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Conserved domains on  [gi|2462496731|ref|XP_054188357|]
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selenocysteine-specific elongation factor isoform X11 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 42-149 2.88e-47

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


The actual alignment was detected with superfamily member cd01889:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 192  Bit Score: 162.92  E-value: 2.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENTKFRGAPI 121
Cdd:cd01889    84 TIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKTRLKDSPI 163

                          90       100
                  ....*....|....*....|....*...
gi 2462496731 122 IPVAAKPGGPEApetEAPQGIPELIELL 149
Cdd:cd01889   164 IPVSAKPGEGEA---ELGGELKNLIVLP 188
eSelB_III cd04094
Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain ...
 251-390 9.52e-47

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: 158.63  E-value: 9.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 251 TVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRLMFFSPAPDNFDQEPILDSFNfsqeylfqeqylskdltpavtd 330
Cdd:cd04094     1 TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFV---------------------- 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 331 ndeaDKKAGQATEGHCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGIL 390
Cdd:cd04094    59 ----EDEDESLEEAKPGSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV 114
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 164-246 1.80e-39

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: 138.04  E-value: 1.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 164 FLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV 243
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80


                  ...
gi 2462496731 244 CAP 246
Cdd:cd03696    81 LSE 83
 
Name Accession Description Interval E-value
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 42-149 2.88e-47

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: 162.92  E-value: 2.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENTKFRGAPI 121
Cdd:cd01889    84 TIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKTRLKDSPI 163

                          90       100
                  ....*....|....*....|....*...
gi 2462496731 122 IPVAAKPGGPEApetEAPQGIPELIELL 149
Cdd:cd01889   164 IPVSAKPGEGEA---ELGGELKNLIVLP 188
eSelB_III cd04094
Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain ...
 251-390 9.52e-47

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: 158.63  E-value: 9.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 251 TVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRLMFFSPAPDNFDQEPILDSFNfsqeylfqeqylskdltpavtd 330
Cdd:cd04094     1 TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFV---------------------- 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 331 ndeaDKKAGQATEGHCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGIL 390
Cdd:cd04094    59 ----EDEDESLEEAKPGSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV 114
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 42-291 2.50e-42

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: 160.08  E-value: 2.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIgqiaCQ-----KLVVVLNKIDLLPEgkrqAAIDKMTKKMQKTLENTKF 116
Cdd:COG3276    67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAI----LDllgikRGIVVLTKADLVDE----EWLELVEEEIRELLAGTFL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 117 RGAPIIPVAAKPGgpeapeteapQGIPELIELLTSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDS 195
Cdd:COG3276   139 EDAPIVPVSAVTG----------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 196 VEI-PALKVVkKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERG-LVCAPESLHTVHAALISVEKIPYFRGPLQTKA 273
Cdd:COG3276   209 LELlPSGKPV-RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGdVLAAPGALRPTDRIDVRLRLLPSAPRPLKHWQ 287

                         250
                  ....*....|....*...
gi 2462496731 274 KFHITVGHETVMGRLMFF 291
Cdd:COG3276   288 RVHLHHGTAEVLARVVLL 305
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 164-246 1.80e-39

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: 138.04  E-value: 1.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 164 FLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV 243
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80


                  ...
gi 2462496731 244 CAP 246
Cdd:cd03696    81 LSE 83
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 42-288 2.15e-28

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: 119.21  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECL-VIGQIACQKLVVVLNKIDLLPEgkrqAAIDKMTKKMQKTLENTKF-RGA 119
Cdd:TIGR00475  66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADRVNE----EEIKRTEMFMKQILNSYIFlKNA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 120 PIIPVAAKPGgpeapeteapQGIPELIELLTSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEI 198
Cdd:TIGR00475 142 KIFKTSAKTG----------QGIGELKKELKNLLeSLDIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 199 PALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLvCAPESLHTVHAalISVEKIPYFrgPLQTKAKFHIT 278
Cdd:TIGR00475 212 LPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGL-LILTPEDPKLR--VVVKFIAEV--PLLELQPYHIA 286

                         250
                  ....*....|
gi 2462496731 279 VGHETVMGRL 288
Cdd:TIGR00475 287 HGMSVTTGKI 296
PRK12736 PRK12736
elongation factor Tu; Reviewed
 46-251 8.60e-24

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 103.49  E-value: 8.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLL--PEgkrqaAIDKMTKKMQKTLENTKFRG--AP 120
Cdd:PRK12736   95 GAAQMDGAILVVAATDGPMPQTREhILLARQVGVPYLVVFLNKVDLVddEE-----LLELVEMEVRELLSEYDFPGddIP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 121 IIPVAAKpggpEAPETEAPQ--GIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEI 198
Cdd:PRK12736  170 VIRGSAL----KALEGDPKWedAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEI 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462496731 199 PALKVVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESL--HT 251
Cdd:PRK12736  246 VGIKETQKtvVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVlAKPGSIkpHT 303
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 178-245 1.26e-06

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: 46.10  E-value: 1.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462496731 178 GTVMTGTILSGSISLGDSVEIPALKVVKK-----VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCA 245
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 46-153 7.30e-06

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: 46.75  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQ--KLVVVLNKIDLLPEGKRQAAIDKMTKK-MQKTLENTKFRgaPII 122
Cdd:pfam00009  89 GLAQADGAILVVDAVEGVMPQTRE--HLRLARQLgvPIIVFINKMDRVDGAELEEVVEEVSRElLEKYGEDGEFV--PVV 164

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462496731 123 PVAAKPGgpeapeteapQGIPELIELLTSQI 153
Cdd:pfam00009 165 PGSALKG----------EGVQTLLDALDEYL 185
 
Name Accession Description Interval E-value
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 42-149 2.88e-47

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: 162.92  E-value: 2.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENTKFRGAPI 121
Cdd:cd01889    84 TIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKTRLKDSPI 163

                          90       100
                  ....*....|....*....|....*...
gi 2462496731 122 IPVAAKPGGPEApetEAPQGIPELIELL 149
Cdd:cd01889   164 IPVSAKPGEGEA---ELGGELKNLIVLP 188
eSelB_III cd04094
Domain III of eukaryotic and archaeal elongation factor SelB; This model represents the domain ...
 251-390 9.52e-47

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: 158.63  E-value: 9.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 251 TVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRLMFFSPAPDNFDQEPILDSFNfsqeylfqeqylskdltpavtd 330
Cdd:cd04094     1 TVTAAIALVCKISFFKGSIKSKSKFHITVGHQTVMARVTFFSDPGKDETEEDESAEFV---------------------- 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 331 ndeaDKKAGQATEGHCPRQQWALVEFEKPVTCPRLCLVIGSRLDADIHTNTCRLAFHGIL 390
Cdd:cd04094    59 ----EDEDESLEEAKPGSEQYALLEFEKPVAAPPGDLFIGSRLDTDPHSNTCRLAFYGRV 114
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 42-291 2.50e-42

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: 160.08  E-value: 2.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIgqiaCQ-----KLVVVLNKIDLLPEgkrqAAIDKMTKKMQKTLENTKF 116
Cdd:COG3276    67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAI----LDllgikRGIVVLTKADLVDE----EWLELVEEEIRELLAGTFL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 117 RGAPIIPVAAKPGgpeapeteapQGIPELIELLTSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDS 195
Cdd:COG3276   139 EDAPIVPVSAVTG----------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 196 VEI-PALKVVkKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERG-LVCAPESLHTVHAALISVEKIPYFRGPLQTKA 273
Cdd:COG3276   209 LELlPSGKPV-RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGdVLAAPGALRPTDRIDVRLRLLPSAPRPLKHWQ 287

                         250
                  ....*....|....*...
gi 2462496731 274 KFHITVGHETVMGRLMFF 291
Cdd:COG3276   288 RVHLHHGTAEVLARVVLL 305
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 164-246 1.80e-39

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: 138.04  E-value: 1.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 164 FLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV 243
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80


                  ...
gi 2462496731 244 CAP 246
Cdd:cd03696    81 LSE 83
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 42-288 2.15e-28

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: 119.21  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECL-VIGQIACQKLVVVLNKIDLLPEgkrqAAIDKMTKKMQKTLENTKF-RGA 119
Cdd:TIGR00475  66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADRVNE----EEIKRTEMFMKQILNSYIFlKNA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 120 PIIPVAAKPGgpeapeteapQGIPELIELLTSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEI 198
Cdd:TIGR00475 142 KIFKTSAKTG----------QGIGELKKELKNLLeSLDIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 199 PALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLvCAPESLHTVHAalISVEKIPYFrgPLQTKAKFHIT 278
Cdd:TIGR00475 212 LPINHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGL-LILTPEDPKLR--VVVKFIAEV--PLLELQPYHIA 286

                         250
                  ....*....|
gi 2462496731 279 VGHETVMGRL 288
Cdd:TIGR00475 287 HGMSVTTGKI 296
PRK12736 PRK12736
elongation factor Tu; Reviewed
 46-251 8.60e-24

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 103.49  E-value: 8.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLL--PEgkrqaAIDKMTKKMQKTLENTKFRG--AP 120
Cdd:PRK12736   95 GAAQMDGAILVVAATDGPMPQTREhILLARQVGVPYLVVFLNKVDLVddEE-----LLELVEMEVRELLSEYDFPGddIP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 121 IIPVAAKpggpEAPETEAPQ--GIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEI 198
Cdd:PRK12736  170 VIRGSAL----KALEGDPKWedAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEI 245

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462496731 199 PALKVVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESL--HT 251
Cdd:PRK12736  246 VGIKETQKtvVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVlAKPGSIkpHT 303
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 46-251 3.16e-22

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: 98.68  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLL--PEgkrqaAIDKMTKKMQKTLENTKFRG--AP 120
Cdd:COG0050    95 GAAQMDGAILVVSATDGPMPQTREHILLArQVGVPYIVVFLNKCDMVddEE-----LLELVEMEVRELLSKYGFPGddTP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 121 IIPVAAKPG--GPEAPETEAPqgIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEI 198
Cdd:COG0050   170 IIRGSALKAleGDPDPEWEKK--ILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEI 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462496731 199 PALKVVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESL--HT 251
Cdd:COG0050   248 VGIRDTQKtvVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVlAKPGSItpHT 305
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 46-267 5.79e-22

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: 97.93  E-value: 5.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLLPEgkrQAAIDKMTKKMQKTLENTKFRG--APII 122
Cdd:TIGR00485  95 GAAQMDGAILVVSATDGPMPQTREHILLArQVGVPYIVVFLNKCDMVDD---EELLELVEMEVRELLSQYDFPGddTPII 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 123 PVAAKPGGPEAPETEAPqgIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALK 202
Cdd:TIGR00485 172 RGSALKALEGDAEWEAK--ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496731 203 VVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESL--HTVHAALISVEK-------IPYFRG 267
Cdd:TIGR00485 250 DTRKttVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVlAKPGSIkpHTKFEAEVYVLSkeeggrhTPFFSG 326
tufA CHL00071
elongation factor Tu
 46-251 4.33e-20

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 92.33  E-value: 4.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLLPEGKrqaAIDKMTKKMQKTLENTKFRGA--PII 122
Cdd:CHL00071   95 GAAQMDGAILVVSAADGPMPQTKEHILLAkQVGVPNIVVFLNKEDQVDDEE---LLELVELEVRELLSKYDFPGDdiPIV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 123 PVAA-------------KPGgpeapETEAPQGIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGS 189
Cdd:CHL00071  172 SGSAllalealtenpkiKRG-----ENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGT 246

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496731 190 ISLGDSVEIPALKVVK--KVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCA-PESL--HT 251
Cdd:CHL00071  247 VKVGDTVEIVGLRETKttTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAkPGTItpHT 313
PRK12735 PRK12735
elongation factor Tu; Reviewed
 46-251 9.65e-20

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 91.44  E-value: 9.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLL--PEgkrqaAIDKMTKKMQKTLENTKFRG--AP 120
Cdd:PRK12735   95 GAAQMDGAILVVSAADGPMPQTREhILLARQVGVPYIVVFLNKCDMVddEE-----LLELVEMEVRELLSKYDFPGddTP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 121 IIPVAAKPG--GPEAPETEAPqgIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEI 198
Cdd:PRK12735  170 IIRGSALKAleGDDDEEWEAK--ILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEI 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462496731 199 PALKVVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESL--HT 251
Cdd:PRK12735  248 VGIKETQKttVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVlAKPGSIkpHT 305
PRK00049 PRK00049
elongation factor Tu; Reviewed
 46-251 1.09e-19

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.02  E-value: 1.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLL--PEgkrqaAIDKMTKKMQKTLENTKFRG--AP 120
Cdd:PRK00049   95 GAAQMDGAILVVSAADGPMPQTREhILLARQVGVPYIVVFLNKCDMVddEE-----LLELVEMEVRELLSKYDFPGddTP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 121 IIPVAAKP---GGPEAPETEApqgIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVE 197
Cdd:PRK00049  170 IIRGSALKaleGDDDEEWEKK---ILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVE 246

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462496731 198 IPALKVVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESL--HT 251
Cdd:PRK00049  247 IVGIRDTQKttVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVlAKPGSItpHT 305
PLN03126 PLN03126
Elongation factor Tu; Provisional
 43-267 4.15e-19

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 90.06  E-value: 4.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  43 VLKGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMqktLENTKFRG--A 119
Cdd:PLN03126  161 MITGAAQMDGAILVVSGADGPMPQTKEhILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVREL---LSSYEFPGddI 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 120 PIIP------VAAKPGGPEAP--ETEAPQGIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSIS 191
Cdd:PLN03126  238 PIISgsallaLEALMENPNIKrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVK 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 192 LGDSVEIPALKVVKK--VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCA-PESL--HTVHAALISVEK----- 261
Cdd:PLN03126  318 VGETVDIVGLRETRSttVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAkPGSItpHTKFEAIVYVLKkeegg 397


                  ....*...
gi 2462496731 262 --IPYFRG 267
Cdd:PLN03126  398 rhSPFFAG 405
PLN03127 PLN03127
Elongation factor Tu; Provisional
 46-251 4.54e-19

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 89.88  E-value: 4.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLPEgkrQAAIDKMTKKMQKTLENTKFRG--APII 122
Cdd:PLN03127  144 GAAQMDGGILVVSAPDGPMPQTKEhILLARQVGVPSLVVFLNKVDVVDD---EELLELVEMELRELLSFYKFPGdeIPII 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 123 PVAAKPGGPEAPETEAPQGIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALK 202
Cdd:PLN03127  221 RGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLR 300

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462496731 203 VVKKVKS----MQMFHMPITSAMQGDRLGICVTQFDPKLLERGLV-CAPESLHT 251
Cdd:PLN03127  301 PGGPLKTtvtgVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQViCKPGSIKT 354
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 42-237 1.42e-16

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 81.82  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGM-QTQSAECLV-IGQIACQKLVVVLNKIDLLPegkRQAAIDKMtKKMQKTLENTKFRGA 119
Cdd:PRK04000  101 TMLSGAALMDGAILVIAANEPCpQPQTKEHLMaLDIIGIKNIVIVQNKIDLVS---KERALENY-EQIKEFVKGTVAENA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 120 PIIPVAAKpggpeapeteapQG--IPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGT--------VMTGTILSGS 189
Cdd:PRK04000  177 PIIPVSAL------------HKvnIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGV 244

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 190 ISLGDSVEI-PALKVVKKVKS-MQMFHMPITSAMQGDR----------LGIcVTQFDPKL 237
Cdd:PRK04000  245 LKVGDEIEIrPGIKVEEGGKTkWEPITTKIVSLRAGGEkveearpgglVGV-GTKLDPSL 303
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 164-246 7.24e-16

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 72.55  E-value: 7.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 164 FLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVK--SMQMFHMPITSAMQGDRLGICVTQFDPKLLERG 241
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTvtGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                  ....*.
gi 2462496731 242 LV-CAP 246
Cdd:cd03697    81 MVlAKP 86
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 46-246 3.10e-15

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: 77.67  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAE------CLVIGQIacqklVVVLNKIDLLP-EGKRQAAIDKMTKKMQKTLeNTKFRG 118
Cdd:COG5256   105 GASQADAAILVVSAKDGVMGQTREhaflarTLGINQL-----IVAVNKMDAVNySEKRYEEVKEEVSKLLKMV-GYKVDK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 119 APIIPVAAKPGG---PEAPETEAPQGiPELIELLtSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDS 195
Cdd:COG5256   179 IPFIPVSAWKGDnvvKKSDNMPWYNG-PTLLEAL-DNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDK 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462496731 196 VEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCAP 246
Cdd:COG5256   257 VVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGH 307
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 44-228 6.03e-15

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 77.78  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  44 LKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIA-CQKLVVVLNKIDLLPEGKrqaaIDKMTKKMQKTLENTKFRGAPII 122
Cdd:PRK10512   69 LAGVGGIDHALLVVACDDGVMAQTREHLAILQLTgNPMLTVALTKADRVDEAR----IAEVRRQVKAVLREYGFAEAKLF 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 123 PVAAKPGgpeapeteapQGIPELIELLtSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALK 202
Cdd:PRK10512  145 VTAATEG----------RGIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN 213

                         170       180
                  ....*....|....*....|....*.
gi 2462496731 203 VVKKVKSMQMFHMPITSAMQGDRLGI 228
Cdd:PRK10512  214 KPMRVRGLHAQNQPTEQAQAGQRIAL 239
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 164-243 5.91e-13

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: 64.55  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 164 FLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVK----KVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLE 239
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfrpvTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                  ....
gi 2462496731 240 RGLV 243
Cdd:cd03694    81 KGMV 84
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 46-246 1.75e-12

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 69.18  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGM----QTQS----AECLVIGQiacqkLVVVLNKIDLLP-EGKRQAAIDKMTKKMQKTLeNTKF 116
Cdd:PRK12317  104 GASQADAAVLVVAADDAGgvmpQTREhvflARTLGINQ-----LIVAINKMDAVNyDEKRYEEVKEEVSKLLKMV-GYKP 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 117 RGAPIIPVAAKPGG---PEAPETEAPQGiPELIELLtSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLG 193
Cdd:PRK12317  178 DDIPFIPVSAFEGDnvvKKSENMPWYNG-PTLLEAL-DNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVG 255

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462496731 194 DSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCAP 246
Cdd:PRK12317  256 DKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGH 308
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 42-198 5.65e-11

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 64.64  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGM-QTQSAECLVIGQIACQKLVVVL-NKIDLLpegKRQAAIDKMtKKMQKTLENTKFRGA 119
Cdd:PTZ00327  133 TMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILqNKIDLV---KEAQAQDQY-EEIRNFVKGTIADNA 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 120 PIIPVAAKPGgpeapeteapQGIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKG--------QGTVMTGTILSGSIS 191
Cdd:PTZ00327  209 PIIPISAQLK----------YNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFDVNKpgedienlKGGVAGGSILQGVLK 278


                  ....*..
gi 2462496731 192 LGDSVEI 198
Cdd:PTZ00327  279 VGDEIEI 285
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 43-245 2.98e-10

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 62.41  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  43 VLKGAQIIDLMMLVIDVTKG-------MQTQSAE-CLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENT 114
Cdd:PLN00043  102 MITGTSQADCAVLIIDSTTGgfeagisKDGQTREhALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKV 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 115 KFR--GAPIIPVAAKPGG---PEAPETEAPQGiPELIELLtSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGS 189
Cdd:PLN00043  182 GYNpdKIPFVPISGFEGDnmiERSTNLDWYKG-PTLLEAL-DQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGV 259

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496731 190 ISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCA 245
Cdd:PLN00043  260 IKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAS 315
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 162-244 1.35e-09

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: 54.89  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 162 GPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERG 241
Cdd:cd03693     3 KPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRG 82


                  ...
gi 2462496731 242 LVC 244
Cdd:cd03693    83 DVA 85
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 42-156 1.49e-09

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: 57.30  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENT-KFRGAP 120
Cdd:cd00881    78 ETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFTFlKGKDVP 157

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462496731 121 IIPVAAKPGGpeapeteapqGIPELIELLTSQISIP 156
Cdd:cd00881   158 IIPISALTGE----------GIEELLDAIVEHLPPP 183
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 51-245 5.96e-09

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 58.22  E-value: 5.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  51 DLMMLVIDVTKG-------MQTQSAE-CLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENTKFRGA--P 120
Cdd:PTZ00141  110 DVAILVVASTAGefeagisKDGQTREhALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEkvP 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 121 IIPVAAKPGG---PEAPETEAPQGiPELIELLtSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVE 197
Cdd:PTZ00141  190 FIPISGWQGDnmiEKSDNMPWYKG-PTLLEAL-DTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVT 267

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462496731 198 IPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCA 245
Cdd:PTZ00141  268 FAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAS 315
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 46-149 6.50e-09

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: 55.17  E-value: 6.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEgkRQAAIDKMTKKMQKTLENTK-FRG-APIIP 123
Cdd:cd01887    69 GASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYG--TEADPERVKNELSELGLVGEeWGGdVSIVP 146

                          90       100
                  ....*....|....*....|....*.
gi 2462496731 124 VAAKPGgpeapeteapQGIPELIELL 149
Cdd:cd01887   147 ISAKTG----------EGIDDLLEAI 162
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 164-245 1.91e-08

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: 51.50  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 164 FLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTqfDPKLLERGLV 243
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGIL--GVKDILTGDT 78


                  ..
gi 2462496731 244 CA 245
Cdd:cd01342    79 LT 80
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 42-151 3.08e-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 bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 53.38  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQI-ACQKLVVVLNKIDLLPEgkrqAAIDKMTKKMQKTLENTKFRGAP 120
Cdd:cd04171    66 NMLAGAGGIDAVLLVVAADEGIMPQTREHLEILELlGIKKGLVVLTKADLVDE----DRLELVEEEILELLAGTFLADAP 141

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462496731 121 IIPVAAKPGgpeapeteapQGIPELIELLTS 151
Cdd:cd04171   142 IFPVSSVTG----------EGIEELKNYLDE 162
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 50-152 9.35e-08

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, 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.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 51.86  E-value: 9.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  50 IDLMMLVIDVTkgmQTQSAECLVIGQIACQK--LVVVLNKIDLLPEGKRQAAIDKMTKKmqktlentKFRGAPIIPVAAK 127
Cdd:cd00880    77 ADLVLLVVDSD---LTPVEEEAKLGLLRERGkpVLLVLNKIDLVPESEEEELLRERKLE--------LLPDLPVIAVSAL 145

                          90       100
                  ....*....|....*....|....*
gi 2462496731 128 PGgpeapeteapQGIPELIELLTSQ 152
Cdd:cd00880   146 PG----------EGIDELRKKIAEL 160
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 42-158 1.45e-07

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


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 51.88  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGM-QTQSAECLV-IGQIACQKLVVVLNKIDLLpegKRQAAIDKMtKKMQKTLENTKFRGA 119
Cdd:cd01888    93 TMLSGAAVMDGALLLIAANEPCpQPQTSEHLAaLEIMGLKHIIILQNKIDLV---KEEQALENY-EQIKEFVKGTIAENA 168

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462496731 120 PIIPVAAKPGgpeapeteapQGIPELIELLTSQISIPTR 158
Cdd:cd01888   169 PIIPISAQLK----------YNIDVLCEYIVKKIPTPPR 197
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 178-245 1.26e-06

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: 46.10  E-value: 1.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462496731 178 GTVMTGTILSGSISLGDSVEIPALKVVKK-----VKSMQMFHMPITSAMQGDRLGICVTQFDPKLLERGLVCA 245
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 51-151 1.92e-06

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: 47.84  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  51 DLMMLVIDVTKGMQTQSAECLVIGQIACQK--LVVVLNKIDLLPEGKRQAAIDKMTKKmqktlentKFRGAPIIPVAAKP 128
Cdd:cd00882    77 DLILLVVDSTDRESEEDAKLLILRRLRKEGipIILVGNKIDLLEEREVEELLRLEELA--------KILGVPVFEVSAKT 148

                          90       100
                  ....*....|....*....|...
gi 2462496731 129 GgpeapeteapQGIPELIELLTS 151
Cdd:cd00882   149 G----------EGVDELFEKLIE 161
infB CHL00189
translation initiation factor 2; Provisional
 44-198 3.64e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 49.83  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  44 LKGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDllpegKRQAAIDKMTKKMQK-TLENTKFRG-API 121
Cdd:CHL00189  313 SRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKID-----KANANTERIKQQLAKyNLIPEKWGGdTPM 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731 122 IPVAAKPGgpeapeteapQGIPELIE--LLTSQI----SIPTRDPSGPFLMS-VDhcfsiKGQGTVMTGTILSGSISLGD 194
Cdd:CHL00189  388 IPISASQG----------TNIDKLLEtiLLLAEIedlkADPTQLAQGIILEAhLD-----KTKGPVATILVQNGTLHIGD 452


                  ....
gi 2462496731 195 SVEI 198
Cdd:CHL00189  453 IIVI 456
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 46-153 7.30e-06

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: 46.75  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQ--KLVVVLNKIDLLPEGKRQAAIDKMTKK-MQKTLENTKFRgaPII 122
Cdd:pfam00009  89 GLAQADGAILVVDAVEGVMPQTRE--HLRLARQLgvPIIVFINKMDRVDGAELEEVVEEVSRElLEKYGEDGEFV--PVV 164

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462496731 123 PVAAKPGgpeapeteapQGIPELIELLTSQI 153
Cdd:pfam00009 165 PGSALKG----------EGVQTLLDALDEYL 185
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
43-148 2.99e-05

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 46.56  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  43 VLKGAQII---DLMMLVIDVTKGMQTQSAEclVIGQIACQK--LVVVLNKIDLLPegKRQAAIDKMTKKMQKTLentKF- 116
Cdd:COG1160   248 VLRTLRAIeraDVVLLVIDATEGITEQDLK--IAGLALEAGkaLVIVVNKWDLVE--KDRKTREELEKEIRRRL---PFl 320

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462496731 117 RGAPIIPVAAKPGgpeapeteapQGIPELIEL 148
Cdd:COG1160   321 DYAPIVFISALTG----------QGVDKLLEA 342
era PRK00089
GTPase Era; Reviewed
 42-165 3.70e-05

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 45.81  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQsaECLVIGQIACQK--LVVVLNKIDLLpegKRQAAIDKMTKKMQKTLENtkfrgA 119
Cdd:PRK00089   77 AAWSSLKDVDLVLFVVDADEKIGPG--DEFILEKLKKVKtpVILVLNKIDLV---KDKEELLPLLEELSELMDF-----A 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462496731 120 PIIPVAAKPGgpeapeteapQGIPELIELLTSQIsiptrdPSGPFL 165
Cdd:PRK00089  147 EIVPISALKG----------DNVDELLDVIAKYL------PEGPPY 176
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 51-170 3.95e-05

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 46.21  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  51 DLMMLVIDVTKGMQTQSAEclVIGQIACQKLVVVLNKIDLLPEgkrqaaidkmtkkmqKTLENTKFRGAPIIPVAAKPGg 130
Cdd:COG0486   294 DLVLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSE---------------ADGELKSLPGEPVIAISAKTG- 355

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462496731 131 peapeteapQGIPELIELLTSQISIPTRDPSGPFLMSVDH 170
Cdd:COG0486   356 ---------EGIDELKEAILELVGEGALEGEGVLLTNARH 386
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
42-165 4.45e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 45.36  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQK--LVVVLNKIDLLPEGKRQAAIDKMTKKMqktlentKFrgA 119
Cdd:COG1159    75 AAWSALEDVDVILFVVDATEKIGEGDEF--ILELLKKLKtpVILVINKIDLVKKEELLPLLAEYSELL-------DF--A 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462496731 120 PIIPVAAKPGgpeapeteapQGIPELIELLTSQIsiptrdPSGPFL 165
Cdd:COG1159   144 EIVPISALKG----------DNVDELLDEIAKLL------PEGPPY 173
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
44-154 1.78e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 42.28  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  44 LKGAqiiDLMMLVIDVTKGMQTQSAE---CLVIGQIACQKLVVVLNKIDLLPEGKRQAAidkmtKKMQKTLENTKFrgAP 120
Cdd:COG1100    77 LTGA---SLYLFVVDGTREETLQSLYellESLRRLGKKSPIILVLNKIDLYDEEEIEDE-----ERLKEALSEDNI--VE 146

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462496731 121 IIPVAAKPGgpeapeteapQGIPELIELLTSQIS 154
Cdd:COG1100   147 VVATSAKTG----------EGVEELFAALAEILR 170
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 163-235 2.45e-04

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: 39.80  E-value: 2.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462496731 163 PFLMSVDHCFSIKGQGTVMTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDP 235
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDP 73
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 43-148 2.66e-04

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: 42.03  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  43 VLKGAQII---DLMMLVIDVTKGMQTQSAEclVIGQIACQK--LVVVLNKIDLLPegKRQAAIDKMTKKMQKTLenTKFR 117
Cdd:cd01895    75 VLRTLKAIeraDVVLLVLDASEGITEQDLR--IAGLILEEGkaLIIVVNKWDLVE--KDEKTMKEFEKELRRKL--PFLD 148

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462496731 118 GAPIIPVAAKPGgpeapeteapQGIPELIEL 148
Cdd:cd01895   149 YAPIVFISALTG----------QGVDKLFDA 169
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 51-151 3.20e-04

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 41.33  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  51 DLMMLVIDVTKGMQTQSAEclVIGQIACQKLVVVLNKIDLLPEGKRQAAIDkmtkkmqktlentkfrGAPIIPVAAKPGg 130
Cdd:cd04164    84 DLVLLVVDASEGLDEEDLE--ILELPAKKPVIVVLNKSDLLSDAEGISELN----------------GKPIIAISAKTG- 144

                          90       100
                  ....*....|....*....|.
gi 2462496731 131 peapeteapQGIPELIELLTS 151
Cdd:cd04164   145 ---------EGIDELKEALLE 156
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 51-170 4.56e-04

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 42.47  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  51 DLMMLVIDVTKGmQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKrqaaidkmtkkmqktlENTKFRGAPIIPVAAKPGg 130
Cdd:pfam12631 175 DLVLLVLDASRP-LDEEDLEILELLKDKKPIIVVLNKSDLLGEID----------------ELEELKGKPVLAISAKTG- 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462496731 131 peapeteapQGIPELIELLTSQISIPTRDPSGPFLMSVDH 170
Cdd:pfam12631 237 ---------EGLDELEEAIKELFLAGEIASDGPIITNARH 267
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 46-129 5.59e-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: 41.40  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  46 GAQIIDLMMLVIDVTKGMQTQS------AECLVIGQIacqklVVVLNKIDLLpeGKRQAAIDKMTKKMQKTLENTKFRGA 119
Cdd:cd04166    98 GASTADLAILLVDARKGVLEQTrrhsyiASLLGIRHV-----VVAVNKMDLV--DYDEEVFEEIKADYLAFAASLGIEDI 170

                          90
                  ....*....|
gi 2462496731 120 PIIPVAAKPG 129
Cdd:cd04166   171 TFIPISALEG 180
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 42-152 5.88e-04

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 40.91  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  42 TVLKGAQIIDLMMLVIDVTKGMQTQsaECLVIGQIACQKL--VVVLNKIDLLPEGKR-QAAIDKMTKKMQktlentkfrG 118
Cdd:cd04163    75 AAWSALKDVDLVLFVVDASEWIGEG--DEFILELLKKSKTpvILVLNKIDLVKDKEDlLPLLEKLKELHP---------F 143

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462496731 119 APIIPVAAKPGgpeapeteapQGIPELIELLTSQ 152
Cdd:cd04163   144 AEIFPISALKG----------ENVDELLEYIVEY 167
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 50-123 8.66e-04

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 40.31  E-value: 8.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462496731  50 IDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVvLNKIDLLPEGKRQAAIDKMTKKMQktlentkfRGAPIIP 123
Cdd:pfam02492 115 LDGVITVVDAANEADGEKIPRKAGDQIAFADLIV-LNKTDLAPEVALLEVLEEDLRRLN--------PGAPVVP 179
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 43-148 1.75e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.80  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  43 VLKGAQII---DLMMLVIDVTKGMQTQSAecLVIGQIACQK--LVVVLNKIDLLPEGKRQAAIDKMTKKMQktlentKFR 117
Cdd:PRK00093  246 VIRTLKAIeraDVVLLVIDATEGITEQDL--RIAGLALEAGraLVIVVNKWDLVDEKTMEEFKKELRRRLP------FLD 317

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462496731 118 GAPIIPVAAKPGgpeapeteapQGIPELIEL 148
Cdd:PRK00093  318 YAPIVFISALTG----------QGVDKLLEA 338
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 178-228 3.38e-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: 3.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462496731 178 GTVMTGTILSGSISLGDSVEIPALkvVKKVKSMQMFHMPITSAMQGDRLGI 228
Cdd:cd16265    14 RQVLTGEVESGVIYVGYKVKGDKG--VALIRAIEREHRKVDFAVAGDEVAL 62
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
51-151 3.92e-03

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 39.71  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496731  51 DLMMLVIDVTKGMQTQSAEclVIGQIACQKLVVVLNKIDLLPEgkrqaaidkmtkkmqktLENTKFRGAPIIPVAAKPGg 130
Cdd:PRK05291  296 DLVLLVLDASEPLTEEDDE--ILEELKDKPVIVVLNKADLTGE-----------------IDLEEENGKPVIRISAKTG- 355

                          90       100
                  ....*....|....*....|.
gi 2462496731 131 peapeteapQGIPELIELLTS 151
Cdd:PRK05291  356 ---------EGIDELREAIKE 367
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 80-155 5.36e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 37.91  E-value: 5.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496731  80 KLVVVLNKIDLLPEgkrqaaiDKMTKKMQKTLENTkfrGAPIIPVAAKPGgpeapeteapQGIPELIELLTSQISI 155
Cdd:pfam03193  55 EPVIVLNKIDLLDE-------EEELEELLKIYRAI---GYPVLFVSAKTG----------EGIEALKELLKGKTTV 110
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 183-229 7.96e-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: 35.62  E-value: 7.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462496731 183 GTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGIC 229
Cdd:cd03695    20 GTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLT 66
 
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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