNKCDMVDDEELLEL---VEMEVRELLS----KYGFPGDDTPIIRGSA-------LKaleG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 188 DKMAWWKGAdvlvgkekihVDCLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC-IFLPT 266
Cdd:COG0050  182 DPDPEWEKK----------ILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVeIVGIR 251

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442798715 267 HTPSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKG 302
Cdd:COG0050  252 DTQKTVVTG----VEMFRKLLDEGEAGDNVGLLLRG 283
PLN03127 PLN03127
Elongation factor Tu; Provisional
 23-315 6.79e-43

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 153.44  E-value: 6.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  23 GSFAFAF-YMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPS-DGNFSaaiakg 100
Cdd:PLN03127  90 KAKAVAFdEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSApDGPMP------ 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 101 nhkagevqgQTRQHALLINLLGVKQLIVGVNKmdCDVAKygieryTEIKDEVVHMLTRvgwkkdfvaksvPVMPISGWCG 180
Cdd:PLN03127 164 ---------QTKEHILLARQVGVPSLVVFLNK--VDVVD------DEELLELVEMELR------------ELLSFYKFPG 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 181 DNL-ITKSDKMAWWKGADVLVGKEKIHVdcLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD 259
Cdd:PLN03127 215 DEIpIIRGSALSALQGTNDEIGKNAILK--LMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGE 292

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442798715 260 ECIFL---PTHTPSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRaGDVM 315
Cdd:PLN03127 293 EVEIVglrPGGPLKTTVTG----VEMFKKILDQGQAGDNVGLLLRGLKREDVQR-GQVI 346
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 2-185 3.07e-42

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: 144.59  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715    2 LGGIPEREMQKLKEEATrlgkgsfafafyMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQAD 81
Cdd:pfam00009  27 TGAISKRGEVKGEGEAG------------LDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKEVIRGLAQAD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   82 VALLMVpsdgnfsaAIAKGnhkageVQGQTRQHALLINLLGVKqLIVGVNKMDCDvakyGIERYTEIKDEVVHMLTRvgw 161
Cdd:pfam00009  95 GAILVV--------DAVEG------VMPQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSRELLE--- 152

                         170       180
                  ....*....|....*....|....
gi 442798715  162 KKDFVAKSVPVMPISGWCGDNLIT 185
Cdd:pfam00009 153 KYGEDGEFVPVVPGSALKGEGVQT 176
PRK12736 PRK12736
elongation factor Tu; Reviewed
 32-310 1.51e-41

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 148.55  E-value: 1.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMV-PSDGnfsaaiakgnhkageVQGQ 110
Cdd:PRK12736  51 DAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVaATDG---------------PMPQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 111 TRQHALLINLLGVKQLIVGVNKmdCDVAkyGIERYTEIKD-EVVHMLTrvgwKKDFVAKSVPVMPISGWC---GDNLITK 186
Cdd:PRK12736 116 TREHILLARQVGVPYLVVFLNK--VDLV--DDEELLELVEmEVRELLS----EYDFPGDDIPVIRGSALKaleGDPKWED 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 187 SdkmawwkgadvlvgkekihVDCLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC-IFLP 265
Cdd:PRK12736 188 A-------------------IMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVeIVGI 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442798715 266 THTPSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPR 310
Cdd:PRK12736 249 KETQKTVVTG----VEMFRKLLDEGQAGDNVGVLLRGVDRDEVER 289
PRK00049 PRK00049
elongation factor Tu; Reviewed
 32-302 7.96e-41

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 146.87  E-value: 7.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPS-DGnfsaaiakgnhkageVQGQ 110
Cdd:PRK00049  51 DKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAaDG---------------PMPQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 111 TRQHALLINLLGVKQLIVGVNKmdCDVAKYgiERYTEIKD-EVVHMLTrvgwKKDFVAKSVPVmpisgwcgdnlITKSDK 189
Cdd:PRK00049 116 TREHILLARQVGVPYIVVFLNK--CDMVDD--EELLELVEmEVRELLS----KYDFPGDDTPI-----------IRGSAL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 190 MAwWKGADVLVGKEKIHVdcLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC-IFLPTHT 268
Cdd:PRK00049 177 KA-LEGDDDEEWEKKILE--LMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVeIVGIRDT 253

                        250       260       270
                 ....*....|....*....|....*....|....
gi 442798715 269 PSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKG 302
Cdd:PRK00049 254 QKTTVTG----VEMFRKLLDEGQAGDNVGALLRG 283
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 31-310 3.47e-40

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: 144.92  E-value: 3.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   31 MDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGnfsaaiakgnhkageVQG 109
Cdd:TIGR00485  50 IDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSaTDG---------------PMP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  110 QTRQHALLINLLGVKQLIVGVNKmdCDVAKyGIERYTEIKDEVVHMLTrvgwKKDFVAKSVPVMPisgwcGDNLITKSDK 189
Cdd:TIGR00485 115 QTREHILLARQVGVPYIVVFLNK--CDMVD-DEELLELVEMEVRELLS----QYDFPGDDTPIIR-----GSALKALEGD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  190 MAWwkgadvlvgKEKIHVdcLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC-IFLPTHT 268
Cdd:TIGR00485 183 AEW---------EAKILE--LMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVeIVGLKDT 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 442798715  269 PSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPR 310
Cdd:TIGR00485 252 RKTTVTG----VEMFRKELDEGRAGDNVGLLLRGIKREEIER 289
PRK12735 PRK12735
elongation factor Tu; Reviewed
 32-302 3.47e-39

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 142.28  E-value: 3.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfSAAiakgnhkagevQG-- 109
Cdd:PRK12735  51 DNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVV------SAA-----------DGpm 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 110 -QTRQHALLINLLGVKQLIVGVNKMD-CDVAkygiERYTEIKDEVVHMLTrvgwKKDFVAKSVPVmpisgwcgdnlITKS 187
Cdd:PRK12735 114 pQTREHILLARQVGVPYIVVFLNKCDmVDDE----ELLELVEMEVRELLS----KYDFPGDDTPI-----------IRGS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 188 DKMAwWKGADVLVGKEKIhvDCLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC-IFLPT 266
Cdd:PRK12735 175 ALKA-LEGDDDEEWEAKI--LELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVeIVGIK 251

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442798715 267 HTPSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKG 302
Cdd:PRK12735 252 ETQKTTVTG----VEMFRKLLDEGQAGDNVGVLLRG 283
PLN03126 PLN03126
Elongation factor Tu; Provisional
 31-317 6.35e-38

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 140.52  E-value: 6.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  31 MDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGNFSaaiakgnhkagevqg 109
Cdd:PLN03126 119 IDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSgADGPMP--------------- 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 110 QTRQHALLINLLGVKQLIVGVNKMDcDVAKYGIERYTEIkdEVVHMLTrvgwKKDFVAKSVPVmpISGWCGDNLITKSDK 189
Cdd:PLN03126 184 QTKEHILLAKQVGVPNMVVFLNKQD-QVDDEELLELVEL--EVRELLS----SYEFPGDDIPI--ISGSALLALEALMEN 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 190 MAWWKGADVLVgkEKIHVdcLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDEC-IFLPTHT 268
Cdd:PLN03126 255 PNIKRGDNKWV--DKIYE--LMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVdIVGLRET 330

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442798715 269 PSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRAgdvMIL 317
Cdd:PLN03126 331 RSTTVTG----VEMFQKILDEALAGDNVGLLLRGIQKADIQRG---MVL 372
tufA CHL00071
elongation factor Tu
 32-317 1.40e-37

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 138.55  E-value: 1.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVP-SDGNFSaaiakgnhkagevqgQ 110
Cdd:CHL00071  51 DSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSaADGPMP---------------Q 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 111 TRQHALLINLLGVKQLIVGVNKMDcdvaKYGIERYTE-IKDEVVHMLTrvgwKKDFVAKSVPVMPISGWCGDNLITKSDK 189
Cdd:CHL00071 116 TKEHILLAKQVGVPNIVVFLNKED----QVDDEELLElVELEVRELLS----KYDFPGDDIPIVSGSALLALEALTENPK 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 190 MAwwKGADVLVgkEKIHVdcLLDCLEHMVTIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD--ECIFLpTH 267
Cdd:CHL00071 188 IK--RGENKWV--DKIYN--LMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDtvEIVGL-RE 260

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442798715 268 TPSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRAgdvMIL 317
Cdd:CHL00071 261 TKTTTVTG----LEMFQKTLDEGLAGDNVGILLRGIQKEDIERG---MVL 303
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 226-320 1.87e-36

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: 126.53  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 226 DLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNa 305
Cdd:cd03693    2 DKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAP-----AGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVS- 75

                         90
                 ....*....|....*
gi 442798715 306 KNMPRAGDVMILKSD 320
Cdd:cd03693   76 VKDIKRGDVAGDSKN 90
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 27-298 7.98e-36

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 136.60  E-value: 7.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  27 FAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSdgnfsaaiAKGnhkage 106
Cdd:PRK05506  75 LALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDA--------RKG------ 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 107 VQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGwkkdfvAKSVPVMPISGWCGDNLITK 186
Cdd:PRK05506 141 VLTQTRRHSFIASLLGIRHVVLAVNKM--DLVDYDQEVFDEIVADYRAFAAKLG------LHDVTFIPISALKGDNVVTR 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 187 SDKMAWWKGADVlvgkekihvdclldcLEHMVTIPVRTPDLA--MRMPlsgafkikgVGDV---------LTGRVEQGTV 255
Cdd:PRK05506 213 SARMPWYEGPSL---------------LEHLETVEIASDRNLkdFRFP---------VQYVnrpnldfrgFAGTVASGVV 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442798715 256 KPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGL 298
Cdd:PRK05506 269 RPGDEVVVLP-----SGKTSRVKRIVTPDGDLDEAFAGQAVTL 306
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 32-314 2.60e-34

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: 132.34  E-value: 2.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIacttkEF-FTPT-----KHYTVIDAPGHRDFIKNMITGASQADVALLMVPSD-Gnfsaaiakgnhka 104
Cdd:COG3276   26 DRLKEEKKRGITI-----DLgFAYLplpdgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVVAADeG------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 105 geVQGQTRQHALLINLLGVKQLIVGVNKmdCDVAkyGIERYTEIKDEVvhmltrvgwkKDFVAKSV----PVMPISGWCG 180
Cdd:COG3276   88 --VMPQTREHLAILDLLGIKRGIVVLTK--ADLV--DEEWLELVEEEI----------RELLAGTFledaPIVPVSAVTG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 181 DNLitksdkmawwkgadvlvgkekihvDCLLDCLEHMV-TIPVRTPDLAMRMPLSGAFKIKGVGDVLTGRVEQGTVKPGD 259
Cdd:COG3276  152 EGI------------------------DELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGD 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442798715 260 ECIFLPTHTPStgctgKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMPRaGDV 314
Cdd:COG3276  208 ELELLPSGKPV-----RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIER-GDV 256
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 5-298 7.78e-34

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 128.26  E-value: 7.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715    5 IPEREMQKLKEEATRLGK--GSFAFAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADV 82
Cdd:TIGR02034  27 IYEDQLAALERDSKKHGTqgGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715   83 ALLMVPSdgnfsaaiAKGnhkageVQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVvhmltrVGWK 162
Cdd:TIGR02034 107 AVLLVDA--------RKG------VLEQTRRHSYIASLLGIRHVVLAVNKM--DLVDYDEEVFENIKKDY------LAFA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  163 KDFVAKSVPVMPISGWCGDNLITKSDKMAWWKGADVlvgkekihvdclldcLEHMVTIPV--RTPDLAMRMPLSGAFK-- 238
Cdd:TIGR02034 165 EQLGFRDVTFIPLSALKGDNVVSRSESMPWYSGPTL---------------LEILETVEVerDAQDLPLRFPVQYVNRpn 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715  239 --IKGvgdvLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGL 298
Cdd:TIGR02034 230 ldFRG----YAGTIASGSVHVGDEVVVLP-----SGRSSRVARIVTFDGDLEQARAGQAVTL 282
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 30-181 1.86e-33

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: 121.63  E-value: 1.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  30 YMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSDgnfsaaiaKGnhkageVQG 109
Cdd:cd00881   36 FLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVRGLAQADGALLVVDAN--------EG------VEP 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715 110 QTRQHaLLINLLGVKQLIVGVNKMDcdvaKYGIERYTEIKDEVVHMLTRVGWKKDFvAKSVPVMPISGWCGD 181
Cdd:cd00881  102 QTREH-LNIALAGGLPIIVAVNKID----RVGEEDFDEVLREIKELLKLIGFTFLK-GKDVPIIPISALTGE 167
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 27-323 2.69e-33

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 127.72  E-value: 2.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  27 FAFYMDRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsDGNfsaaiaKGnhkage 106
Cdd:PRK05124  78 LALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLI--DAR------KG------ 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 107 VQGQTRQHALLINLLGVKQLIVGVNKMdcDVAKYGIERYTEIKDEVVHMLTRVGWKKDfvaksVPVMPISGWCGDNLITK 186
Cdd:PRK05124 144 VLDQTRRHSFIATLLGIKHLVVAVNKM--DLVDYSEEVFERIREDYLTFAEQLPGNLD-----IRFVPLSALEGDNVVSQ 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 187 SDKMAWWKGADvlvgkekihvdcLLDCLEhMVTIPVRTPDLAMRMPlsgafkikgVGDVL---------TGRVEQGTVKP 257
Cdd:PRK05124 217 SESMPWYSGPT------------LLEVLE-TVDIQRVVDAQPFRFP---------VQYVNrpnldfrgyAGTLASGVVKV 274

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715 258 GDECIFLPthtpstgcTGKVFTVEmhhKQV------DAAYAGDNVGLNIKglNAKNMPRaGDvMILKSDTTL 323
Cdd:PRK05124 275 GDRVKVLP--------SGKESNVA---RIVtfdgdlEEAFAGEAITLVLE--DEIDISR-GD-LLVAADEAL 331
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 32-134 3.54e-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: 99.97  E-value: 3.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfsaAIAKGnhkageVQGQT 111
Cdd:cd01884   41 DKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNMITGAAQMDGAILVV--------SATDG------PMPQT 106

                         90       100
                 ....*....|....*....|...
gi 442798715 112 RQHALLINLLGVKQLIVGVNKMD 134
Cdd:cd01884  107 REHLLLARQVGVPYIVVFLNKAD 129
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 32-313 9.55e-19

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 87.03  E-value: 9.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTI----ActtkefFTPTKHYTV---IDAPGHRDFIKNMITGASQADVALLMVPSDGNfsaaiakgnhka 104
Cdd:PRK10512  26 DRLPEEKKRGMTIdlgyA------YWPQPDGRVlgfIDVPGHEKFLSNMLAGVGGIDHALLVVACDDG------------ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 105 geVQGQTRQHALLINLLGVKQLIVGVNKMDcdvaKYGIERYTEIKDEVVHMLTRVGWkkdfvaKSVPVMPISGWCGdnli 184
Cdd:PRK10512  88 --VMAQTREHLAILQLTGNPMLTVALTKAD----RVDEARIAEVRRQVKAVLREYGF------AEAKLFVTAATEG---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 185 tksdkmawwKGADVLvgkekihvdclldcLEHMVTIPVRTPDLAMRMPLS--GAFKIKGVGDVLTGRVEQGTVKPGDEcI 262
Cdd:PRK10512 152 ---------RGIDAL--------------REHLLQLPEREHAAQHRFRLAidRAFTVKGAGLVVTGTALSGEVKVGDT-L 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442798715 263 FLpthtpsTGCTGKVFTVEMH--HKQVDAAYAGDNVGLNIKGLNAKNMPRAGD 313
Cdd:PRK10512 208 WL------TGVNKPMRVRGLHaqNQPTEQAQAGQRIALNIAGDAEKEQINRGD 254
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 230-314 1.13e-16

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: 73.71  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 230 RMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECIFLPTHTpstgcTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMP 309
Cdd:cd03696    2 RLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGK-----EVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELE 76


                 ....*
gi 442798715 310 RaGDV 314
Cdd:cd03696   77 R-GFV 80
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 32-134 2.07e-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: 75.72  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTIACTTKEFFTPT-KHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfsaAIAKGnhkageVQGQ 110
Cdd:cd04171   25 DRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLVV--------AADEG------IMPQ 90

                         90       100
                 ....*....|....*....|....
gi 442798715 111 TRQHALLINLLGVKQLIVGVNKMD 134
Cdd:cd04171   91 TREHLEILELLGIKKGLVVLTKAD 114
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 231-310 1.03e-15

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 71.01  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 231 MPLSGAFKIKGVGDVLTGRVEQGTVKPGDECIFLP-THTPSTGCTGkvftVEMHHKQVDAAYAGDNVGLNIKGLNAKNMP 309
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGfKETLKTTVTG----IEMFRKTLDEAEAGDNVGVLLRGVKKEDVE 78


                 .
gi 442798715 310 R 310
Cdd:cd03697   79 R 79
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 32-260 4.57e-15

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 75.27  E-value: 4.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  32 DRQKDERERGVTI----------ACTTKEfftPTKHYTV-------------------IDAPGHRDFIKNMITGASQADV 82
Cdd:PRK04000  35 DRHSEELKRGITIrlgyadatirKCPDCE---EPEAYTTepkcpncgsetellrrvsfVDAPGHETLMATMLSGAALMDG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  83 ALLMVpsdgnfsAAiakgNHKAGevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKDEVvhmltrvgwk 162
Cdd:PRK04000 112 AILVI-------AA----NEPCP--QPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFV---------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 163 KDFVAKSVPVMPISgwcgdnlitksdkmawwkgadvlvGKEKIHVDCLLDCLEHMVTIPVRTPDLAMRMPLSGAFKI--- 239
Cdd:PRK04000 169 KGTVAENAPIIPVS------------------------ALHKVNIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVnkp 224

                        250       260
                 ....*....|....*....|....*.
gi 442798715 240 -----KGVGDVLTGRVEQGTVKPGDE 260
Cdd:PRK04000 225 gtppeKLKGGVIGGSLIQGVLKVGDE 250
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 230-304 1.32e-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: 65.36  E-value: 1.32e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442798715 230 RMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLN 304
Cdd:cd01342    2 VMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP-----KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK 71
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 243-315 2.80e-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: 64.21  E-value: 2.80e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798715  243 GDVLTGRVEQGTVKPGDECIFLPTHTPSTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNMpRAGDVM 315
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDI-RVGDTL 72
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 21-223 6.16e-13

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


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 66.52  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  21 GKGSFAFAF---YMDRQKDERERGVTI------------------------ACTTKEFFTPTK---HYTVIDAPGHRDFI 70
Cdd:cd01888   12 GKTTLVKALsgvWTVRHKEELKRNITIklgyanakiykcpncgcprpydtpECECPGCGGETKlvrHVSFVDCPGHEILM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  71 KNMITGASQADVALLMVpsDGNFSAAiakgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDCDVAKYGIERYTEIKD 150
Cdd:cd01888   92 ATMLSGAAVMDGALLLI--AANEPCP-----------QPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALENYEQIKE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798715 151 EVvhmltrvgwkKDFVAKSVPVMPISgwcgdnlitksdkmawwkgadvlvGKEKIHVDCLLDCLEHMVTIPVR 223
Cdd:cd01888  159 FV----------KGTIAENAPIIPIS------------------------AQLKYNIDVLCEYIVKKIPTPPR 197
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 56-260 5.28e-11

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 63.10  E-value: 5.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  56 KHYTVIDAPGHRDFIKNMITGASQADVALLMVPSDGNFSaaiakgnhkagevQGQTRQHALLINLLGVKQLIVGVNKMDC 135
Cdd:PTZ00327 117 RHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCP-------------QPQTSEHLAAVEIMKLKHIIILQNKIDL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 136 DVAKYGIERYTEIKDEVvhmltrvgwkKDFVAKSVPVMPISGwcgdnlitksdkmawwkgadVLvgkeKIHVDCLLDCLE 215
Cdd:PTZ00327 184 VKEAQAQDQYEEIRNFV----------KGTIADNAPIIPISA--------------------QL----KYNIDVVLEYIC 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442798715 216 HMVTIPVRTPDLAMRMPLSGAFKIKGVGD--------VLTGRVEQGTVKPGDE 260
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 ...
 229-315 1.19e-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: 54.44  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 229 MRMPLSGAFKIKGVGDVLTGRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNM 308
Cdd:cd16267    2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMP-----SNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHL 76


                 ....*..
gi 442798715 309 pRAGDVM 315
Cdd:cd16267   77 -RVGSIL 82
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 229-302 1.31e-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: 54.03  E-value: 1.31e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442798715 229 MRMPLSGAFKIKGVgdVLTGRVEQGTVKPGDECIFLPTHTPStgctgKVFTVEMHHKQVDAAYAGDNVGLNIKG 302
Cdd:cd04089    2 LRMPILDKYKDMGT--VVMGKVESGTIRKGQKLVLMPNKTKV-----EVTGIYIDEEEVDSAKPGENVKLKLKG 68
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 37-150 1.20e-08

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: 54.94  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  37 ERERGVTIACTTKEFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVpsdgnfSAaiakgnhKAGeVQGQTRqhaL 116
Cdd:cd04168   45 ERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEVERSLSVLDGAILVI------SA-------VEG-VQAQTR---I 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 442798715 117 LINLLgvKQL----IVGVNKMDcdvaKYGIER---YTEIKD 150
Cdd:cd04168  108 LFRLL--RKLniptIIFVNKID----RAGADLekvYQEIKE 142
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 231-316 1.42e-06

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: 45.67  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 231 MPLSGAFKIKGVGDVLTGRVEQGTVKPGDECIFLPThtpSTGC--TGKVFTVEMHHKQVDAAYAGDNVGLNIKGLNAKNM 308
Cdd:cd03694    3 FQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPD---ADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79


                 ....*...
gi 442798715 309 PRaGDVMI 316
Cdd:cd03694   80 RK-GMVLV 86
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 235-315 5.36e-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: 43.82  E-value: 5.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 235 GAFKIKGV-----GDVLTGRVEQGTVKPGDECIFLPTHtpstgctGKVFTVEMHHKQVDAAYAGDNVGLNIKG-LNAKNm 308
Cdd:cd16265    1 GKFRVEKVfkilgRQVLTGEVESGVIYVGYKVKGDKGV-------ALIRAIEREHRKVDFAVAGDEVALILEGkIKVKE- 72


                 ....*..
gi 442798715 309 praGDVM 315
Cdd:cd16265   73 ---GDVL 76
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 30-87 6.42e-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: 6.42e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442798715  30 YMDRQKDERERGVTIACTTKEFFTPTKHY-----TVIDAPGHRDFIKNMITGASQADVALLMV 87
Cdd:cd04167   40 YTDTRKDEQERGISIKSNPISLVLEDSKGksyliNIIDTPGHVNFMDEVAAALRLCDGVVLVV 102
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
31-134 1.65e-05

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 46.27  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  31 MDRQKDERERGVTI--ACTTkeFFTPTKHYTVIDAPGHRDFIKNMITGASQADVALLMVPSDgnfsaaiakgnhkaGEVQ 108
Cdd:PRK12740  35 MDFMPEERERGISItsAATT--CEWKGHKINLIDTPGHVDFTGEVERALRVLDGAVVVVCAV--------------GGVE 98

                         90       100
                 ....*....|....*....|....*.
gi 442798715 109 GQTRQHALLINLLGVKQLIVgVNKMD 134
Cdd:PRK12740  99 PQTETVWRQAEKYGVPRIIF-VNKMD 123
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 31-191 1.87e-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: 44.89  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  31 MDRQKDERERGVTI-ACTTKEFFTPTKhYTVIDAPGHRDF------IKNMITGasqadVALLMVPSDGnfsaaiakgnhk 103
Cdd:cd01891   40 MDSNDLERERGITIlAKNTAITYKDTK-INIIDTPGHADFggeverVLSMVDG-----VLLLVDASEG------------ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715 104 ageVQGQTR---QHALLINLlgvkQLIVGVNKMDCDVAkygieRYTEIKDEVVHMLTRVGWKKDFVakSVPVMPIS---G 177
Cdd:cd01891  102 ---PMPQTRfvlKKALEAGL----KPIVVINKIDRPDA-----RPEEVVDEVFDLFLELNATDEQL--DFPIVYASaknG 167

                        170
                 ....*....|....
gi 442798715 178 WCGDNLITKSDKMA 191
Cdd:cd01891  168 WASLNLDDPSEDLD 181
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 31-175 1.96e-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: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  31 MDRQKDERERGVTI--ACTTkeFFTPTKHYTVIDAPGHRDFIKNMITGASQADVAlLMVpsdgnFSAaiakgnhKAGeVQ 108
Cdd:COG0480   49 MDWMPEEQERGITItsAATT--CEWKGHKINIIDTPGHVDFTGEVERSLRVLDGA-VVV-----FDA-------VAG-VE 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715 109 GQT----RQhallINLLGVKQLIVgVNKMDCDVAKYgieryteikDEVVHMLtrvgwKKDFVAKSVPV-MPI 175
Cdd:COG0480  113 PQTetvwRQ----ADKYGVPRIVF-VNKMDREGADF---------DRVLEQL-----KERLGANPVPLqLPI 165
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 248-298 3.78e-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: 41.40  E-value: 3.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442798715 248 GRVEQGTVKPGDECIFLPthtpsTGCTGKVFTVEMHHKQVDAAYAGDNVGL 298
Cdd:cd03695   20 GTIASGSIRVGDEVTVLP-----SGKTSRVKSIVTFDGELDSAGAGEAVTL 65
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 30-87 2.23e-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: 2.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442798715  30 YMDRQKDERERGVTIA-------CTTKEFFTPTKHYTV--IDAPGHRDFIKNMITGASQADVALLMV 87
Cdd:cd01885   37 YLDTREDEQERGITIKssaislyFEYEEEKMDGNDYLInlIDSPGHVDFSSEVTAALRLTDGALVVV 103
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 3-69 3.80e-04

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: 40.59  E-value: 3.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442798715   3 GGIPEREMQklkeeatrlgkgsfafAFYMDRQKDERERGVTI---ACTTKEFFTPTKHYTV--IDAPGHRDF 69
Cdd:cd01890   25 GTVSEREMK----------------EQVLDSMDLERERGITIkaqAVRLFYKAKDGEEYLLnlIDTPGHVDF 80
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 31-69 6.94e-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: 40.55  E-value: 6.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 442798715  31 MDRQKDERERGVTI--ACTTkeFFTPTKHYTVIDAPGHRDF 69
Cdd:cd01886   39 MDWMEQERERGITIqsAATT--CFWKDHRINIIDTPGHVDF 77
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 59-134 6.00e-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: 37.07  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442798715  59 TVIDAPGHRDFiKNMIT-GASQADVALLMVpsdgnfsaAIAKGnhkageVQGQTR---QHALLINllgvKQLIVGVNKMD 134
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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