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Conserved domains on  [gi|1958770998|ref|XP_038964094|]
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selenocysteine-specific elongation factor isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eSelB_III cd04094
Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain ...
 86-226 5.04e-46

Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain III of archaeal and eukaryotic selenocysteine (Sec)-specific eukaryotic elongation factor (eEFSec or eSelB), which is homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.


:

Pssm-ID: 294009  Cd Length: 114  Bit Score: 153.24  E-value: 5.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998  86 TVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRMLFFSPAPDNFDSEPVLDSFDlsreylfqeqylckdsmpTATE 165
Cdd:cd04094     1 TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFV------------------EDED 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958770998 166 GNDEADTkagnspeghCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGVL 226
Cdd:cd04094    63 ESLEEAK---------PGSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV 114
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 1-81 5.93e-40

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: 136.50  E-value: 5.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:cd03696     3 LPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFVLS 82


                  .
gi 1958770998  81 P 81
Cdd:cd03696    83 E 83
 
Name Accession Description Interval E-value
eSelB_III cd04094
Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain ...
 86-226 5.04e-46

Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain III of archaeal and eukaryotic selenocysteine (Sec)-specific eukaryotic elongation factor (eEFSec or eSelB), which is homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.


Pssm-ID: 294009  Cd Length: 114  Bit Score: 153.24  E-value: 5.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998  86 TVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRMLFFSPAPDNFDSEPVLDSFDlsreylfqeqylckdsmpTATE 165
Cdd:cd04094     1 TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFV------------------EDED 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958770998 166 GNDEADTkagnspeghCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGVL 226
Cdd:cd04094    63 ESLEEAK---------PGSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV 114
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 1-81 5.93e-40

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: 136.50  E-value: 5.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:cd03696     3 LPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFVLS 82


                  .
gi 1958770998  81 P 81
Cdd:cd03696    83 E 83
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-126 1.26e-23

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: 102.30  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEI-PALKVVkKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERG-LV 78
Cdd:COG3276   179 LPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELlPSGKPV-RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGdVL 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958770998  79 CAPESLHTVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRMLFF 126
Cdd:COG3276   258 AAPGALRPTDRIDVRLRLLPSAPRPLKHWQRVHLHHGTAEVLARVVLL 305
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-120 5.36e-17

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: 82.23  E-value: 5.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERG-LVC 79
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGlLIL 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958770998  80 APESlHTVHAALISVEKIPYFRG-PLQTKAKFHITVGHETVM 120
Cdd:TIGR00475 259 TPED-PKLRVVVKFIAEVPLLELqPYHIAHGMSVTTGKISLL 299
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-86 1.17e-12

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 68.43  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:PRK12736  213 MPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKtvVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQV 292

                          90
                  ....*....|.
gi 1958770998  79 -CAPESL--HT 86
Cdd:PRK12736  293 lAKPGSIkpHT 303
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 13-80 8.13e-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: 48.80  E-value: 8.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958770998  13 GTVMTGTILSGTISLGDSVEIPALKVVKK-----VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
 
Name Accession Description Interval E-value
eSelB_III cd04094
Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain ...
 86-226 5.04e-46

Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain III of archaeal and eukaryotic selenocysteine (Sec)-specific eukaryotic elongation factor (eEFSec or eSelB), which is homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.


Pssm-ID: 294009  Cd Length: 114  Bit Score: 153.24  E-value: 5.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998  86 TVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRMLFFSPAPDNFDSEPVLDSFDlsreylfqeqylckdsmpTATE 165
Cdd:cd04094     1 TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFV------------------EDED 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958770998 166 GNDEADTkagnspeghCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGVL 226
Cdd:cd04094    63 ESLEEAK---------PGSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV 114
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 1-81 5.93e-40

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: 136.50  E-value: 5.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:cd03696     3 LPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFVLS 82


                  .
gi 1958770998  81 P 81
Cdd:cd03696    83 E 83
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-126 1.26e-23

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: 102.30  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEI-PALKVVkKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERG-LV 78
Cdd:COG3276   179 LPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELlPSGKPV-RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGdVL 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958770998  79 CAPESLHTVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRMLFF 126
Cdd:COG3276   258 AAPGALRPTDRIDVRLRLLPSAPRPLKHWQRVHLHHGTAEVLARVVLL 305
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-120 5.36e-17

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: 82.23  E-value: 5.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERG-LVC 79
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGlLIL 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958770998  80 APESlHTVHAALISVEKIPYFRG-PLQTKAKFHITVGHETVM 120
Cdd:TIGR00475 259 TPED-PKLRVVVKFIAEVPLLELqPYHIAHGMSVTTGKISLL 299
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 1-81 4.44e-15

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 69.85  E-value: 4.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVK--SMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTvtGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82


                  ....
gi 1958770998  79 -CAP 81
Cdd:cd03697    83 lAKP 86
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-86 1.17e-12

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 68.43  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:PRK12736  213 MPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKtvVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQV 292

                          90
                  ....*....|.
gi 1958770998  79 -CAPESL--HT 86
Cdd:PRK12736  293 lAKPGSIkpHT 303
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 1-78 3.71e-12

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


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 61.47  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVK----KVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERG 76
Cdd:cd03694     3 FQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfrpvTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKG 82


                  ..
gi 1958770998  77 LV 78
Cdd:cd03694    83 MV 84
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-86 9.58e-12

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: 65.56  E-value: 9.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:COG0050   215 MPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKtvVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQV 294

                          90
                  ....*....|.
gi 1958770998  79 -CAPESL--HT 86
Cdd:COG0050   295 lAKPGSItpHT 305
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-102 7.99e-11

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 63.10  E-value: 7.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:PLN03126  292 LAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSttVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMV 371

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958770998  79 CA-PESL--HTVHAALISVEK-------IPYFRG 102
Cdd:PLN03126  372 LAkPGSItpHTKFEAIVYVLKkeeggrhSPFFAG 405
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-102 1.48e-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: 62.10  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:TIGR00485 213 LPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKttVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMV 292

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958770998  79 -CAPESL--HTVHAALISVEK-------IPYFRG 102
Cdd:TIGR00485 293 lAKPGSIkpHTKFEAEVYVLSkeeggrhTPFFSG 326
tufA CHL00071
elongation factor Tu
 1-86 2.00e-10

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 61.90  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVK--KVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:CHL00071  223 MAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETKttTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMV 302

                          90
                  ....*....|.
gi 1958770998  79 CA-PESL--HT 86
Cdd:CHL00071  303 LAkPGTItpHT 313
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-86 5.42e-10

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 60.20  E-value: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:PRK00049  215 MPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKttVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQV 294

                          90
                  ....*....|.
gi 1958770998  79 -CAPESL--HT 86
Cdd:PRK00049  295 lAKPGSItpHT 305
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 1-79 7.08e-10

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: 55.27  E-value: 7.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVC 79
Cdd:cd03693     7 LPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGDVA 85
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 7-81 1.26e-09

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: 59.18  E-value: 1.26e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958770998   7 FSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCAP 81
Cdd:COG5256   233 YSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGH 307
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 1-80 1.41e-09

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: 54.19  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTqfDPKLLERGLVCA 80
Cdd:cd01342     3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGIL--GVKDILTGDTLT 80
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-86 2.33e-09

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 58.31  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKK--VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLV 78
Cdd:PRK12735  215 MPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKttVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQV 294

                          90
                  ....*....|.
gi 1958770998  79 -CAPESL--HT 86
Cdd:PRK12735  295 lAKPGSIkpHT 305
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-86 4.20e-09

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 57.91  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKS----MQMFHTPVTSAMQGDRLGICVTQFDPKLLERG 76
Cdd:PLN03127  264 MPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPGGPLKTtvtgVEMFKKILDQGQAGDNVGLLLRGLKREDVQRG 343

                          90
                  ....*....|.
gi 1958770998  77 LV-CAPESLHT 86
Cdd:PLN03127  344 QViCKPGSIKT 354
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 7-81 6.06e-09

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 57.24  E-value: 6.06e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958770998   7 FSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCAP 81
Cdd:PRK12317  234 YSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGH 308
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 13-80 8.13e-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: 48.80  E-value: 8.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958770998  13 GTVMTGTILSGTISLGDSVEIPALKVVKK-----VKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 7-80 1.07e-06

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 50.13  E-value: 1.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958770998   7 FSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:PTZ00141  242 YKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAS 315
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-63 1.97e-06

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 49.66  E-value: 1.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGI 63
Cdd:PRK10512  177 LAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIAL 239
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 7-80 7.56e-04

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 41.23  E-value: 7.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958770998   7 FSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDPKLLERGLVCA 80
Cdd:PLN00043  242 YKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAS 315
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 13-63 2.15e-03

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 36.50  E-value: 2.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958770998  13 GTVMTGTILSGTISLGDSVEIPALkvVKKVKSMQMFHTPVTSAMQGDRLGI 63
Cdd:cd16265    14 RQVLTGEVESGVIYVGYKVKGDKG--VALIRAIEREHRKVDFAVAGDEVAL 62
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 18-64 3.88e-03

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: 36.00  E-value: 3.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958770998  18 GTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGIC 64
Cdd:cd03695    20 GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLT 66
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 1-70 9.16e-03

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: 34.80  E-value: 9.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770998   1 MSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKVVKKVKSMQMFHTPVTSAMQGDRLGICVTQFDP 70
Cdd:cd16267     4 LSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDP 73
 
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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