NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2702100883|ref|WP_337892086|]
View 

EF-Tu/IF-2/RF-3 family GTPase, partial [Leeuwenhoekiella blandensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CysN super family cl34513
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-201 6.73e-105

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


The actual alignment was detected with superfamily member COG2895:

Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 308.17  E-value: 6.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   1 DHNMVDCRFPVQNVIRPFsdefHDYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:COG2895   227 DRNDAPFRFPVQYVNRPN----LDFRGYAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEDE 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 IDISRGDMIVREHNQPEPKQDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRQEEyGTVGMNDII 160
Cdd:COG2895   303 IDISRGDVIVAADAPPEVADQFEATLVWMDEEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAA-DSLELNDIG 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2702100883 161 RVKMRTTKPLLVDEYNQNKGTGSFILIDESTNETVAAGMVI 201
Cdd:COG2895   382 RVTLRLAEPIAFDPYADNRATGSFILIDRLTNATVGAGMIR 422
 
Name Accession Description Interval E-value
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-201 6.73e-105

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: 308.17  E-value: 6.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   1 DHNMVDCRFPVQNVIRPFsdefHDYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:COG2895   227 DRNDAPFRFPVQYVNRPN----LDFRGYAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEDE 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 IDISRGDMIVREHNQPEPKQDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRQEEyGTVGMNDII 160
Cdd:COG2895   303 IDISRGDVIVAADAPPEVADQFEATLVWMDEEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAA-DSLELNDIG 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2702100883 161 RVKMRTTKPLLVDEYNQNKGTGSFILIDESTNETVAAGMVI 201
Cdd:COG2895   382 RVTLRLAEPIAFDPYADNRATGSFILIDRLTNATVGAGMIR 422
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-201 1.37e-86

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 267.18  E-value: 1.37e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   1 DHNMVDCRFPVQNVIRPFSDefhdYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:PRK05506  236 DRNLKDFRFPVQYVNRPNLD----FRGFAGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 IDISRGDMIVREHNQPEPKQDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRqEEYGTVGMNDII 160
Cdd:PRK05506  312 IDISRGDMLARADNRPEVADQFDATVVWMAEEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLER-LAAKTLELNEIG 390

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2702100883 161 RVKMRTTKPLLVDEYNQNKGTGSFILIDESTNETVAAGMVI 201
Cdd:PRK05506  391 RCNLSTDAPIAFDPYARNRTTGSFILIDRLTNATVGAGMID 431
CysN_NoDQ_III cd04095
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ...
 100-200 6.30e-48

Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N- and C-termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 294010 [Multi-domain]  Cd Length: 103  Bit Score: 152.20  E-value: 6.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883 100 QDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRQEEyGTVGMNDIIRVKMRTTKPLLVDEYNQNK 179
Cdd:cd04095     4 DQFEATLVWMDEKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLEREPA-DTLALNDIGRVTLRLAEPLAFDPYAENR 82

                          90       100
                  ....*....|....*....|.
gi 2702100883 180 GTGSFILIDESTNETVAAGMV 200
Cdd:cd04095    83 ATGSFILIDRLTNATVAAGMI 103
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 30-87 1.37e-05

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: 41.48  E-value: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2702100883  30 GRVTSGIFKKGDEVMVLP-----SGFKSKIQSIVLGEEELEEAFP--PQSVTINLEDDIDISRGD 87
Cdd:pfam03144   6 GRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAgdNAGLILAGVGLEDIRVGD 70
 
Name Accession Description Interval E-value
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-201 6.73e-105

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: 308.17  E-value: 6.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   1 DHNMVDCRFPVQNVIRPFsdefHDYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:COG2895   227 DRNDAPFRFPVQYVNRPN----LDFRGYAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLEDE 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 IDISRGDMIVREHNQPEPKQDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRQEEyGTVGMNDII 160
Cdd:COG2895   303 IDISRGDVIVAADAPPEVADQFEATLVWMDEEPLLPGRKYLLKHGTRTVRATVTAIKYRIDVNTLEHEAA-DSLELNDIG 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2702100883 161 RVKMRTTKPLLVDEYNQNKGTGSFILIDESTNETVAAGMVI 201
Cdd:COG2895   382 RVTLRLAEPIAFDPYADNRATGSFILIDRLTNATVGAGMIR 422
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-201 1.37e-86

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 267.18  E-value: 1.37e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   1 DHNMVDCRFPVQNVIRPFSDefhdYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:PRK05506  236 DRNLKDFRFPVQYVNRPNLD----FRGFAGTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLADE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 IDISRGDMIVREHNQPEPKQDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRqEEYGTVGMNDII 160
Cdd:PRK05506  312 IDISRGDMLARADNRPEVADQFDATVVWMAEEPLLPGRPYLLKHGTRTVPASVAAIKYRVDVNTLER-LAAKTLELNEIG 390

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2702100883 161 RVKMRTTKPLLVDEYNQNKGTGSFILIDESTNETVAAGMVI 201
Cdd:PRK05506  391 RCNLSTDAPIAFDPYARNRTTGSFILIDRLTNATVGAGMID 431
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-201 1.16e-72

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 227.10  E-value: 1.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   1 DHNMVDCRFPVQNVIRPfsDEfhDYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:PRK05124  240 VVDAQPFRFPVQYVNRP--NL--DFRGYAGTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 IDISRGDMIVREHNQPEPKQDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTL-HRQEEygTVGMNDI 159
Cdd:PRK05124  316 IDISRGDLLVAADEALQAVQHASADVVWMAEQPLQPGQSYDIKIAGKKTRARVDAIRYQVDINTLtQREAE--NLPLNGI 393

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2702100883 160 IRVKMRTTKPLLVDEYNQNKGTGSFILIDESTNETVAAGMVI 201
Cdd:PRK05124  394 GLVELTFDEPLVLDPYQQNRVTGGFIFIDRLTNVTVGAGMVR 435
CysN_NoDQ_III cd04095
Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of ...
 100-200 6.30e-48

Domain III of the large subunit of ATP sulfurylase (ATPS); This model represents domain III of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and is homologous to domain III of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD and CysN. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N- and C-termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 294010 [Multi-domain]  Cd Length: 103  Bit Score: 152.20  E-value: 6.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883 100 QDIEAMLCWMNNDKMSPRAKYAIKHTSVEARAMIKEVLYKVDINTLHRQEEyGTVGMNDIIRVKMRTTKPLLVDEYNQNK 179
Cdd:cd04095     4 DQFEATLVWMDEKPLQPGRRYLLKHGTRTVRARVTEIDYRIDVNTLEREPA-DTLALNDIGRVTLRLAEPLAFDPYAENR 82

                          90       100
                  ....*....|....*....|.
gi 2702100883 180 GTGSFILIDESTNETVAAGMV 200
Cdd:cd04095    83 ATGSFILIDRLTNATVAAGMI 103
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 8-91 9.36e-38

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 125.37  E-value: 9.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   8 RFPVQNVIRPFSDefhdYRGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDDIDISRGD 87
Cdd:cd03695     2 RFPVQYVNRPNLD----FRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDEIDVSRGD 77


                  ....
gi 2702100883  88 MIVR 91
Cdd:cd03695    78 LIVR 81
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 30-90 2.94e-13

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


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 62.28  E-value: 2.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2702100883  30 GRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDDIDISRGDMIV 90
Cdd:cd01342    20 GRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVKDILTGDTLT 80
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 30-201 3.18e-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: 64.18  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  30 GRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLE--DDIDISRGDMIVREHNQPEPKQDIEAMLC 107
Cdd:COG5256   244 GRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRgvEKNDIKRGDVAGHPDNPPTVAEEFTAQIV 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883 108 WMNNDKmsprakyAIK---------HTSVEArAMIKEVLYKVDINTLHRQEEYGT-VGMNDIIRVKMRTTKPLLVDEYNQ 177
Cdd:COG5256   324 VLQHPS-------AITvgytpvfhvHTAQVA-CTFVELVSKLDPRTGQVKEENPQfLKTGDAAIVKIKPTKPLVIEKFKE 395

                         170       180
                  ....*....|....*....|....
gi 2702100883 178 NKGTGSFILIDesTNETVAAGMVI 201
Cdd:COG5256   396 FPQLGRFAIRD--MGQTVAAGVVL 417
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 30-201 1.19e-11

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 62.64  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  30 GRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLE--DDIDISRGDMIVREHNQPEPKQDIEAMLC 107
Cdd:PRK12317  245 GRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRgvGKKDIKRGDVCGHPDNPPTVAEEFTAQIV 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883 108 WMNNDKmsprakyAIK---------HTSVEArAMIKEVLYKVDINTLHRQEEYGT-VGMNDIIRVKMRTTKPLLVDEYNQ 177
Cdd:PRK12317  325 VLQHPS-------AITvgytpvfhaHTAQVA-CTFEELVKKLDPRTGQVAEENPQfIKTGDAAIVKIKPTKPLVIEKVKE 396

                         170       180
                  ....*....|....*....|....
gi 2702100883 178 NKGTGSFILIDesTNETVAAGMVI 201
Cdd:PRK12317  397 IPQLGRFAIRD--MGQTIAAGMVI 418
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 8-200 3.26e-10

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 58.61  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   8 RFPVQNVIR-------PfsdefhdyrgyAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDD 80
Cdd:PTZ00141  235 RLPLQDVYKiggigtvP-----------VGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNV 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  81 I--DISRGDMIVREHNQPePK--QDIEAMLCWMNNDKmSPRAKYAIK---HTSVEArAMIKEVLYKVDINTLHRQEEY-G 152
Cdd:PTZ00141  304 SvkDIKRGYVASDSKNDP-AKecADFTAQVIVLNHPG-QIKNGYTPVldcHTAHIA-CKFAEIESKIDRRSGKVLEENpK 380

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2702100883 153 TVGMNDIIRVKMRTTKPLLVDEYNQNKGTGSFILIDesTNETVAAGMV 200
Cdd:PTZ00141  381 AIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRD--MKQTVAVGVI 426
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 30-200 1.23e-08

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 53.94  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  30 GRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLEDDI--DISRGDMIVREHNQP-EPKQDIEAML 106
Cdd:PLN00043  253 GRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAvkDLKRGYVASNSKDDPaKEAANFTSQV 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883 107 CWMNN-----DKMSPRAKYAIKHTSVEaramIKEVLYKVDINT---LHRQEEY---GTVGMndiirVKMRTTKPLLVDEY 175
Cdd:PLN00043  333 IIMNHpgqigNGYAPVLDCHTSHIAVK----FAEILTKIDRRSgkeLEKEPKFlknGDAGF-----VKMIPTKPMVVETF 403

                         170       180
                  ....*....|....*....|....*
gi 2702100883 176 NQNKGTGSFILIDesTNETVAAGMV 200
Cdd:PLN00043  404 SEYPPLGRFAVRD--MRQTVAVGVI 426
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 30-201 8.15e-08

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 51.45  E-value: 8.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883  30 GRVTSGIFKKGDEVMVLPSGFKSKIQSI-VLGEEElEEAFPPQSVTINL---EDDiDISRGDMIVREHNqPEPKQDIEAM 105
Cdd:COG3276   196 GTLLSGTVRVGDELELLPSGKPVRVRGIqVHGQPV-EEAYAGQRVALNLagvEKE-EIERGDVLAAPGA-LRPTDRIDVR 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883 106 LcwmnndKMSPRAKYAIKH---------TS-VEARAmikeVLYkvDINTLHRQEEYgtvgmndiiRVKMRTTKPLLVdEY 175
Cdd:COG3276   273 L------RLLPSAPRPLKHwqrvhlhhgTAeVLARV----VLL--DREELAPGEEA---------LAQLRLEEPLVA-AR 330

                         170       180
                  ....*....|....*....|....*.
gi 2702100883 176 NQnkgtgSFILIDESTNETVAAGMVI 201
Cdd:COG3276   331 GD-----RFILRDYSPRRTIGGGRVL 351
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 28-89 1.98e-07

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 47.18  E-value: 1.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2702100883  28 YAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLE--DDIDISRGDMI 89
Cdd:cd03693    22 PVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKgvSVKDIKRGDVA 85
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 30-89 2.10e-07

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 46.75  E-value: 2.10e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2702100883  30 GRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINL--EDDIDISRGDMI 89
Cdd:cd03696    20 GTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLtgVDAKELERGFVL 81
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 17-89 5.74e-07

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 45.55  E-value: 5.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2702100883  17 PFSDEFHDYRGYA-GRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINL---EDDiDISRGDMI 89
Cdd:cd04089     5 PILDKYKDMGTVVmGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLkgvEEE-DISPGFVL 80
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 8-89 4.14e-06

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


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 43.27  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2702100883   8 RFPVQNVIRPFSDEFhdyrGYAGRVTSGIFKKGDEVMVLPSGFKSKIQSIVLGEEELEEAFPPQSVTINLE--DDIDISR 85
Cdd:cd16267     3 RLSVSDVFKGQGSGF----TVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTgiDPNHLRV 78


                  ....
gi 2702100883  86 GDMI 89
Cdd:cd16267    79 GSIL 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 30-87 1.37e-05

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: 41.48  E-value: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2702100883  30 GRVTSGIFKKGDEVMVLP-----SGFKSKIQSIVLGEEELEEAFP--PQSVTINLEDDIDISRGD 87
Cdd:pfam03144   6 GRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAgdNAGLILAGVGLEDIRVGD 70
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 124-200 6.58e-04

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 37.76  E-value: 6.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2702100883 124 HTSVEArAMIKEVLYKVDINTLhRQEEYGTVGMNDIIRVKMRTTKPLLVDEYNQNKGTGSFILIDESTneTVAAGMV 200
Cdd:cd01513    30 GTAHVP-GRIAKLLSKEDGKTK-EKKPPDSLQPGENGTVEVELQKPVVLERGKEFPTLGRFALRDGGR--TVGAGLI 102
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 162-200 5.00e-03

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 35.25  E-value: 5.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2702100883 162 VKMRTTKPLLVDEYNQNKGTGSFILIDesTNETVAAGMV 200
Cdd:cd03705    68 VKMVPTKPLCVETFSEYPPLGRFAVRD--MRQTVAVGVI 104
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH