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Conserved domains on  [gi|25306283|ref|NP_733781|]
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ribosome-releasing factor 2, mitochondrial isoform 3 [Homo sapiens]

Protein Classification

translation factor GTPase family protein( domain architecture ID 1903461)

translation factor GTPase family protein such as elongation factor G that catalyzes the translocation step of protein synthesis, and TetM/TetW/TetO/TetS family tetracycline resistance ribosomal protection proteins that abolish the inhibitory effect of tetracyclin on protein synthesis; contains a PIN/NYN nuclease domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FusA super family cl43154
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 66-498 2.10e-178

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


The actual alignment was detected with superfamily member COG0480:

Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 517.68  E-value: 2.10e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  66 PIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGH 145
Cdd:COG0480   5 PLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLP 225
Cdd:COG0480  85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLP 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 226 IGEAKTFKGVVDVVMKEKLLWncNSNDGKDFERKPLlemnDPELLKETTEARNALIEQVADLDDEFADLVLEEfsenfDL 305
Cdd:COG0480 165 IGAEDDFKGVIDLVTMKAYVY--DDELGAKYEEEEI----PAELKEEAEEAREELIEAVAETDDELMEKYLEG-----EE 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 306 LPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEER----------NYEFLQWYKDD--LCALAFK 373
Cdd:COG0480 234 LTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVpaikgvdpdtGEEVERKPDDDepFSALVFK 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 374 VLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIvsskss 453
Cdd:COG0480 314 TMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTL------ 387

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 25306283 454 alaaarraeregekkhrqNNEAERLLLAGVEIPEPVFFCTIEPPS 498
Cdd:COG0480 388 ------------------CDEDHPIVLEPIEFPEPVISVAIEPKT 414
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 66-498 2.10e-178

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: 517.68  E-value: 2.10e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  66 PIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGH 145
Cdd:COG0480   5 PLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLP 225
Cdd:COG0480  85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLP 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 226 IGEAKTFKGVVDVVMKEKLLWncNSNDGKDFERKPLlemnDPELLKETTEARNALIEQVADLDDEFADLVLEEfsenfDL 305
Cdd:COG0480 165 IGAEDDFKGVIDLVTMKAYVY--DDELGAKYEEEEI----PAELKEEAEEAREELIEAVAETDDELMEKYLEG-----EE 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 306 LPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEER----------NYEFLQWYKDD--LCALAFK 373
Cdd:COG0480 234 LTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVpaikgvdpdtGEEVERKPDDDepFSALVFK 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 374 VLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIvsskss 453
Cdd:COG0480 314 TMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTL------ 387

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 25306283 454 alaaarraeregekkhrqNNEAERLLLAGVEIPEPVFFCTIEPPS 498
Cdd:COG0480 388 ------------------CDEDHPIVLEPIEFPEPVISVAIEPKT 414
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 72-352 7.85e-160

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: 454.64  E-value: 7.85e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKT 231
Cdd:cd01886  81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 232 FKGVVDVVMKEKLLWncNSNDGKDFERKPLlemnDPELLKETTEARNALIEQVADLDDEFADLVLEEFSenfdlLPAEKL 311
Cdd:cd01886 161 FEGVVDLIEMKALYW--DGELGEKIEETDI----PEDLLEEAEEAREELIETLAEVDDELMEKYLEGEE-----ITEEEI 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25306283 312 QTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP 352
Cdd:cd01886 230 KAAIRKGTIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
PRK13351 PRK13351
elongation factor G-like protein;
64-496 1.79e-150

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 445.94  E-value: 1.79e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   64 NPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTP 143
Cdd:PRK13351   2 EMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  144 GHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQ 223
Cdd:PRK13351  82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  224 LPIGEAKTFKGVVDVVMKEKLLWNcNSNDGKDFERKPLLEmndpELLKETTEARNALIEQVADLDDEfadlVLEEFSENF 303
Cdd:PRK13351 162 LPIGSEDGFEGVVDLITEPELHFS-EGDGGSTVEEGPIPE----ELLEEVEEAREKLIEALAEFDDE----LLELYLEGE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  304 DlLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNyeFLQWYKDD-------------LCAL 370
Cdd:PRK13351 233 E-LSAEQLRAPLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVP--PPRGSKDNgkpvkvdpdpekpLLAL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  371 AFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSs 450
Cdd:PRK13351 310 VFKVQYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHD- 388

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 25306283  451 kssalaaarraeregekkhrqnnEAERLLLAGVEIPEPVFFCTIEP 496
Cdd:PRK13351 389 -----------------------SADPVLLELLTFPEPVVSLAVEP 411
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
 66-502 4.21e-138

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 414.59  E-value: 4.21e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    66 PIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGH 145
Cdd:TIGR00484   6 DLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLP 225
Cdd:TIGR00484  86 VDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   226 IGEAKTFKGVVDVVMKEKLLWncNSNDGKDFERKPLLEmndpELLKETTEARNALIEQVADLDDEFADLVLEEfsenfDL 305
Cdd:TIGR00484 166 IGAEDNFIGVIDLVEMKAYFF--NGDKGTKAIEKEIPS----DLLEQAKELRENLVEAVAEFDEELMEKYLEG-----EE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   306 LPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP----------EERNYEFLQWYKDDL--CALAFK 373
Cdd:TIGR00484 235 LTIEEIKNAIRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidPDTEKEIERKASDDEpfSALAFK 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   374 VLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVsskss 453
Cdd:TIGR00484 315 VATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLC----- 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 25306283   454 alaaarraeregekkhrqnNEAERLLLAGVEIPEPVFFCTIEPPSLSKQ 502
Cdd:TIGR00484 390 -------------------DPKIDVILERMEFPEPVISLAVEPKTKADQ 419
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 69-351 2.51e-67

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: 214.70  E-value: 2.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    69 KIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTD-FMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVD 147
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGLdNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   148 FTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDK-TGASFKYAVESIREKLKAKplllqlpI 226
Cdd:pfam00009  82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRvDGAELEEVVEEVSRELLEK-------Y 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   227 GEAKTFkgvvdvvmkekllwncnsndgkdferkpllemndpellkettearnalieqvadlddefadlvleefsenfdll 306
Cdd:pfam00009 155 GEDGEF-------------------------------------------------------------------------- 160

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 25306283   307 paeklqtaihrvtlaqtaVPVLCGSALKNKGIQPLLDAVTMYLPS 351
Cdd:pfam00009 161 ------------------VPVVPGSALKGEGVQTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 66-498 2.10e-178

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: 517.68  E-value: 2.10e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  66 PIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGH 145
Cdd:COG0480   5 PLEKIRNIGIVAHIDAGKTTLTERILFYTGAIHRIGEVHDGNTVMDWMPEEQERGITITSAATTCEWKGHKINIIDTPGH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLP 225
Cdd:COG0480  85 VDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNKMDREGADFDRVLEQLKERLGANPVPLQLP 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 226 IGEAKTFKGVVDVVMKEKLLWncNSNDGKDFERKPLlemnDPELLKETTEARNALIEQVADLDDEFADLVLEEfsenfDL 305
Cdd:COG0480 165 IGAEDDFKGVIDLVTMKAYVY--DDELGAKYEEEEI----PAELKEEAEEAREELIEAVAETDDELMEKYLEG-----EE 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 306 LPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEER----------NYEFLQWYKDD--LCALAFK 373
Cdd:COG0480 234 LTEEEIKAGLRKATLAGKIVPVLCGSAFKNKGVQPLLDAVVDYLPSPLDVpaikgvdpdtGEEVERKPDDDepFSALVFK 313

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 374 VLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIvsskss 453
Cdd:COG0480 314 TMTDPFVGKLSFFRVYSGTLKSGSTVYNSTKGKKERIGRLLRMHGNKREEVDEAGAGDIVAVVKLKDTTTGDTL------ 387

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 25306283 454 alaaarraeregekkhrqNNEAERLLLAGVEIPEPVFFCTIEPPS 498
Cdd:COG0480 388 ------------------CDEDHPIVLEPIEFPEPVISVAIEPKT 414
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 72-352 7.85e-160

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: 454.64  E-value: 7.85e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:cd01886   1 NIGIIAHIDAGKTTTTERILYYTGRIHKIGEVHGGGATMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVDFTIE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKT 231
Cdd:cd01886  81 VERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRTGADFYRVVEQIREKLGANPVPLQLPIGAEDD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 232 FKGVVDVVMKEKLLWncNSNDGKDFERKPLlemnDPELLKETTEARNALIEQVADLDDEFADLVLEEFSenfdlLPAEKL 311
Cdd:cd01886 161 FEGVVDLIEMKALYW--DGELGEKIEETDI----PEDLLEEAEEAREELIETLAEVDDELMEKYLEGEE-----ITEEEI 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25306283 312 QTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP 352
Cdd:cd01886 230 KAAIRKGTIANKIVPVLCGSAFKNKGVQPLLDAVVDYLPSP 270
PRK13351 PRK13351
elongation factor G-like protein;
64-496 1.79e-150

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 445.94  E-value: 1.79e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   64 NPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTP 143
Cdd:PRK13351   2 EMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEVEDGTTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  144 GHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQ 223
Cdd:PRK13351  82 GHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRVGADLFKVLEDIEERFGKRPLPLQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  224 LPIGEAKTFKGVVDVVMKEKLLWNcNSNDGKDFERKPLLEmndpELLKETTEARNALIEQVADLDDEfadlVLEEFSENF 303
Cdd:PRK13351 162 LPIGSEDGFEGVVDLITEPELHFS-EGDGGSTVEEGPIPE----ELLEEVEEAREKLIEALAEFDDE----LLELYLEGE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  304 DlLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNyeFLQWYKDD-------------LCAL 370
Cdd:PRK13351 233 E-LSAEQLRAPLREGTRSGHLVPVLFGSALKNIGIEPLLDAVVDYLPSPLEVP--PPRGSKDNgkpvkvdpdpekpLLAL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  371 AFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSs 450
Cdd:PRK13351 310 VFKVQYDPYAGKLTYLRVYSGTLRAGSQLYNGTGGKREKVGRLFRLQGNKREEVDRAKAGDIVAVAGLKELETGDTLHD- 388

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 25306283  451 kssalaaarraeregekkhrqnnEAERLLLAGVEIPEPVFFCTIEP 496
Cdd:PRK13351 389 -----------------------SADPVLLELLTFPEPVVSLAVEP 411
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
76-496 1.41e-145

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 433.01  E-value: 1.41e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   76 MAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERC 155
Cdd:PRK12740   1 VGHSGAGKTTLTEAILFYTGAIHRIGEVEDGTTTMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  156 LRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGV 235
Cdd:PRK12740  81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDRAGADFFRVLAQLQEKLGAPVVPLQLPIGEGDDFTGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  236 VDVVMKEKLLWncnsNDGKDFERKPLlemnDPELLKETTEARNALIEQVADLDDEFADLVLEEFSenfdlLPAEKLQTAI 315
Cdd:PRK12740 161 VDLLSMKAYRY----DEGGPSEEIEI----PAELLDRAEEAREELLEALAEFDDELMEKYLEGEE-----LSEEEIKAGL 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  316 HRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDD----------LCALAFKVLHDKQRGPLVF 385
Cdd:PRK12740 228 RKATLAGEIVPVFCGSALKNKGVQRLLDAVVDYLPSPLEVPPVDGEDGEEGaelapdpdgpLVALVFKTMDDPFVGKLSL 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  386 MRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIvsskssalaaarraereg 465
Cdd:PRK12740 308 VRVYSGTLKKGDTLYNSGTGKKERVGRLYRMHGKQREEVDEAVAGDIVAVAKLKDAATGDTL------------------ 369

                        410       420       430
                 ....*....|....*....|....*....|.
gi 25306283  466 ekkhrqNNEAERLLLAGVEIPEPVFFCTIEP 496
Cdd:PRK12740 370 ------CDKGDPILLEPMEFPEPVISLAIEP 394
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
 66-502 4.21e-138

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 414.59  E-value: 4.21e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    66 PIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGH 145
Cdd:TIGR00484   6 DLNRFRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATMDWMEQEKERGITITSAATTVFWKGHRINIIDTPGH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLP 225
Cdd:TIGR00484  86 VDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMDKTGANFLRVVNQIKQRLGANAVPIQLP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   226 IGEAKTFKGVVDVVMKEKLLWncNSNDGKDFERKPLLEmndpELLKETTEARNALIEQVADLDDEFADLVLEEfsenfDL 305
Cdd:TIGR00484 166 IGAEDNFIGVIDLVEMKAYFF--NGDKGTKAIEKEIPS----DLLEQAKELRENLVEAVAEFDEELMEKYLEG-----EE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   306 LPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP----------EERNYEFLQWYKDDL--CALAFK 373
Cdd:TIGR00484 235 LTIEEIKNAIRKGVLNCEFFPVLCGSAFKNKGVQLLLDAVVDYLPSPtdvpaikgidPDTEKEIERKASDDEpfSALAFK 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   374 VLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVsskss 453
Cdd:TIGR00484 315 VATDPFVGQLTFVRVYSGVLKSGSYVKNSRKNKKERVGRLVKMHANNREEIKEVRAGDICAAIGLKDTTTGDTLC----- 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 25306283   454 alaaarraeregekkhrqnNEAERLLLAGVEIPEPVFFCTIEPPSLSKQ 502
Cdd:TIGR00484 390 -------------------DPKIDVILERMEFPEPVISLAVEPKTKADQ 419
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 72-352 7.17e-79

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


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 247.51  E-value: 7.17e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:cd04170   1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVEDGNTVSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKT 231
Cdd:cd04170  81 TLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDRARADFDKTLAALREAFGRPVVPIQLPIGEGDE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 232 FKGVVDVVMKEKLLWNcnsndgkdfERKPLLEMNDPELLKET-TEARNALIEQVADLDDEFADLVLEEfsenfDLLPAEK 310
Cdd:cd04170 161 FTGVVDLLSEKAYRYD---------PGEPSVEIEIPEELKEKvAEAREELLEAVAETDEELMEKYLEE-----GELTEEE 226

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 25306283 311 LQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP 352
Cdd:cd04170 227 LRAGLRRALRAGLIVPVFFGSALTGIGVRRLLDALVELAPSP 268
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 72-352 1.65e-67

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: 217.10  E-value: 1.65e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:cd04168   1 NIGILAHVDAGKTTLTESLLYTSGAIRELGSVDKGTTRTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQlpigeakt 231
Cdd:cd04168  81 VERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRAGADLEKVYQEIKEKLSPDIVPMQ-------- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 232 fkgvvDVVMKEKLLWNCNSNDgkdferkpllemndpellkettearnALIEQVADLDDEFADLVLEEfsenfDLLPAEKL 311
Cdd:cd04168 153 -----KVGLYPNICDTNNIDD--------------------------EQIETVAEGNDELLEKYLSG-----GPLEELEL 196

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 25306283 312 QTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP 352
Cdd:cd04168 197 DNELSARIQKASLFPVYHGSALKGIGIDELLEGITNLFPTS 237
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 69-351 2.51e-67

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: 214.70  E-value: 2.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    69 KIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTD-FMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVD 147
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGLdNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   148 FTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDK-TGASFKYAVESIREKLKAKplllqlpI 226
Cdd:pfam00009  82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRvDGAELEEVVEEVSRELLEK-------Y 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   227 GEAKTFkgvvdvvmkekllwncnsndgkdferkpllemndpellkettearnalieqvadlddefadlvleefsenfdll 306
Cdd:pfam00009 155 GEDGEF-------------------------------------------------------------------------- 160

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 25306283   307 paeklqtaihrvtlaqtaVPVLCGSALKNKGIQPLLDAVTMYLPS 351
Cdd:pfam00009 161 ------------------VPVVPGSALKGEGVQTLLDALDEYLPS 187
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
 71-352 2.26e-52

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


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 178.56  E-value: 2.26e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  71 RNIGIMAHIDAGKTTTTERILYYSG---------------YTRSlgdvddgdtvtDFMAQERERGITIQSAAVTFDWKGY 135
Cdd:cd04169   3 RTFAIISHPDAGKTTLTEKLLLFGGaiqeagavkarksrkHATS-----------DWMEIEKQRGISVTSSVMQFEYKGC 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 136 RVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKL 215
Cdd:cd04169  72 VINLLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDREGRDPLELLDEIENEL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 216 KAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNdGKDFERKPLLEMNDPELLKET-TEARNALIEQVadlddEFADL 294
Cdd:cd04169 152 GIDCAPMTWPIGMGKDFKGVYDRYDKEIYLYERGAG-GAIKAPEETKGLDDPKLDELLgEDLAEQLREEL-----ELVEG 225

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25306283 295 VLEEFS-ENFdllpaeklqtaihrvtLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSP 352
Cdd:cd04169 226 AGPEFDkELF----------------LAGELTPVFFGSALNNFGVQELLDAFVKLAPAP 268
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 72-216 5.77e-47

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: 161.31  E-value: 5.77e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGytRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:cd00881   1 NVGVIGHVDHGKTTLTGSLLYQTG--AIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25306283 152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGAS-FKYAVESIREKLK 216
Cdd:cd00881  79 TVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEdFDEVLREIKELLK 144
mtEFG2_II_like cd04092
Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic ...
 367-448 1.56e-43

Domain II of mitochondrial elongation factor G2-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG1s are not present in this group.


Pssm-ID: 293909 [Multi-domain]  Cd Length: 83  Bit Score: 148.62  E-value: 1.56e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 367 LCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDT 446
Cdd:cd04092   1 LCALAFKVIHDPQRGPLVFVRVYSGTLKAGSNVYNTTTGKKERISRLLKMHADQTEEVDSLSAGNIGVITGLKVTSTGDT 80


                ..
gi 25306283 447 IV 448
Cdd:cd04092  81 LV 82
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 70-448 3.82e-41

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 157.33  E-value: 3.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   70 IRNIGIMAHIDAGKTTTTERILYYSGYT------RSLGDVddgdtvtdFMAQERERGITIQSAAVT----FDWKGYRVNL 139
Cdd:PRK07560  20 IRNIGIIAHIDHGKTTLSDNLLAGAGMIseelagEQLALD--------FDEEEQARGITIKAANVSmvheYEGKEYLINL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  140 IDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTgasfkyavesIREklkakp 219
Cdd:PRK07560  92 IDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRL----------IKE------ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  220 llLQLPIGEaktfkgvvdvvMKEKLLwncnsndgkdferkpllemndpELLKETtearNALIEQVADlddefadlvlEEF 299
Cdd:PRK07560 156 --LKLTPQE-----------MQQRLL----------------------KIIKDV----NKLIKGMAP----------EEF 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  300 SENFdLLPAEKLQTAIhrvtlaqtavpvlcGSALKN----------KGIQ--------------------PL----LDAV 345
Cdd:PRK07560 187 KEKW-KVDVEDGTVAF--------------GSALYNwaisvpmmqkTGIKfkdiidyyekgkqkelaekaPLhevvLDMV 251

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  346 TMYLPSPEE-RNYEFLQWYKDDLCALAFK-VLHDKQRGPLVFM----------------RIYSGTIKPQLAIHNINGNCT 407
Cdd:PRK07560 252 VKHLPNPIEaQKYRIPKIWKGDLNSEVGKaMLNCDPNGPLVMMvtdiivdphagevatgRVFSGTLRKGQEVYLVGAKKK 331

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 25306283  408 ERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIV 448
Cdd:PRK07560 332 NRVQQVGIYMGPEREEVEEIPAGNIAAVTGLKDARAGETVV 372
prfC PRK00741
peptide chain release factor 3; Provisional
 67-447 4.02e-41

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 154.91  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   67 IAKIRNIGIMAHIDAGKTTTTERILYYSG---------------YTRSlgdvddgdtvtDFMAQERERGITIQSAAVTFD 131
Cdd:PRK00741   7 VAKRRTFAIISHPDAGKTTLTEKLLLFGGaiqeagtvkgrksgrHATS-----------DWMEMEKQRGISVTSSVMQFP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  132 WKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQT---LTVWRQadkHNIPRICFLNKMDKTGASFKYAV 208
Cdd:PRK00741  76 YRDCLINLLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTrklMEVCRL---RDTPIFTFINKLDRDGREPLELL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  209 ESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNcNSNDGKDFERKPLLEMNDPELlketteaRNALIEQVAD-L 287
Cdd:PRK00741 153 DEIEEVLGIACAPITWPIGMGKRFKGVYDLYNDEVELYQ-PGEGHTIQEVEIIKGLDNPEL-------DELLGEDLAEqL 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  288 DDEFaDLVlEEFSENFDLlpaEKLqtaihrvtLA--QTavPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYE--FLQWY 363
Cdd:PRK00741 225 REEL-ELV-QGASNEFDL---EAF--------LAgeLT--PVFFGSALNNFGVQEFLDAFVEWAPAPQPRQTDerEVEPT 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  364 KDDLCALAFKV---LHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFAD--QHVEipSLTAGNIaltVGL 438
Cdd:PRK00741 290 EEKFSGFVFKIqanMDPKHRDRIAFVRVCSGKFEKGMKVRHVRTGKDVRISNALTFMAQdrEHVE--EAYAGDI---IGL 364

                        410
                 ....*....|..
gi 25306283  439 KHTAT---GDTI 447
Cdd:PRK00741 365 HNHGTiqiGDTF 376
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 70-447 1.07e-37

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 147.35  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    70 IRNIGIMAHIDAGKTTTTERILYYSGYTRSlgDVDDGDTVTDFMAQERERGITIQSAAV----TFDWKGYRVNLIDTPGH 145
Cdd:TIGR00490  19 IRNIGIVAHIDHGKTTLSDNLLAGAGMISE--ELAGQQLYLDFDEQEQERGITINAANVsmvhEYEGNEYLINLIDTPGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKlkakplLLQLP 225
Cdd:TIGR00490  97 VDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQER------FIKII 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   226 IGEAKTFKGVVDVVMKEKllWNCNSNDGK--------------DFERKPLLEMNDpeLLKETTEARNALIEQVADLDDEF 291
Cdd:TIGR00490 171 TEVNKLIKAMAPEEFRDK--WKVRVEDGSvafgsayynwaisvPSMKKTGIGFKD--IYKYCKEDKQKELAKKSPLHQVV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   292 ADLVLEEFSEnfdllPAEklqtaihrvtlAQT-AVPVLCGSALKNKGIQPLLDAvtmylpSPEernyeflqwykDDLCAL 370
Cdd:TIGR00490 247 LDMVIRHLPS-----PIE-----------AQKyRIPVIWKGDLNSEVGKAMLNC------DPK-----------GPLALM 293

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25306283   371 AFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTI 447
Cdd:TIGR00490 294 ITKIVVDKHAGEVAVGRLYSGTIRPGMEVYIVDRKAKARIQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAVAGETI 370
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 71-199 6.44e-36

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: 133.13  E-value: 6.44e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  71 RNIGIMAHIDAGKTTTTERILYYSGYTRSlgDVDDGDTVTDFMAQERERGITIQSAAV---------TFDWKGYRVNLID 141
Cdd:cd01885   1 RNICIIAHVDHGKTTLSDSLLASAGIISE--KLAGKARYLDTREDEQERGITIKSSAIslyfeyeeeKMDGNDYLINLID 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 25306283 142 TPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDK 199
Cdd:cd01885  79 SPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDR 136
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 71-213 5.04e-35

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: 129.19  E-value: 5.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  71 RNIGIMAHIDAGKTTTTERILYYSGytrSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWK-----GYRVNLIDTPGH 145
Cdd:cd01890   1 RNFSIIAHIDHGKSTLADRLLELTG---TVSEREMKEQVLDSMDLERERGITIKAQAVRLFYKakdgeEYLLNLIDTPGH 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25306283 146 VDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIRE 213
Cdd:cd01890  78 VDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKIDLPAADPDRVKQEIED 145
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 69-211 6.58e-34

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: 126.55  E-value: 6.58e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  69 KIRNIGIMAHIDAGKTTTTERILYYSGYTRSlgDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDF 148
Cdd:cd01891   1 KIRNIAIIAHVDHGKTTLVDALLKQSGTFRE--NEEVGERVMDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADF 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25306283 149 TLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESI 211
Cdd:cd01891  79 GGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDRPDARPEEVVDEV 141
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
 68-447 4.38e-33

elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]


Pssm-ID: 130460 [Multi-domain]  Cd Length: 595  Bit Score: 132.83  E-value: 4.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    68 AKIRNIGIMAHIDAGKTTTTERILYYsgyTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWK-----GYRVNLIDT 142
Cdd:TIGR01393   1 KNIRNFSIIAHIDHGKSTLADRLLEY---TGAISEREMREQVLDSMDLERERGITIKAQAVRLNYKakdgeTYVLNLIDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   143 PGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDktgasfkyavesireklkakplll 222
Cdd:TIGR01393  78 PGHVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKID------------------------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   223 qLPIGeaktfkgvvdvvmkekllwncnsndgkdferkpllemnDPELLKETtearnalIEQVADLDDEFADLVleefsen 302
Cdd:TIGR01393 134 -LPSA--------------------------------------DPERVKKE-------IEEVIGLDASEAILA------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   303 fdllpaeklqtaihrvtlaqtavpvlcgSALKNKGIQPLLDAVTMYLPSPeernyeflqwyKDD----LCALAFKVLHDK 378
Cdd:TIGR01393 161 ----------------------------SAKTGIGIEEILEAIVKRVPPP-----------KGDpdapLKALIFDSHYDN 201

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25306283   379 QRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLpFADQHVEIPSLTAGNIA-LTVGLKH---TATGDTI 447
Cdd:TIGR01393 202 YRGVVALVRVFEGTIKPGDKIRFMSTGKEYEVDEVGV-FTPKLTKTDELSAGEVGyIIAGIKDvsdVRVGDTI 273
EFG_mtEFG_II cd04088
Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation ...
 367-447 7.25e-32

Domain II of bacterial elongation factor G and C-terminal domain of mitochondrial Elongation factors G1 and G2; This family represents the domain II of bacterial Elongation factor G (EF-G)and mitochondrial Elongation factors G1 (mtEFG1) and G2 (mtEFG2). During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homolog of mtEFG2, MEF2.


Pssm-ID: 293905 [Multi-domain]  Cd Length: 83  Bit Score: 117.24  E-value: 7.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 367 LCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDT 446
Cdd:cd04088   1 FSALVFKTMADPFVGKLTFFRVYSGTLKSGSTVYNSTKGKKERVGRLLRMHGKKREEVEELGAGDIGAVVGLKDTRTGDT 80


                .
gi 25306283 447 I 447
Cdd:cd04088  81 L 81
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 69-506 8.60e-32

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 128.98  E-value: 8.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  69 KIRNIGIMAHIDAGKTTTTERILYYSGytrslgdvddgdtvtDF-------------MAQERERGITIQSAAVTFDWKGY 135
Cdd:COG1217   5 DIRNIAIIAHVDHGKTTLVDALLKQSG---------------TFrenqevaervmdsNDLERERGITILAKNTAVRYKGV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 136 RVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGAsfkyavesirekl 215
Cdd:COG1217  70 KINIVDTPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTRFVLKKALELGLKPIVVINKIDRPDA------------- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 216 kakplllqlpigeaktfkgvvdvvmkekllwncnsndgkdferkpllemnDPEllkettEArnalIEQVADLddeFADLV 295
Cdd:COG1217 137 --------------------------------------------------RPD------EV----VDEVFDL---FIELG 153

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 296 LEEfsenfdllpaeklqtaihrvtlAQTAVPVLCGSAL----------KNKGIQPLLDAVTMYLPSPEERNYEFLQwykd 365
Cdd:COG1217 154 ATD----------------------EQLDFPVVYASARngwasldlddPGEDLTPLFDTILEHVPAPEVDPDGPLQ---- 207

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 366 dlcALAFKVLHDKQRGPLVFMRIYSGTIKP--QLAIHNINGNC-TERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTA 442
Cdd:COG1217 208 ---MLVTNLDYSDYVGRIAIGRIFRGTIKKgqQVALIKRDGKVeKGKITKLFGFEGLERVEVEEAEAGDIVAIAGIEDIN 284

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25306283 443 TGDTIvsskssalaaarraeregekkhrqnneaerlllAGVEIPEPVFFCTIEPPSLSKQPGIN 506
Cdd:COG1217 285 IGDTI---------------------------------CDPENPEALPPIKIDEPTLSMTFSVN 315
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
 66-198 6.77e-31

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 126.29  E-value: 6.77e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  66 PIAKIRNIGIMAHIDAGKTTTTERILYYSG--YTRSlgdvddgdtvtdFMAQ-------ERERGITIQSAAVTFDWKG-- 134
Cdd:COG0481   2 DQKNIRNFSIIAHIDHGKSTLADRLLELTGtlSERE------------MKEQvldsmdlERERGITIKAQAVRLNYKAkd 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 135 ---YRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHN---IPricFLNKMD 198
Cdd:COG0481  70 getYQLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDleiIP---VINKID 136
PTZ00416 PTZ00416
elongation factor 2; Provisional
 70-437 8.16e-28

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 117.84  E-value: 8.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   70 IRNIGIMAHIDAGKTTTTERILYYSGYTRSlgdvdDGDTVTDFM---AQERERGITIQSAAVT--FDW--------KGYR 136
Cdd:PTZ00416  19 IRNMSVIAHVDHGKSTLTDSLVCKAGIISS-----KNAGDARFTdtrADEQERGITIKSTGISlyYEHdledgddkQPFL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  137 VNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREK-- 214
Cdd:PTZ00416  94 INLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDRAILELQLDPEEIYQNfv 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  215 --------------------LKAKPLLLQLPIGE----------------AKTFKGVVDVVMKEklLWNCNSNDGKDFER 258
Cdd:PTZ00416 174 ktienvnviiatyndelmgdVQVYPEKGTVAFGSglqgwaftlttfariyAKKFGVEESKMMER--LWGDNFFDAKTKKW 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  259 KPLLEMNDPEllkettEARNALIEQVADLDDEFADLVLEEfsenfDLLPAEKLQTAIHrVTLAQTAVPvLCGSALKNKGI 338
Cdd:PTZ00416 252 IKDETNAQGK------KLKRAFCQFILDPICQLFDAVMNE-----DKEKYDKMLKSLN-ISLTGEDKE-LTGKPLLKAVM 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  339 Q---PLLDA----VTMYLPSPEE-RNYEFLQWYK---DDLCALAFKVLHDKqrGPLV-----------------FMRIYS 390
Cdd:PTZ00416 319 QkwlPAADTllemIVDHLPSPKEaQKYRVENLYEgpmDDEAANAIRNCDPN--GPLMmyiskmvptsdkgrfyaFGRVFS 396

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25306283  391 GTI-----------------KPQLAIHNINgncterisRLLLPFADQHVEIPSLTAGNIALTVG 437
Cdd:PTZ00416 397 GTVatgqkvriqgpnyvpgkKEDLFEKNIQ--------RTVLMMGRYVEQIEDVPCGNTVGLVG 452
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 70-239 6.65e-26

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 103.61  E-value: 6.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    70 IRNIGIMAHIDAGKTTTTERIL--------YYSGYTRSLGdvddgdtvtdfMAQERERGITiqsaavtfdwkgYRVNLID 141
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLgnkgsiteYYPGTTRNYV-----------TTVIEEDGKT------------YKFNLLD 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   142 TPGHVDF-------TLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKhNIPRICFLNKMDKTGASFKYAVESIREK 214
Cdd:TIGR00231  58 TAGQEDYdairrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHADS-GVPIILVGNKIDLKDADLKTHVASEFAK 136

                         170       180
                  ....*....|....*....|....*
gi 25306283   215 LKAKPLLLQlpigEAKTFKGVVDVV 239
Cdd:TIGR00231 137 LNGEPIIPL----SAETGKNIDSAF 157
PRK10218 PRK10218
translational GTPase TypA;
67-235 1.42e-24

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 107.49  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   67 IAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMaqERERGITIQSAAVTFDWKGYRVNLIDTPGHV 146
Cdd:PRK10218   2 IEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDL--EKERGITILAKNTAIKWNDYRINIVDTPGHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  147 DFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIRE---KLKAKPLLLQ 223
Cdd:PRK10218  80 DFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDlfvNLDATDEQLD 159

                        170
                 ....*....|..
gi 25306283  224 LPIGEAKTFKGV 235
Cdd:PRK10218 160 FPIVYASALNGI 171
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 56-199 9.15e-23

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 102.49  E-value: 9.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   56 IKSLHSIINPPiAKIRNIGIMAHIDAGKTTTTERILYYSGY-------------TRslgdvddgdtvtdfmAQERERGIT 122
Cdd:PLN00116   6 AEELRRIMDKK-HNIRNMSVIAHVDHGKSTLTDSLVAAAGIiaqevagdvrmtdTR---------------ADEAERGIT 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  123 IQSAAVTF----------------DWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKH 186
Cdd:PLN00116  70 IKSTGISLyyemtdeslkdfkgerDGNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGE 149

                        170
                 ....*....|...
gi 25306283  187 NIPRICFLNKMDK 199
Cdd:PLN00116 150 RIRPVLTVNKMDR 162
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 71-199 2.99e-20

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: 89.25  E-value: 2.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  71 RNIGIMAHIDAGKTTTTERILYYS-GYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTF-----DWKGYRVNLIDTPG 144
Cdd:cd04167   1 RNVCIAGHLHHGKTSLLDMLIEQThKRTPSVKLGWKPLRYTDTRKDEQERGISIKSNPISLvledsKGKSYLINIIDTPG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 25306283 145 HVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDK 199
Cdd:cd04167  81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDR 135
infB CHL00189
translation initiation factor 2; Provisional
 55-215 1.17e-14

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 76.79  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   55 DIKSLHSIINPPIakirnIGIMAHIDAGKTTTTERIlyysgytrslgdvddgdtVTDFMAQERERGITIQSAA--VTFDW 132
Cdd:CHL00189 234 SAFTENSINRPPI-----VTILGHVDHGKTTLLDKI------------------RKTQIAQKEAGGITQKIGAyeVEFEY 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  133 KGYRVNLI--DTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASfkyaVES 210
Cdd:CHL00189 291 KDENQKIVflDTPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANAN----TER 366


                 ....*
gi 25306283  211 IREKL 215
Cdd:CHL00189 367 IKQQL 371
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 72-217 2.19e-12

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: 68.81  E-value: 2.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGYT-----RSLGDVDDGDTVTDF--------MAQERERGITIQSAAVTFDWKGYRVN 138
Cdd:COG5256   9 NLVVIGHVDHGKSTLVGRLLYETGAIdehiiEKYEEEAEKKGKESFkfawvmdrLKEERERGVTIDLAHKKFETDKYYFT 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 139 LIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTltvwRQ----ADKHNIPR-ICFLNKMDKTGAS---FKYAVES 210
Cdd:COG5256  89 IIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQT----REhaflARTLGINQlIVAVNKMDAVNYSekrYEEVKEE 164


                ....*..
gi 25306283 211 IREKLKA 217
Cdd:COG5256 165 VSKLLKM 171
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 72-216 3.27e-11

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 65.33  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERILYYSGYT-----RSLGDVDDGDTVTDF--------MAQERERGITIQSAAVTFDWKGYRVN 138
Cdd:PRK12317   8 NLAVIGHVDHGKSTLVGRLLYETGAIdehiiEELREEAKEKGKESFkfawvmdrLKEERERGVTIDLAHKKFETDKYYFT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  139 LIDTPGHVDFTLEVERCLRVLDGAVAVFDA--SAGVEAQTltvwRQ----ADKHNIPR-ICFLNKMDKTGAS---FKYAV 208
Cdd:PRK12317  88 IVDCPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQT----REhvflARTLGINQlIVAINKMDAVNYDekrYEEVK 163


                 ....*...
gi 25306283  209 ESIREKLK 216
Cdd:PRK12317 164 EEVSKLLK 171
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 75-217 3.84e-11

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: 61.72  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  75 IMAHIDAGKTTTTERIlyysgytRSLGDvddgdtvtdfmaQERE-RGITIQSAA--VTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:cd01887   5 VMGHVDHGKTTLLDKI-------RKTNV------------AAGEaGGITQHIGAyqVPIDVKIPGITFIDTPGHEAFTNM 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25306283 152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTgasfkYAVESIREKLKA 217
Cdd:cd01887  66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKP-----YGTEADPERVKN 126
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 72-205 9.63e-11

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: 61.74  E-value: 9.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYSGY-----TRSLGDVDDGDTVTDF--------MAQERERGITIQSAAVTFDWKGYRVN 138
Cdd:cd01883   1 NLVVIGHVDAGKSTLTGHLLYKLGGvdkrtIEKYEKEAKEMGKESFkyawvldkLKEERERGVTIDVGLAKFETEKYRFT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 139 LIDTPGHVDF-------TLEVERCLRVLDGAVAVFDASAGVEAQT---------LTVwRQAdkhniprICFLNKMDKTGA 202
Cdd:cd01883  81 IIDAPGHRDFvknmitgASQADVAVLVVSARKGEFEAGFEKGGQTrehallartLGV-KQL-------IVAVNKMDDVTV 152


                ...
gi 25306283 203 SFK 205
Cdd:cd01883 153 NWS 155
mtEFG1_II_like cd04091
Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic ...
 367-448 3.29e-10

Domain II of mitochondrial elongation factor G1-like proteins found in eukaryotes; Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s); mtEFG2s are not present in this group.


Pssm-ID: 293908 [Multi-domain]  Cd Length: 81  Bit Score: 56.53  E-value: 3.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 367 LCALAFKvLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKhTATGDT 446
Cdd:cd04091   1 FVGLAFK-LEEGRFGQLTYMRVYQGVLRKGDTIYNVRTGKKVRVPRLVRMHSDEMEDIEEVYAGDICALFGID-CASGDT 78


                ..
gi 25306283 447 IV 448
Cdd:cd04091  79 FT 80
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 72-198 5.14e-10

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: 61.33  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    72 NIGIMAHIDAGKTTTTERIlyysgyTRSLGDVDDGDTVT----DFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVD 147
Cdd:TIGR00485  14 NVGTIGHVDHGKTTLTAAI------TTVLAKEGGAAARAydqiDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHAD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25306283   148 FTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRI-CFLNKMD 198
Cdd:TIGR00485  88 YVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIvVFLNKCD 139
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 72-233 5.30e-10

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


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 61.81  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283    72 NIGIMAHIDAGKTTTTERIlyysgytrslgdvddGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE 151
Cdd:TIGR00475   2 IIATAGHVDHGKTTLLKAL---------------TGIAADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISN 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   152 VERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPR-ICFLNKMDKTGASFKYAVESIREKLKAKPLLLQlpigEAK 230
Cdd:TIGR00475  67 AIAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVNEEEIKRTEMFMKQILNSYIFLK----NAK 142


                  ...
gi 25306283   231 TFK 233
Cdd:TIGR00475 143 IFK 145
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 74-241 1.44e-09

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 57.08  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  74 GIMAHIDAGKTTTTERILYysgytrslgdvddgdtvTDFMAQERERGIT--IQSAAVTFDWKGYRVNLIDTPGHVDF--- 148
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLG-----------------GEVGEVSDVPGTTrdPDVYVKELDKGKVKLVLVDTPGLDEFggl 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 149 --TLEVERCLRVLDGAVAVFDAS--AGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASfkyaVESIREKLKAKPLLLQL 224
Cdd:cd00882  64 grEELARLLLRGADLILLVVDSTdrESEEDAKLLILRRLRKEGIPIILVGNKIDLLEER----EVEELLRLEELAKILGV 139

                       170
                ....*....|....*....
gi 25306283 225 PIGE--AKTFKGVVDVVMK 241
Cdd:cd00882 140 PVFEvsAKTGEGVDELFEK 158
PLN03127 PLN03127
Elongation factor Tu; Provisional
 72-198 2.11e-09

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 59.45  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERI---LYYSGYTRSLGDVDDGDTvtdfmAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDF 148
Cdd:PLN03127  63 NVGTIGHVDHGKTTLTAAItkvLAEEGKAKAVAFDEIDKA-----PEEKARGITIATAHVEYETAKRHYAHVDCPGHADY 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 25306283  149 TLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRI-CFLNKMD 198
Cdd:PLN03127 138 VKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLvVFLNKVD 188
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 72-207 5.30e-09

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 58.18  E-value: 5.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERILYYSG-----YTRSLGDVDDGDTVTDF--------MAQERERGITIQSAAVTFDWKGYRVN 138
Cdd:PLN00043   9 NIVVIGHVDSGKSTTTGHLIYKLGgidkrVIERFEKEAAEMNKRSFkyawvldkLKAERERGITIDIALWKFETTKYYCT 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25306283  139 LIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNI--------PRICFLNKMDKTGASFKYA 207
Cdd:PLN00043  89 VIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALlaftlgvkQMICCCNKMDATTPKYSKA 165
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 72-205 5.99e-09

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 58.22  E-value: 5.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERILYYSG-----YTRSLGDVDDGDTVTDF--------MAQERERGITIQSAAVTFDWKGYRVN 138
Cdd:PTZ00141   9 NLVVIGHVDSGKSTTTGHLIYKCGgidkrTIEKFEKEAAEMGKGSFkyawvldkLKAERERGITIDIALWKFETPKYYFT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  139 LIDTPGHVDF-------TLEVERCLRVLDGAVAVFDASAGVEAQ---------TLTVwRQAdkhniprICFLNKMDKTGA 202
Cdd:PTZ00141  89 IIDAPGHRDFiknmitgTSQADVAILVVASTAGEFEAGISKDGQtrehallafTLGV-KQM-------IVCINKMDDKTV 160


                 ...
gi 25306283  203 SFK 205
Cdd:PTZ00141 161 NYS 163
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 72-198 7.97e-09

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: 55.67  E-value: 7.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERILYYS---GYTRSLGDVDDGDTVtdfmaQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDF 148
Cdd:cd01884   4 NVGTIGHVDHGKTTLTAAITKVLakkGGAKAKKYDEIDKAP-----EEKARGITINTAHVEYETANRHYAHVDCPGHADY 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25306283 149 tleverclrV---------LDGAVAVFDASAGVEAQT---LTVWRQAdkhNIPRI-CFLNKMD 198
Cdd:cd01884  79 ---------IknmitgaaqMDGAILVVSATDGPMPQTrehLLLARQV---GVPYIvVFLNKAD 129
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 120-216 9.30e-09

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 54.75  E-value: 9.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 120 GITIQSAAVTFDWKGYRVNLIDTPG-----HVDFTLE---VERCLRVLDGA---VAVFDASAGVEAQTLTVWRQADKHNI 188
Cdd:cd01895  35 GTTRDSIDVPFEYDGQKYTLIDTAGirkkgKVTEGIEkysVLRTLKAIERAdvvLLVLDASEGITEQDLRIAGLILEEGK 114

                        90       100       110
                ....*....|....*....|....*....|.
gi 25306283 189 PRICFLNKMD---KTGASFKYAVESIREKLK 216
Cdd:cd01895 115 ALIIVVNKWDlveKDEKTMKEFEKELRRKLP 145
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 72-198 9.80e-09

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: 57.47  E-value: 9.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTERIlyysgyTRSLgdvdDGDTVTDFMA--------QERERGITIQSAAVTFDWKGYRVNLIDTP 143
Cdd:COG0050  14 NIGTIGHVDHGKTTLTAAI------TKVL----AKKGGAKAKAydqidkapEEKERGITINTSHVEYETEKRHYAHVDCP 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25306283 144 GHVDFtleverclrV---------LDGAVAVFDASAGVEAQT---LTVWRQAdkhNIPRI-CFLNKMD 198
Cdd:COG0050  84 GHADY---------VknmitgaaqMDGAILVVSATDGPMPQTrehILLARQV---GVPYIvVFLNKCD 139
Tet_II cd03690
Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain ...
 364-447 1.12e-08

Domain II of ribosomal protection proteins Tet(M) and Tet(O); This subfamily represents domain II of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to domain II of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.


Pssm-ID: 293891 [Multi-domain]  Cd Length: 86  Bit Score: 52.24  E-value: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 364 KDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTAT 443
Cdd:cd03690   1 ESELSGTVFKIEYDPKGERLAYLRLYSGTLRLRDSVRVSGEEEKIKITELRTFENGELVKVDRVYAGDIAILVGLKSLRV 80


                ....
gi 25306283 444 GDTI 447
Cdd:cd03690  81 GDVL 84
PLN03126 PLN03126
Elongation factor Tu; Provisional
 72-199 2.78e-08

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 56.16  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTerilyySGYTRSLGDVDDGDTVT----DFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVD 147
Cdd:PLN03126  83 NIGTIGHVDHGKTTLT------AALTMALASMGGSAPKKydeiDAAPEERARGITINTATVEYETENRHYAHVDCPGHAD 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 25306283  148 FTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPR-ICFLNKMDK 199
Cdd:PLN03126 157 YVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNmVVFLNKQDQ 209
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 72-249 4.48e-08

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 53.14  E-value: 4.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  72 NIGIMAHIDAGKTTTTeRILYYSGYTRSLGDVDdgdtvtdfmaQERERGITI---------QSAAVTFDWKG-----YRV 137
Cdd:cd01889   2 NVGLLGHVDSGKTSLA-KALSEIASTAAFDKNP----------QSQERGITLdlgfssfevDKPKHLEDNENpqienYQI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 138 NLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKT-GASFKYAVESIREKLK 216
Cdd:cd01889  71 TLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIpEEERKRKIEKMKKRLQ 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 25306283 217 ---AKPLLLQLPIGE--AKT---FKGVVDVVMKEKLLWNCN 249
Cdd:cd01889 151 ktlEKTRLKDSPIIPvsAKPgegEAELGGELKNLIVLPLIN 191
PRK12736 PRK12736
elongation factor Tu; Reviewed
 72-198 7.70e-08

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 54.57  E-value: 7.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERIlyysgyTRSLgdvdDGDTVTDFMA--------QERERGITIQSAAVTFDWKGYRVNLIDTP 143
Cdd:PRK12736  14 NIGTIGHVDHGKTTLTAAI------TKVL----AERGLNQAKDydsidaapEEKERGITINTAHVEYETEKRHYAHVDCP 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 25306283  144 GHVDFTLEVERCLRVLDGAVAVFDASAGVEAQT---LTVWRQAdkhNIPRI-CFLNKMD 198
Cdd:PRK12736  84 GHADYVKNMITGAAQMDGAILVVAATDGPMPQTrehILLARQV---GVPYLvVFLNKVD 139
PRK00049 PRK00049
elongation factor Tu; Reviewed
 72-198 7.81e-08

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 54.42  E-value: 7.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERIlyysgyTRSLgdvdDGDTVTDFMA--------QERERGITIQSAAVTFDWKGYRVNLIDTP 143
Cdd:PRK00049  14 NVGTIGHVDHGKTTLTAAI------TKVL----AKKGGAEAKAydqidkapEEKARGITINTAHVEYETEKRHYAHVDCP 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25306283  144 GHVDFtleverclrV---------LDGAVAVFDASAGVEAQT---LTVWRQAdkhNIPRI-CFLNKMD 198
Cdd:PRK00049  84 GHADY---------VknmitgaaqMDGAILVVSAADGPMPQTrehILLARQV---GVPYIvVFLNKCD 139
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 381-448 9.69e-08

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: 49.19  E-value: 9.69e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25306283   381 GPLVFMRIYSGTIKP-----QLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIV 448
Cdd:pfam03144   1 GTVATGRVESGTLKKgdkvrILPNGTGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PRK12735 PRK12735
elongation factor Tu; Reviewed
 72-198 1.22e-07

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 53.69  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERIlyysgyTRSLgdvdDGDTVTDFMA--------QERERGITIQSAAVTFDWKGYRVNLIDTP 143
Cdd:PRK12735  14 NVGTIGHVDHGKTTLTAAI------TKVL----AKKGGGEAKAydqidnapEEKARGITINTSHVEYETANRHYAHVDCP 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 25306283  144 GHVDFTLEVERCLRVLDGAVAVFDASAGVEAQT---LTVWRQAdkhNIPRI-CFLNKMD 198
Cdd:PRK12735  84 GHADYVKNMITGAAQMDGAILVVSAADGPMPQTrehILLARQV---GVPYIvVFLNKCD 139
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 367-448 7.58e-07

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: 46.87  E-value: 7.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 367 LCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLlpfaDQHVEIPSLTAG-NIALTV-GLKHTATG 444
Cdd:cd01342   1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIE----RFHEEVDEAKAGdIVGIGIlGVKDILTG 76


                ....
gi 25306283 445 DTIV 448
Cdd:cd01342  77 DTLT 80
tufA CHL00071
elongation factor Tu
 72-199 9.38e-07

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 51.11  E-value: 9.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   72 NIGIMAHIDAGKTTTTERI-----LYYSGYTRSLGDVDDGDtvtdfmaQERERGITIQSAAVTFDWKGYRVNLIDTPGHV 146
Cdd:CHL00071  14 NIGTIGHVDHGKTTLTAAItmtlaAKGGAKAKKYDEIDSAP-------EEKARGITINTAHVEYETENRHYAHVDCPGHA 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 25306283  147 DFTLEVERCLRVLDGAVAVFDASAGVEAQT---LTVWRQADKHNIprICFLNKMDK 199
Cdd:CHL00071  87 DYVKNMITGAAQMDGAILVVSAADGPMPQTkehILLAKQVGVPNI--VVFLNKEDQ 140
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
120-216 1.71e-06

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 50.41  E-value: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 120 GITIQSAAVTFDWKGYRVNLIDTPG-----HVDFTLE---VERCLRVLDGA-VAVF--DASAGVEAQTLTVWRQADKHNI 188
Cdd:COG1160 208 GTTRDSIDTPFERDGKKYTLIDTAGirrkgKVDEGIEkysVLRTLRAIERAdVVLLviDATEGITEQDLKIAGLALEAGK 287

                        90       100       110
                ....*....|....*....|....*....|.
gi 25306283 189 PRICFLNKMD---KTGASFKYAVESIREKLK 216
Cdd:COG1160 288 ALVIVVNKWDlveKDRKTREELEKEIRRRLP 318
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 73-220 1.84e-06

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: 47.99  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  73 IGIMAHIDAGKTTTTERIlyySGY-TRSLgdvddgdtvtdfmAQERERGITIQ-SAAVTFDWKGYRVNLIDTPGHVDFTL 150
Cdd:cd04171   2 IGTAGHIDHGKTTLIKAL---TGIeTDRL-------------PEEKKRGITIDlGFAYLDLPDGKRLGFIDVPGHEKFVK 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25306283 151 EVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPR-ICFLNKMDKTGASFKYAVES-IREKLKAKPL 220
Cdd:cd04171  66 NMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKgLVVLTKADLVDEDRLELVEEeILELLAGTFL 137
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 115-216 6.16e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 48.51  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283  115 QER-----ERGITIQSAAVTFDWKGYRVNLIDTPG-----HVDFTLE---VERCLRVLDGA---VAVFDASAGVEAQTLT 178
Cdd:PRK00093 196 EERvivsdIAGTTRDSIDTPFERDGQKYTLIDTAGirrkgKVTEGVEkysVIRTLKAIERAdvvLLVIDATEGITEQDLR 275

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 25306283  179 VWRQADKHNIPRICFLNKMDK-TGASFKYAVESIREKLK 216
Cdd:PRK00093 276 IAGLALEAGRALVIVVNKWDLvDEKTMEEFKKELRRRLP 314
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 120-196 1.13e-05

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 44.53  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283   120 GITIQSAAVTFDWKGYRVNLIDTPGHVDFT----------LEVERClrvlDGAVAVFDASAGVEAQTLTVWRQADKHNIP 189
Cdd:pfam01926  31 GTTRDPNEGRLELKGKQIILVDTPGLIEGAsegeglgrafLAIIEA----DLILFVVDSEEGITPLDEELLELLRENKKP 106


                  ....*..
gi 25306283   190 RICFLNK 196
Cdd:pfam01926 107 IILVLNK 113
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 116-198 1.41e-04

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: 42.94  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 116 ERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICF-L 194
Cdd:cd04166  59 EREQGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVaV 138


                ....
gi 25306283 195 NKMD 198
Cdd:cd04166 139 NKMD 142
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 116-198 1.85e-04

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: 43.92  E-value: 1.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 116 ERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTleveR--------ClrvlDGAVAVFDASAGVEAQTLtvwrqadKH- 186
Cdd:COG2895  76 EREQGITIDVAYRYFSTPKRKFIIADTPGHEQYT----RnmvtgastA----DLAILLIDARKGVLEQTR-------RHs 140

                        90
                ....*....|....*....
gi 25306283 187 ------NIPRICFL-NKMD 198
Cdd:COG2895 141 yiasllGIRHVVVAvNKMD 159
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 381-447 2.62e-03

Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 37.17  E-value: 2.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 381 GPLVFMRIYSGTIKP--QLAIHNINGNCTE-RISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTI 447
Cdd:cd03691  15 GRIAIGRIFSGTVKVgqQVTVVDEDGKIEKgRVTKLFGFEGLERVEVEEAEAGDIVAIAGLEDITIGDTI 84
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
120-246 7.08e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 37.65  E-value: 7.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25306283 120 GITIQSAAVTFDWKGYRVNLIDTPGHVDFTLE---VERCLRVLDGAVAVFDASAGVEAQTLTVW----RQADKhNIPRIC 192
Cdd:COG1100  38 GVTIDKKELKLDGLDVDLVIWDTPGQDEFRETrqfYARQLTGASLYLFVVDGTREETLQSLYELleslRRLGK-KSPIIL 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25306283 193 FLNKMDktgasfKYAVESIREKLKAKPLLLQLPIGE-----AKTFKGVVDVV--MKEKLLW 246
Cdd:COG1100 117 VLNKID------LYDEEEIEDEERLKEALSEDNIVEvvatsAKTGEGVEELFaaLAEILRG 171
 
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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