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Conserved domains on  [gi|2289442737|ref|NP_001398377|]
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selenocysteine-specific elongation factor isoform 11 [Mus musculus]

Protein Classification

GTP-binding protein TypA; selenocysteine-specific translation elongation factor( domain architecture ID 10112162)

GTP-binding protein TypA/BipA-like involved in stress response and virulence regulation| selenocysteine-specific translation elongation factor binds GTP and GDP and transfers selenocysteyl-tRNA to the ribosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 8-197 1.07e-103

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: 299.28  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTAAFDKQPQSRERGITLDLGFSCFVVPLPGAEPGSS---DTLLQVTLVDCPGHAS 84
Cdd:cd01889     1 VNVGLLGHVDSGKTSLAKALSEIASTAAFDKNPQSQERGITLDLGFSSFEVDKPKHLEDNEnpqIENYQITLVDCPGHAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  85 LIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLAEGKRQAAIDKMTKKMQKTLENTKFRG 164
Cdd:cd01889    81 LIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKTRLKD 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2289442737 165 APIIPVAAKPGGPEApetEAPQGISELIELLKS 197
Cdd:cd01889   161 SPIIPVSAKPGEGEA---ELGGELKNLIVLPLI 190
Translation_Factor_II_like super family cl02787
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 210-250 1.78e-17

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.


The actual alignment was detected with superfamily member cd03696:

Pssm-ID: 445922 [Multi-domain]  Cd Length: 83  Bit Score: 74.87  E-value: 1.78e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2289442737 210 FLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKEK 250
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKE 41
 
Name Accession Description Interval E-value
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 8-197 1.07e-103

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: 299.28  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTAAFDKQPQSRERGITLDLGFSCFVVPLPGAEPGSS---DTLLQVTLVDCPGHAS 84
Cdd:cd01889     1 VNVGLLGHVDSGKTSLAKALSEIASTAAFDKNPQSQERGITLDLGFSSFEVDKPKHLEDNEnpqIENYQITLVDCPGHAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  85 LIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLAEGKRQAAIDKMTKKMQKTLENTKFRG 164
Cdd:cd01889    81 LIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKTRLKD 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2289442737 165 APIIPVAAKPGGPEApetEAPQGISELIELLKS 197
Cdd:cd01889   161 SPIIPVSAKPGEGEA---ELGGELKNLIVLPLI 190
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 8-244 1.81e-53

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: 182.81  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFSCFvvPLPGAEpgssdtllQVTLVDCPGHASLIR 87
Cdd:COG3276     1 MIIGTAGHIDHGKTTLVKALTGIDT----DRLKEEKKRGITIDLGFAYL--PLPDGR--------RLGFVDVPGHEKFIK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  88 TIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIgqiaCQ-----KLVVVLNKIDLLAEgkrqAAIDKMTKKMQKTLENTKF 162
Cdd:COG3276    67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAI----LDllgikRGIVVLTKADLVDE----EWLELVEEEIRELLAGTFL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 163 RGAPIIPVAAKPGgpeapeteapQGISELIELLKSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDS 241
Cdd:COG3276   139 EDAPIVPVSAVTG----------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDE 208


                  ...
gi 2289442737 242 VEI 244
Cdd:COG3276   209 LEL 211
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 8-244 7.91e-45

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: 158.88  E-value: 7.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFSCFvvPLPGAEPGssdtllqvtLVDCPGHASLIR 87
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAA----DRLPEEKKRGMTIDLGFAYF--PLPDYRLG---------FIDVPGHEKFIS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  88 TIIGGAQIIDLMMLVIDVTKGMQTQSAECL-VIGQIACQKLVVVLNKIDLLAEgkrqAAIDKMTKKMQKTLENTKF-RGA 165
Cdd:TIGR00475  66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADRVNE----EEIKRTEMFMKQILNSYIFlKNA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 166 PIIPVAAKPGgpeapeteapQGISELIELLKSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEI 244
Cdd:TIGR00475 142 KIFKTSAKTG----------QGIGELKKELKNLLeSLDIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL 211
PRK12736 PRK12736
elongation factor Tu; Reviewed
 8-254 9.72e-35

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 128.52  E-value: 9.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAST---------AAFDKQPQSRERGITLDLgfscfvvplpgAEPGSSDTLLQVTLVD 78
Cdd:PRK12736   13 VNIGTIGHVDHGKTTLTAAITKVLAErglnqakdyDSIDAAPEEKERGITINT-----------AHVEYETEKRHYAHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  79 CPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLAEgkrQAAIDKMTKKMQKTL 157
Cdd:PRK12736   82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREhILLARQVGVPYLVVFLNKVDLVDD---EELLELVEMEVRELL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 158 ENTKFRG--APIIPVAAKPGGPEAPETEapQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGT 235
Cdd:PRK12736  159 SEYDFPGddIPVIRGSALKALEGDPKWE--DAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236

                         250
                  ....*....|....*....
gi 2289442737 236 ISLGDSVEIPALKEKQAAT 254
Cdd:PRK12736  237 VKVGDEVEIVGIKETQKTV 255
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 8-195 1.81e-25

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: 99.14  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALA------------RALSTTASTAAFDKQPQSRERGITLDLGFSCFVVPLPgaepgssdtllQVT 75
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTdrllyytgaiskRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDY-----------LIN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  76 LVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQ--KLVVVLNKIDLLAEGKRQAAIDKMTKK- 152
Cdd:pfam00009  73 LIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTRE--HLRLARQLgvPIIVFINKMDRVDGAELEEVVEEVSREl 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2289442737 153 MQKTLENTKFRgaPIIPVAAKPGgpeapeteapQGISELIELL 195
Cdd:pfam00009 151 LEKYGEDGEFV--PVVPGSALKG----------EGVQTLLDAL 181
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 210-250 1.78e-17

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: 74.87  E-value: 1.78e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2289442737 210 FLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKEK 250
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKE 41
 
Name Accession Description Interval E-value
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 8-197 1.07e-103

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: 299.28  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTAAFDKQPQSRERGITLDLGFSCFVVPLPGAEPGSS---DTLLQVTLVDCPGHAS 84
Cdd:cd01889     1 VNVGLLGHVDSGKTSLAKALSEIASTAAFDKNPQSQERGITLDLGFSSFEVDKPKHLEDNEnpqIENYQITLVDCPGHAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  85 LIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLAEGKRQAAIDKMTKKMQKTLENTKFRG 164
Cdd:cd01889    81 LIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLIPEEERKRKIEKMKKRLQKTLEKTRLKD 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2289442737 165 APIIPVAAKPGGPEApetEAPQGISELIELLKS 197
Cdd:cd01889   161 SPIIPVSAKPGEGEA---ELGGELKNLIVLPLI 190
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 8-244 1.81e-53

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: 182.81  E-value: 1.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFSCFvvPLPGAEpgssdtllQVTLVDCPGHASLIR 87
Cdd:COG3276     1 MIIGTAGHIDHGKTTLVKALTGIDT----DRLKEEKKRGITIDLGFAYL--PLPDGR--------RLGFVDVPGHEKFIK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  88 TIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIgqiaCQ-----KLVVVLNKIDLLAEgkrqAAIDKMTKKMQKTLENTKF 162
Cdd:COG3276    67 NMLAGAGGIDLVLLVVAADEGVMPQTREHLAI----LDllgikRGIVVLTKADLVDE----EWLELVEEEIRELLAGTFL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 163 RGAPIIPVAAKPGgpeapeteapQGISELIELLKSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDS 241
Cdd:COG3276   139 EDAPIVPVSAVTG----------EGIDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDE 208


                  ...
gi 2289442737 242 VEI 244
Cdd:COG3276   209 LEL 211
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 8-244 7.91e-45

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: 158.88  E-value: 7.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFSCFvvPLPGAEPGssdtllqvtLVDCPGHASLIR 87
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAA----DRLPEEKKRGMTIDLGFAYF--PLPDYRLG---------FIDVPGHEKFIS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  88 TIIGGAQIIDLMMLVIDVTKGMQTQSAECL-VIGQIACQKLVVVLNKIDLLAEgkrqAAIDKMTKKMQKTLENTKF-RGA 165
Cdd:TIGR00475  66 NAIAGGGGIDAALLVVDADEGVMTQTGEHLaVLDLLGIPHTIVVITKADRVNE----EEIKRTEMFMKQILNSYIFlKNA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 166 PIIPVAAKPGgpeapeteapQGISELIELLKSQI-SIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEI 244
Cdd:TIGR00475 142 KIFKTSAKTG----------QGIGELKKELKNLLeSLDIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRL 211
PRK12736 PRK12736
elongation factor Tu; Reviewed
 8-254 9.72e-35

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 128.52  E-value: 9.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAST---------AAFDKQPQSRERGITLDLgfscfvvplpgAEPGSSDTLLQVTLVD 78
Cdd:PRK12736   13 VNIGTIGHVDHGKTTLTAAITKVLAErglnqakdyDSIDAAPEEKERGITINT-----------AHVEYETEKRHYAHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  79 CPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLAEgkrQAAIDKMTKKMQKTL 157
Cdd:PRK12736   82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREhILLARQVGVPYLVVFLNKVDLVDD---EELLELVEMEVRELL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 158 ENTKFRG--APIIPVAAKPGGPEAPETEapQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGT 235
Cdd:PRK12736  159 SEYDFPGddIPVIRGSALKALEGDPKWE--DAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGT 236

                         250
                  ....*....|....*....
gi 2289442737 236 ISLGDSVEIPALKEKQAAT 254
Cdd:PRK12736  237 VKVGDEVEIVGIKETQKTV 255
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 8-254 1.40e-34

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: 127.97  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTT------ASTAAF---DKQPQSRERGITLDLGFSCFvvplpgaepgSSDTLlQVTLVD 78
Cdd:TIGR00485  13 VNVGTIGHVDHGKTTLTAAITTVlakeggAAARAYdqiDNAPEEKARGITINTAHVEY----------ETETR-HYAHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  79 CPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLLAEgkrQAAIDKMTKKMQKTL 157
Cdd:TIGR00485  82 CPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLArQVGVPYIVVFLNKCDMVDD---EELLELVEMEVRELL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 158 ENTKFRG--APIIPVAAKPGGPEAPETEAPqgISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGT 235
Cdd:TIGR00485 159 SQYDFPGddTPIIRGSALKALEGDAEWEAK--ILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGI 236

                         250
                  ....*....|....*....
gi 2289442737 236 ISLGDSVEIPALKEKQAAT 254
Cdd:TIGR00485 237 IKVGEEVEIVGLKDTRKTT 255
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 8-254 1.54e-34

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: 127.96  E-value: 1.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTA------AF---DKQPQSRERGITLDLGfscfvvplpgaepgssdtllQV---- 74
Cdd:COG0050    13 VNIGTIGHVDHGKTTLTAAITKVLAKKggakakAYdqiDKAPEEKERGITINTS--------------------HVeyet 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  75 -----TLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLLAEgkrQAAIDK 148
Cdd:COG0050    73 ekrhyAHVDCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLArQVGVPYIVVFLNKCDMVDD---EELLEL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 149 MTKKMQKTLENTKFRG--APIIPVAAKPGGPEAPETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTV 226
Cdd:COG0050   150 VEMEVRELLSKYGFPGddTPIIRGSALKALEGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTV 229

                         250       260
                  ....*....|....*....|....*...
gi 2289442737 227 MTGTILSGTISLGDSVEIPALKEKQAAT 254
Cdd:COG0050   230 VTGRVERGIIKVGDEVEIVGIRDTQKTV 257
PRK12735 PRK12735
elongation factor Tu; Reviewed
 8-254 2.19e-34

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 127.65  E-value: 2.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTAAF---------DKQPQSRERGITLDlgfscfvvplpgaepgSSDTLLQVT--- 75
Cdd:PRK12735   13 VNVGTIGHVDHGKTTLTAAITKVLAKKGGgeakaydqiDNAPEEKARGITIN----------------TSHVEYETAnrh 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  76 --LVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLL--AEgkrqaAIDKMT 150
Cdd:PRK12735   77 yaHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREhILLARQVGVPYIVVFLNKCDMVddEE-----LLELVE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 151 KKMQKTLENTKFRG--APIIPVAAKPGGPEAPETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMT 228
Cdd:PRK12735  152 MEVRELLSKYDFPGddTPIIRGSALKALEGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVT 231

                         250       260
                  ....*....|....*....|....*.
gi 2289442737 229 GTILSGTISLGDSVEIPALKEKQAAT 254
Cdd:PRK12735  232 GRVERGIVKVGDEVEIVGIKETQKTT 257
PRK00049 PRK00049
elongation factor Tu; Reviewed
 8-254 4.97e-34

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 126.46  E-value: 4.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTA------AF---DKQPQSRERGITLDlgfscfvvplpgaepgssdtllqvT--- 75
Cdd:PRK00049   13 VNVGTIGHVDHGKTTLTAAITKVLAKKggaeakAYdqiDKAPEEKARGITIN------------------------Tahv 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  76 ----------LVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLAEgkrQA 144
Cdd:PRK00049   69 eyetekrhyaHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREhILLARQVGVPYIVVFLNKCDMVDD---EE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 145 AIDKMTKKMQKTLENTKFRG--APIIPVAAKP---GGPEAPETEApqgISELIELLKSQISIPTRDPSGPFLMSVDHCFS 219
Cdd:PRK00049  146 LLELVEMEVRELLSKYDFPGddTPIIRGSALKaleGDDDEEWEKK---ILELMDAVDSYIPTPERAIDKPFLMPIEDVFS 222

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2289442737 220 IKGQGTVMTGTILSGTISLGDSVEIPALKEKQAAT 254
Cdd:PRK00049  223 ISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTT 257
tufA CHL00071
elongation factor Tu
 8-254 2.19e-32

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 122.37  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTASTAA---------FDKQPQSRERGITLDLgfscfvvplpgAEPGSSDTLLQVTLVD 78
Cdd:CHL00071   13 VNIGTIGHVDHGKTTLTAAITMTLAAKGgakakkydeIDSAPEEKARGITINT-----------AHVEYETENRHYAHVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  79 CPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLLAEGKrqaAIDKMTKKMQKTL 157
Cdd:CHL00071   82 CPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAkQVGVPNIVVFLNKEDQVDDEE---LLELVELEVRELL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 158 ENTKFRGA--PIIPVAA-------------KPGgpeapETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKG 222
Cdd:CHL00071  159 SKYDFPGDdiPIVSGSAllalealtenpkiKRG-----ENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITG 233

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2289442737 223 QGTVMTGTILSGTISLGDSVEIPALKEKQAAT 254
Cdd:CHL00071  234 RGTVATGRIERGTVKVGDTVEIVGLRETKTTT 265
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 8-248 1.50e-31

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 120.34  E-value: 1.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFS--------------CFVV----PLPGAEPgssD 69
Cdd:PRK04000   10 VNIGMVGHVDHGKTTLVQALTGVWT----DRHSEELKRGITIRLGYAdatirkcpdceepeAYTTepkcPNCGSET---E 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  70 TLLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGM-QTQSAECLV-IGQIACQKLVVVLNKIDLLAegkRQAAID 147
Cdd:PRK04000   83 LLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMaLDIIGIKNIVIVQNKIDLVS---KERALE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 148 KMtKKMQKTLENTKFRGAPIIPVAAKpggpeapeteapQG--ISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGT 225
Cdd:PRK04000  160 NY-EQIKEFVKGTVAENAPIIPVSAL------------HKvnIDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGT 226

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2289442737 226 --------VMTGTILSGTISLGDSVEI-PALK 248
Cdd:PRK04000  227 ppeklkggVIGGSLIQGVLKVGDEIEIrPGIK 258
PLN03127 PLN03127
Elongation factor Tu; Provisional
 8-249 3.48e-31

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 119.93  E-value: 3.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTT------ASTAAF---DKQPQSRERGITLDlgfscfvvplpGAEPGSSDTLLQVTLVD 78
Cdd:PLN03127   62 VNVGTIGHVDHGKTTLTAAITKVlaeegkAKAVAFdeiDKAPEEKARGITIA-----------TAHVEYETAKRHYAHVD 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  79 CPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLAEgkrQAAIDKMTKKMQKTL 157
Cdd:PLN03127  131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEhILLARQVGVPSLVVFLNKVDVVDD---EELLELVEMELRELL 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 158 ENTKFRG--APIIPVAAKPGGPEAPETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGT 235
Cdd:PLN03127  208 SFYKFPGdeIPIIRGSALSALQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGT 287

                         250
                  ....*....|....
gi 2289442737 236 ISLGDSVEIPALKE 249
Cdd:PLN03127  288 IKVGEEVEIVGLRP 301
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 9-202 2.23e-30

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: 112.00  E-value: 2.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARALST---------TASTAAFDKQPQSRERGITLDLGFSCFVVPLPgaepgssdtllQVTLVDC 79
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYqtgaidrrgTRKETFLDTLKEERERGITIKTGVVEFEWPKR-----------RINFIDT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  80 PGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLAEGKRQAAIDKMTKKMQKTLEN 159
Cdd:cd00881    70 PGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFT 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2289442737 160 T-KFRGAPIIPVAAKPGGpeapeteapqGISELIELLKSQISIP 202
Cdd:cd00881   150 FlKGKDVPIIPISALTGE----------GIEELLDAIVEHLPPP 183
PLN03126 PLN03126
Elongation factor Tu; Provisional
 4-254 6.89e-29

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 113.94  E-value: 6.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   4 RRVNVNVGVLGHIDSGKT----ALARALSTTASTAA-----FDKQPQSRERGITLDLgfscfvvplpgAEPGSSDTLLQV 74
Cdd:PLN03126   78 KKPHVNIGTIGHVDHGKTtltaALTMALASMGGSAPkkydeIDAAPEERARGITINT-----------ATVEYETENRHY 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  75 TLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE-CLVIGQIACQKLVVVLNKIDLLAEGKRQAAIDKMTKKM 153
Cdd:PLN03126  147 AHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEhILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVREL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 154 qktLENTKFRG--APIIP------VAAKPGGPEAP--ETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQ 223
Cdd:PLN03126  227 ---LSSYEFPGddIPIISgsallaLEALMENPNIKrgDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGR 303

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2289442737 224 GTVMTGTILSGTISLGDSVEIPALKEKQAAT 254
Cdd:PLN03126  304 GTVATGRVERGTVKVGETVDIVGLRETRSTT 334
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 14-242 2.52e-28

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 113.22  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  14 GHIDSGKTALARALsTTASTaafDKQPQSRERGITLDLGFSCFvvPLPGAEPgssdtllqVTLVDCPGHASLIRTIIGGA 93
Cdd:PRK10512    7 GHVDHGKTTLLQAI-TGVNA---DRLPEEKKRGMTIDLGYAYW--PQPDGRV--------LGFIDVPGHEKFLSNMLAGV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  94 QIIDLMMLVIDVTKGMQTQSAECLVIGQIA-CQKLVVVLNKIDLLAEGKrqaaIDKMTKKMQKTLENTKFRGAPIIPVAA 172
Cdd:PRK10512   73 GGIDHALLVVACDDGVMAQTREHLAILQLTgNPMLTVALTKADRVDEAR----IAEVRRQVKAVLREYGFAEAKLFVTAA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 173 KPGgpeapeteapQGISELIELLkSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSV 242
Cdd:PRK10512  149 TEG----------RGIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTL 207
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 10-197 9.18e-28

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: 104.61  E-value: 9.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  10 VGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFSCFvvPLPGAEPgssdtllqVTLVDCPGHASLIRTI 89
Cdd:cd04171     2 IGTAGHIDHGKTTLIKALTGIET----DRLPEEKKRGITIDLGFAYL--DLPDGKR--------LGFIDVPGHEKFVKNM 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  90 IGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQI-ACQKLVVVLNKIDLLAEgkrqAAIDKMTKKMQKTLENTKFRGAPII 168
Cdd:cd04171    68 LAGAGGIDAVLLVVAADEGIMPQTREHLEILELlGIKKGLVVLTKADLVDE----DRLELVEEEILELLAGTFLADAPIF 143

                         170       180
                  ....*....|....*....|....*....
gi 2289442737 169 PVAAKPGgpeapeteapQGISELIELLKS 197
Cdd:cd04171   144 PVSSVTG----------EGIEELKNYLDE 162
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 4-256 9.25e-26

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 105.09  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   4 RRVNVNVGVLGHIDSGKTALARALSTTaSTAAFDkqpQSRERGITLDLG------FSCFVVPLPGA----------EP-- 65
Cdd:PTZ00327   31 RQATINIGTIGHVAHGKSTVVKALSGV-KTVRFK---REKVRNITIKLGyanakiYKCPKCPRPTCyqsygsskpdNPpc 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  66 ---GSSDTLLQ-VTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGM-QTQSAECLVIGQIACQKLVVVL-NKIDLLae 139
Cdd:PTZ00327  107 pgcGHKMTLKRhVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHLAAVEIMKLKHIIILqNKIDLV-- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 140 gKRQAAIDKMtKKMQKTLENTKFRGAPIIPVAAKPGgpeapeteapQGISELIELLKSQISIPTRDPSGPFLMSVDHCFS 219
Cdd:PTZ00327  185 -KEAQAQDQY-EEIRNFVKGTIADNAPIIPISAQLK----------YNIDVVLEYICTQIPIPKRDLTSPPRMIVIRSFD 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2289442737 220 IKG--------QGTVMTGTILSGTISLGDSVEI-PALKEKQAATQL 256
Cdd:PTZ00327  253 VNKpgedienlKGGVAGGSILQGVLKVGDEIEIrPGIISKDSGGEF 298
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 8-195 1.81e-25

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: 99.14  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALA------------RALSTTASTAAFDKQPQSRERGITLDLGFSCFVVPLPgaepgssdtllQVT 75
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTdrllyytgaiskRGEVKGEGEAGLDNLPEERERGITIKSAAVSFETKDY-----------LIN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  76 LVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQ--KLVVVLNKIDLLAEGKRQAAIDKMTKK- 152
Cdd:pfam00009  73 LIDTPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTRE--HLRLARQLgvPIIVFINKMDRVDGAELEEVVEEVSREl 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2289442737 153 MQKTLENTKFRgaPIIPVAAKPGgpeapeteapQGISELIELL 195
Cdd:pfam00009 151 LEKYGEDGEFV--PVVPGSALKG----------EGVQTLLDAL 181
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 8-173 1.93e-24

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: 96.57  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTAStaafDKQPQSRERGITLDLGFS------CFV--VPLPGAEP-------GSSDTLL 72
Cdd:cd01888     1 INIGTIGHVAHGKTTLVKALSGVWT----VRHKEELKRNITIKLGYAnakiykCPNcgCPRPYDTPececpgcGGETKLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  73 Q-VTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGM-QTQSAECLV-IGQIACQKLVVVLNKIDLLaegKRQAAIDKM 149
Cdd:cd01888    77 RhVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHLAaLEIMGLKHIIILQNKIDLV---KEEQALENY 153

                         170       180
                  ....*....|....*....|....
gi 2289442737 150 tKKMQKTLENTKFRGAPIIPVAAK 173
Cdd:cd01888   154 -EQIKEFVKGTIAENAPIIPISAQ 176
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-242 1.43e-19

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: 87.30  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   1 MAGRRVNVNVGVLGHIDSGKTAL------------ARALSTTASTA----------AF--DKQPQSRERGITLDLGFSCF 56
Cdd:COG5256     1 MASEKPHLNLVVIGHVDHGKSTLvgrllyetgaidEHIIEKYEEEAekkgkesfkfAWvmDRLKEERERGVTIDLAHKKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  57 vvplpgaepgSSDTLLqVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAE------CLVIGQIacqklVVV 130
Cdd:COG5256    81 ----------ETDKYY-FTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREhaflarTLGINQL-----IVA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 131 LNKIDLLA-EGKRQAAIDKMTKKMQKTLeNTKFRGAPIIPVAAKPG------GPEAPETEAPQgiseLIELLkSQISIPT 203
Cdd:COG5256   145 VNKMDAVNySEKRYEEVKEEVSKLLKMV-GYKVDKIPFIPVSAWKGdnvvkkSDNMPWYNGPT----LLEAL-DNLKEPE 218

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2289442737 204 RDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSV 242
Cdd:COG5256   219 KPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKV 257
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 210-250 1.78e-17

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: 74.87  E-value: 1.78e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2289442737 210 FLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKEK 250
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKE 41
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 7-202 4.37e-17

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 76.85  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   7 NVNVGVLGHIDSGKTALARALSTTASTA---------AFDKQPQSRERGITLDLgfscfvvplpgAEPGSSDTLLQVTLV 77
Cdd:cd01884     2 HVNVGTIGHVDHGKTTLTAAITKVLAKKggakakkydEIDKAPEEKARGITINT-----------AHVEYETANRHYAHV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  78 DCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIG-QIACQKLVVVLNKIDLLAEgkrQAAIDKMTKKMQKT 156
Cdd:cd01884    71 DCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLArQVGVPYIVVFLNKADMVDD---EELLELVEMEVREL 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2289442737 157 LENTKFRG--APIIPVAAKPGGPEAPETEAPQGISELIELLKSQISIP 202
Cdd:cd01884   148 LSKYGFDGddTPIVRGSALKALEGDDPNKWVDKILELLDALDSYIPTP 195
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 8-242 1.14e-16

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 78.81  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGK-TALARALSTTAS-------------------TAAF----DKQPQSRERGITLDLGFSCFvvplpga 63
Cdd:PRK12317    7 LNLAVIGHVDHGKsTLVGRLLYETGAidehiieelreeakekgkeSFKFawvmDRLKEERERGVTIDLAHKKF------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  64 epgssDT-LLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGM----QTQS----AECLVIGQiacqkLVVVLNKI 134
Cdd:PRK12317   80 -----ETdKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDAGgvmpQTREhvflARTLGINQ-----LIVAINKM 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 135 DLLA-EGKRQAAIDKMTKKMQKTLeNTKFRGAPIIPVAAKPG------GPEAPETEAPQgiseLIELLkSQISIPTRDPS 207
Cdd:PRK12317  150 DAVNyDEKRYEEVKEEVSKLLKMV-GYKPDDIPFIPVSAFEGdnvvkkSENMPWYNGPT----LLEAL-DNLKPPEKPTD 223

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2289442737 208 GPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSV 242
Cdd:PRK12317  224 KPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKV 258
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 10-195 3.47e-16

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: 74.05  E-value: 3.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  10 VGVLGHIDSGKTALARALSTTastaafdkQPQSRE-RGITLDLGfsCFVVPLPGAEPGssdtllqVTLVDCPGHASLIRT 88
Cdd:cd01887     3 VTVMGHVDHGKTTLLDKIRKT--------NVAAGEaGGITQHIG--AYQVPIDVKIPG-------ITFIDTPGHEAFTNM 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  89 IIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLaeGKRQAAIDKMTKKMQKTLENTK-FRG-AP 166
Cdd:cd01887    66 RARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKP--YGTEADPERVKNELSELGLVGEeWGGdVS 143

                         170       180
                  ....*....|....*....|....*....
gi 2289442737 167 IIPVAAKPGgpeapeteapQGISELIELL 195
Cdd:cd01887   144 IVPISAKTG----------EGIDDLLEAI 162
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-239 2.05e-14

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 72.43  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   1 MAGRRVNVNVGVLGHIDSGKTALA------------RALSTTASTAA------------FDKQPQSRERGITLDLGFSCF 56
Cdd:PLN00043    1 MGKEKVHINIVVIGHVDSGKSTTTghliyklggidkRVIERFEKEAAemnkrsfkyawvLDKLKAERERGITIDIALWKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  57 vvplpgaepgsSDTLLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKG-------MQTQSAE-CLVIGQIACQKLV 128
Cdd:PLN00043   81 -----------ETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREhALLAFTLGVKQMI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 129 VVLNKIDLLAEGKRQAAIDKMTKKMQKTLENTKFR--GAPIIPVAAKPGG---PEAPETEAPQGISeLIELLkSQISIPT 203
Cdd:PLN00043  150 CCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNpdKIPFVPISGFEGDnmiERSTNLDWYKGPT-LLEAL-DQINEPK 227

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2289442737 204 RDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLG 239
Cdd:PLN00043  228 RPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG 263
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-242 2.43e-14

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 72.09  E-value: 2.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   1 MAGRRVNVNVGVLGHIDSGKTALARAL------------------STTASTAAF------DKQPQSRERGITLDLGFSCF 56
Cdd:PTZ00141    1 MGKEKTHINLVVIGHVDSGKSTTTGHLiykcggidkrtiekfekeAAEMGKGSFkyawvlDKLKAERERGITIDIALWKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  57 VVPLpgaepgssdtlLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKG-------MQTQSAE-CLVIGQIACQKLV 128
Cdd:PTZ00141   81 ETPK-----------YYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagisKDGQTREhALLAFTLGVKQMI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 129 VVLNKIDLLAEGKRQAAIDKMTKKMQKTLENTKFRGA--PIIPVAAKPG------GPEAPETEAPQgiseLIELLKSqIS 200
Cdd:PTZ00141  150 VCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEkvPFIPISGWQGdnmiekSDNMPWYKGPT----LLEALDT-LE 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2289442737 201 IPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISLGDSV 242
Cdd:PTZ00141  225 PPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVV 266
infB CHL00189
translation initiation factor 2; Provisional
 10-244 9.47e-13

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 67.55  E-value: 9.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  10 VGVLGHIDSGKTALARALSTTASTaafdkqpQSRERGITLDLGfsCFVVPLPgaepgSSDTLLQVTLVDCPGHASLIRTI 89
Cdd:CHL00189  247 VTILGHVDHGKTTLLDKIRKTQIA-------QKEAGGITQKIG--AYEVEFE-----YKDENQKIVFLDTPGHEAFSSMR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  90 IGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDllaegKRQAAIDKMTKKMQK-TLENTKFRG-API 167
Cdd:CHL00189  313 SRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKID-----KANANTERIKQQLAKyNLIPEKWGGdTPM 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 168 IPVAAKPGgpeapeteapQGISELIE--LLKSQI----SIPTRDPSGPFLMS-VDhcfsiKGQGTVMTGTILSGTISLGD 240
Cdd:CHL00189  388 IPISASQG----------TNIDKLLEtiLLLAEIedlkADPTQLAQGIILEAhLD-----KTKGPVATILVQNGTLHIGD 452


                  ....
gi 2289442737 241 SVEI 244
Cdd:CHL00189  453 IIVI 456
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 9-172 1.52e-12

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 64.82  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTAL------------ARAL------STTASTAAF------DKQPQSRERGITLDLGFSCFVVPLpgae 64
Cdd:cd01883     1 NLVVIGHVDAGKSTLtghllyklggvdKRTIekyekeAKEMGKESFkyawvlDKLKEERERGVTIDVGLAKFETEK---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  65 pgssdtlLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKG-------MQTQSAE-CLVIGQIACQKLVVVLNKIDL 136
Cdd:cd01883    77 -------YRFTIIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREhALLARTLGVKQLIVAVNKMDD 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2289442737 137 LAEGKRQAAIDKMTKKMQKTLENTKFRGA--PIIPVAA 172
Cdd:cd01883   150 VTVNWSQERYDEIKKKVSPFLKKVGYNPKdvPFIPISG 187
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 11-195 5.68e-12

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: 62.09  E-value: 5.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  11 GVLGHIDSGKTALARALSTTASTAAfdkqpqSRERGITLDLGFSCFVVPLPGaepgssdtlLQVTLVDCPGH-------- 82
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEV------SDVPGTTRDPDVYVKELDKGK---------VKLVLVDTPGLdefgglgr 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  83 ASLIRTIIGGAqiiDLMMLVIDVTKGMQTQSAECLVIGQIACQK--LVVVLNKIDLLAEGKRQAAIDKMTKKmqktlent 160
Cdd:cd00882    66 EELARLLLRGA---DLILLVVDSTDRESEEDAKLLILRRLRKEGipIILVGNKIDLLEEREVEELLRLEELA-------- 134

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2289442737 161 KFRGAPIIPVAAKPGgpeapeteapQGISELIELL 195
Cdd:cd00882   135 KILGVPVFEVSAKTG----------EGVDELFEKL 159
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 210-254 2.42e-10

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: 55.60  E-value: 2.42e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2289442737 210 FLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEIPALKEKQAAT 254
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTT 45
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
 9-137 5.54e-10

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 57.66  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTAL-------ARALSTTAS-----TAAFDKQPQSRERGITLDLGFSCFVVPlpgaepGSSDTLLQVTL 76
Cdd:cd04167     2 NVCIAGHLHHGKTSLldmlieqTHKRTPSVKlgwkpLRYTDTRKDEQERGISIKSNPISLVLE------DSKGKSYLINI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2289442737  77 VDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQKL--VVVLNKIDLL 137
Cdd:cd04167    76 IDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTER--LIRHAIQEGLpmVLVINKIDRL 136
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
 9-202 1.20e-09

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 56.00  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALA-RALSTTASTAAFDKQPQ-------SRERGITLDLGfscfVVPLPGAEPGSSDTLLQvtLVDCP 80
Cdd:cd01890     2 NFSIIAHIDHGKSTLAdRLLELTGTVSEREMKEQvldsmdlERERGITIKAQ----AVRLFYKAKDGEEYLLN--LIDTP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  81 GHA--------SLIRTiiGGAqiidlmMLVIDVTKGMQTQS-AEClvigQIACQ---KLVVVLNKIDLLAegkrqAAIDK 148
Cdd:cd01890    76 GHVdfsyevsrSLAAC--EGA------LLVVDATQGVEAQTlANF----YLALEnnlEIIPVINKIDLPA-----ADPDR 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2289442737 149 MTKKMQKTLentkfrGAP---IIPVAAKPGgpeapeteapQGISELIELLKSQISIP 202
Cdd:cd01890   139 VKQEIEDVL------GLDaseAILVSAKTG----------LGVEDLLEAIVERIPPP 179
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 43-175 2.17e-09

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: 56.04  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  43 RERGITLDLGFSCFvvplpgaepgSSDTLLQVtLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQS------AEC 116
Cdd:cd04166    60 REQGITIDVAYRYF----------STPKRKFI-IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTrrhsyiASL 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289442737 117 LVIGQIacqklVVVLNKIDLLaeGKRQAAIDKMTKKMQKTLENTKFRGAPIIPVAAKPG 175
Cdd:cd04166   129 LGIRHV-----VVAVNKMDLV--DYDEEVFEEIKADYLAFAASLGIEDITFIPISALEG 180
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 9-170 3.64e-09

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


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 56.06  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARALSTTAS-----------TAAFDKQPQSRERGITLDLGfscfVVPLPGAEpgssdtlLQVTLV 77
Cdd:cd04170     1 NIALVGHSGSGKTTLAEALLYATGaidrlgrvedgNTVSDYDPEEKKRKMSIETS----VAPLEWNG-------HKINLI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  78 DCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAecLVIGQIACQKL--VVVLNKIDllaegKRQAAIDKMTKKMQK 155
Cdd:cd04170    70 DTPGYADFVGETLSALRAVDAALIVVEAQSGVEVGTE--KVWEFLDDAKLprIIFINKMD-----RARADFDKTLAALRE 142

                         170
                  ....*....|....*
gi 2289442737 156 TLentkfrGAPIIPV 170
Cdd:cd04170   143 AF------GRPVVPI 151
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 9-170 6.10e-09

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 56.21  E-value: 6.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARAL-----------STTASTAAFDKQPQSRERGITLDLGF-SCFVvplpgaepgsSDTllQVTL 76
Cdd:COG0480    11 NIGIVAHIDAGKTTLTERIlfytgaihrigEVHDGNTVMDWMPEEQERGITITSAAtTCEW----------KGH--KINI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  77 VDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAecLVIGQIACQKL--VVVLNKIDllAEGkrqAAIDKMTKKMQ 154
Cdd:COG0480    79 IDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTE--TVWRQADKYGVprIVFVNKMD--REG---ADFDRVLEQLK 151

                         170
                  ....*....|....*.
gi 2289442737 155 KTLentkfrGAPIIPV 170
Cdd:COG0480   152 ERL------GANPVPL 161
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
5-200 6.16e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 54.22  E-value: 6.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   5 RVNVNVGVLGHIDSGKTALARALSTtastAAFDKQPQSRERGITLDLgfscFVVPLPGAEpgssdtlLQVTLVDCPG--- 81
Cdd:COG1100     1 MGEKKIVVVGTGGVGKTSLVNRLVG----DIFSLEKYLSTNGVTIDK----KELKLDGLD-------VDLVIWDTPGqde 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  82 ----HASLIRTIIGgaqiIDLMMLVIDVTKGMQTQSAE---CLVIGQIACQKLVVVLNKIDLLAEGKRQAAidkmtKKMQ 154
Cdd:COG1100    66 fretRQFYARQLTG----ASLYLFVVDGTREETLQSLYellESLRRLGKKSPIILVLNKIDLYDEEEIEDE-----ERLK 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2289442737 155 KTLENTKFrgAPIIPVAAKPGgpeapeteapQGISELIELLKSQIS 200
Cdd:COG1100   137 EALSEDNI--VEVVATSAKTG----------EGVEELFAALAEILR 170
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
 9-137 7.87e-09

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 54.54  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARAL--------STTASTAAF-DKQPQSRERGITLD-----LGFScfvvpLPGAEPGSSDTLLQv 74
Cdd:cd01885     2 NICIIAHVDHGKTTLSDSLlasagiisEKLAGKARYlDTREDEQERGITIKssaisLYFE-----YEEEKMDGNDYLIN- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2289442737  75 tLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLvigQIACQ---KLVVVLNKIDLL 137
Cdd:cd01885    76 -LIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVL---RQALEervKPVLVINKIDRL 137
PRK13351 PRK13351
elongation factor G-like protein;
9-135 8.94e-09

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 55.73  E-value: 8.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALA-RALSTTASTAAF----------DKQPQSRERGITLdlgFSCFV-VPLPGaepgssdtlLQVTL 76
Cdd:PRK13351   10 NIGILAHIDAGKTTLTeRILFYTGKIHKMgevedgttvtDWMPQEQERGITI---ESAATsCDWDN---------HRINL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2289442737  77 VDCPGH----ASLIRTIIGgaqiIDLMMLVIDVTKGMQTQSAecLVIGQIACQKL--VVVLNKID 135
Cdd:PRK13351   78 IDTPGHidftGEVERSLRV----LDGAVVVFDAVTGVQPQTE--TVWRQADRYGIprLIFINKMD 136
PRK04004 PRK04004
translation initiation factor IF-2; Validated
 10-242 1.64e-08

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 54.80  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  10 VGVLGHIDSGKTALaraLSTTASTAAFDKQPQsrerGITLDLGFScfVVPLPG----AEPGSSDTLLQVTL-----VDCP 80
Cdd:PRK04004    9 VVVLGHVDHGKTTL---LDKIRGTAVAAKEAG----GITQHIGAT--EVPIDViekiAGPLKKPLPIKLKIpgllfIDTP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  81 GHA---SLIRTiiGGAqIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLaEGKR-------QAAIDKMT 150
Cdd:PRK04004   80 GHEaftNLRKR--GGA-LADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRI-PGWKstedapfLESIEKQS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 151 KKMQKTLEN----------------------TKF-RGAPIIPVAAKPGgpeapeteapQGISELIELL--------KSQI 199
Cdd:PRK04004  156 QRVQQELEEklyeligqlselgfsadrfdrvKDFtKTVAIVPVSAKTG----------EGIPDLLMVLaglaqrylEERL 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2289442737 200 SIPTRDPSGPFLMSVDhcfSIKGQGTVMTGTILSGTISLGDSV 242
Cdd:PRK04004  226 KIDVEGPGKGTVLEVK---EERGLGTTIDVILYDGTLRKGDTI 265
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 11-198 2.93e-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: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  11 GVLGHIDSGKTALARAL-----STTASTAAFDKQPQSRErgitldlgfscfvVPLPGaepgssdtLLQVTLVDCPG---- 81
Cdd:cd00880     1 AIFGRPNVGKSSLLNALlgqnvGIVSPIPGTTRDPVRKE-------------WELLP--------LGPVVLIDTPGldee 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  82 ------HASLIRTIIGGAqiiDLMMLVIDVTkgmQTQSAECLVIGQIACQK--LVVVLNKIDLLAEGKRQAAIDKMTKKm 153
Cdd:cd00880    60 gglgreRVEEARQVADRA---DLVLLVVDSD---LTPVEEEAKLGLLRERGkpVLLVLNKIDLVPESEEEELLRERKLE- 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2289442737 154 qktlentKFRGAPIIPVAAKPGgpeapeteapQGISELIELLKSQ 198
Cdd:cd00880   133 -------LLPDLPVIAVSALPG----------EGIDELRKKIAEL 160
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
13-170 3.22e-08

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 53.98  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  13 LGHIDSGKTALARAL-----------STTASTAAFDKQPQSRERGITLDLGF-SCFVvplpgaepgsSDTllQVTLVDCP 80
Cdd:PRK12740    1 VGHSGAGKTTLTEAIlfytgaihrigEVEDGTTTMDFMPEERERGISITSAAtTCEW----------KGH--KINLIDTP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  81 GHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAecLVIGQIACQKL--VVVLNKIDllAEGkrqAAIDKMTKKMQKTLe 158
Cdd:PRK12740   69 GHVDFTGEVERALRVLDGAVVVVCAVGGVEPQTE--TVWRQAEKYGVprIIFVNKMD--RAG---ADFFRVLAQLQEKL- 140

                         170
                  ....*....|..
gi 2289442737 159 ntkfrGAPIIPV 170
Cdd:PRK12740  141 -----GAPVVPL 147
era PRK00089
GTPase Era; Reviewed
 73-211 1.33e-07

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 51.59  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  73 QVTLVDCPG-HA-------SLIRTIIGGAQIIDLMMLVIDVTKGMQTQsaECLVIGQIA--CQKLVVVLNKIDLLaegKR 142
Cdd:PRK00089   54 QIIFVDTPGiHKpkralnrAMNKAAWSSLKDVDLVLFVVDADEKIGPG--DEFILEKLKkvKTPVILVLNKIDLV---KD 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289442737 143 QAAIDKMTKKMQKTLENtkfrgAPIIPVAAKPGgpeapeteapQGISELIELLKSQIsiptrdPSGPFL 211
Cdd:PRK00089  129 KEELLPLLEELSELMDF-----AEIVPISALKG----------DNVDELLDVIAKYL------PEGPPY 176
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
73-211 7.62e-07

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 49.22  E-value: 7.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  73 QVTLVDCPG--------HASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAEclVIGQIACQK--LVVVLNKIDLLAEGKR 142
Cdd:COG1159    52 QIVFVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATEKIGEGDEF--ILELLKKLKtpVILVINKIDLVKKEEL 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2289442737 143 QAAIDKMTKKMqktlentKFrgAPIIPVAAKPGgpeapeteapQGISELIELLKSQIsiptrdPSGPFL 211
Cdd:COG1159   130 LPLLAEYSELL-------DF--AEIVPISALKG----------DNVDELLDEIAKLL------PEGPPY 173
PRK10218 PRK10218
translational GTPase TypA;
9-244 2.11e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 48.55  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARALSTTASTaaFDKQPQSRERGI-TLDLGFSCFVVPLpgaepgSSDTLLQ-----VTLVDCPGH 82
Cdd:PRK10218    7 NIAIIAHVDHGKTTLVDKLLQQSGT--FDSRAETQERVMdSNDLEKERGITIL------AKNTAIKwndyrINIVDTPGH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  83 ASLIRTIIGGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDllAEGKR-QAAIDKMTK---KMQKTLE 158
Cdd:PRK10218   79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVD--RPGARpDWVVDQVFDlfvNLDATDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 159 NTKFrgaPIIPVAAKPGGPEAPETEAPQGISELIELLKSQISIPTRDPSGPFLMSVDHCFSIKGQGTVMTGTILSGTISL 238
Cdd:PRK10218  157 QLDF---PIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKP 233


                  ....*.
gi 2289442737 239 GDSVEI 244
Cdd:PRK10218  234 NQQVTI 239
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
84-196 2.22e-06

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 48.10  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  84 SLIRTIiggaQII---DLMMLVIDVTKGMQTQSAEclVIGQIACQK--LVVVLNKIDLLAegKRQAAIDKMTKKMQKTLe 158
Cdd:COG1160   247 SVLRTL----RAIeraDVVLLVIDATEGITEQDLK--IAGLALEAGkaLVIVVNKWDLVE--KDRKTREELEKEIRRRL- 317

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2289442737 159 ntKF-RGAPIIPVAAKPGgpeapeteapQGISELIELLK 196
Cdd:COG1160   318 --PFlDYAPIVFISALTG----------QGVDKLLEAVD 344
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 43-242 2.96e-06

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 48.00  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  43 RERGITLDLGFSCFvvplpgaepgsSDTLLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQS------AEC 116
Cdd:PRK05506   86 REQGITIDVAYRYF-----------ATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTrrhsfiASL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 117 LVIGQIacqklVVVLNKIDLLaeGKRQAAIDKMTKKMQKTLENTKFRGAPIIPVAAKPG------GPEAPETEAPQgise 190
Cdd:PRK05506  155 LGIRHV-----VLAVNKMDLV--DYDQEVFDEIVADYRAFAAKLGLHDVTFIPISALKGdnvvtrSARMPWYEGPS---- 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 191 LIELLKSqISIPTRDPSGPFLMSV--------DHcfsiKGqgtvMTGTILSGTISLGDSV 242
Cdd:PRK05506  224 LLEHLET-VEIASDRNLKDFRFPVqyvnrpnlDF----RG----FAGTVASGVVRPGDEV 274
PTZ00416 PTZ00416
elongation factor 2; Provisional
 9-135 3.28e-06

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 48.12  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARAL--------STTASTAAF-DKQPQSRERGITL-DLGFSC-FVVPLPGAEpGSSDTLlqVTLV 77
Cdd:PTZ00416   21 NMSVIAHVDHGKSTLTDSLvckagiisSKNAGDARFtDTRADEQERGITIkSTGISLyYEHDLEDGD-DKQPFL--INLI 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2289442737  78 DCPGHASLIRTIIGGAQIIDLMMLVIDVTKG--MQTQSaeclVIGQiACQ---KLVVVLNKID 135
Cdd:PTZ00416   98 DSPGHVDFSSEVTAALRVTDGALVVVDCVEGvcVQTET----VLRQ-ALQeriRPVLFINKVD 155
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 8-173 6.12e-06

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 45.06  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   8 VNVGVLGHIDSGKTALARALSTTastaafDKQPQSRERGITLDLGFSCFVVplpgaepgsSDTLLQVTLVDCPGHASL-- 85
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGN------KGSITEYYPGTTRNYVTTVIEE---------DGKTYKFNLLDTAGQEDYda 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  86 -----IRTIIGGAQIIDLMMLVIDVTKGM--QTQSAECLVIGQIacqKLVVVLNKIDLlaegkRQAaidKMTKKMQKTLE 158
Cdd:TIGR00231  67 irrlyYPQVERSLRVFDIVILVLDVEEILekQTKEIIHHADSGV---PIILVGNKIDL-----KDA---DLKTHVASEFA 135

                         170
                  ....*....|....*
gi 2289442737 159 NTKFrgAPIIPVAAK 173
Cdd:TIGR00231 136 KLNG--EPIIPLSAE 148
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 73-198 9.85e-06

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: 44.76  E-value: 9.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  73 QVTLVDCPG-HAS-------LIRTIIGGAQIIDLMMLVIDVTKGMQTQsaECLVIGQIACQKL--VVVLNKIDLLAEGKR 142
Cdd:cd04163    52 QIIFVDTPGiHKPkkklgerMVKAAWSALKDVDLVLFVVDASEWIGEG--DEFILELLKKSKTpvILVLNKIDLVKDKED 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2289442737 143 -QAAIDKMTKKMQktlentkfrGAPIIPVAAKPGgpeapeteapQGISELIELLKSQ 198
Cdd:cd04163   130 lLPLLEKLKELHP---------FAEIFPISALKG----------ENVDELLEYIVEY 167
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 43-244 1.32e-05

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 45.67  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  43 RERGITLDLGFSCFvvplpgaepgSSDTLlQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKGMQTQS------AEC 116
Cdd:PRK05124   89 REQGITIDVAYRYF----------STEKR-KFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTrrhsfiATL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 117 LVIGQiacqkLVVVLNKIDLLaeGKRQAAIDKMT---KKMQKTL-ENTKFRgapIIPVAAKPGGPEAPETEA-P--QGIS 189
Cdd:PRK05124  158 LGIKH-----LVVAVNKMDLV--DYSEEVFERIRedyLTFAEQLpGNLDIR---FVPLSALEGDNVVSQSESmPwySGPT 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2289442737 190 eLIELLKSqISIPTRDPSGPFLMSVDHC----FSIKGqgtvMTGTILSGTISLGDSVEI 244
Cdd:PRK05124  228 -LLEVLET-VDIQRVVDAQPFRFPVQYVnrpnLDFRG----YAGTLASGVVKVGDRVKV 280
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 9-159 3.51e-05

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 43.76  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARAL-----------STTASTAAFDKQPQSRERGITLDlgfscfvvplpgaepgSSDTLLQ---- 73
Cdd:cd04168     1 NIGILAHVDAGKTTLTESLlytsgairelgSVDKGTTRTDSMELERQRGITIF----------------SAVASFQwedt 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  74 -VTLVDCPGHASLI----RTIiggaQIIDLMMLVIDVTKGMQTQSAeclVIGQiACQKL----VVVLNKIDllAEGkrqA 144
Cdd:cd04168    65 kVNIIDTPGHMDFIaeveRSL----SVLDGAILVISAVEGVQAQTR---ILFR-LLRKLniptIIFVNKID--RAG---A 131

                         170
                  ....*....|....*
gi 2289442737 145 AIDKMTKKMQKTLEN 159
Cdd:cd04168   132 DLEKVYQEIKEKLSP 146
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
 84-196 4.06e-05

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: 42.80  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  84 SLIRTIiggaQII---DLMMLVIDVTKGMQTQSAEclVIGQIACQK--LVVVLNKIDLLaeGKRQAAIDKMTKKMQKTLe 158
Cdd:cd01895    74 SVLRTL----KAIeraDVVLLVLDASEGITEQDLR--IAGLILEEGkaLIIVVNKWDLV--EKDEKTMKEFEKELRRKL- 144

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2289442737 159 nTKFRGAPIIPVAAKPGgpeapeteapQGISELIELLK 196
Cdd:cd01895   145 -PFLDYAPIVFISALTG----------QGVDKLFDAIK 171
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 210-244 6.03e-05

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: 40.67  E-value: 6.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2289442737 210 FLMSVDHCFSIKGQGTVMTGTILSGTISLGDSVEI 244
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLL 35
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 97-216 7.91e-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: 43.51  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  97 DLMMLVIDVTKGMQTQSAEclVIGQIACQKLVVVLNKIDLLAEgkrqaaidkmtkkmqKTLENTKFRGAPIIPVAAKPGg 176
Cdd:COG0486   294 DLVLLLLDASEPLTEEDEE--ILEKLKDKPVIVVLNKIDLPSE---------------ADGELKSLPGEPVIAISAKTG- 355

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2289442737 177 peapeteapQGISELIELLKSQISIPTRDPSGPFLMSVDH 216
Cdd:COG0486   356 ---------EGIDELKEAILELVGEGALEGEGVLLTNARH 386
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
 84-194 1.99e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 42.34  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  84 SLIRTIiggaQII---DLMMLVIDVTKGMQTQSAecLVIGQIACQK--LVVVLNKIDLLAEGKRQAAIDKMTKKMQktle 158
Cdd:PRK00093  245 SVIRTL----KAIeraDVVLLVIDATEGITEQDL--RIAGLALEAGraLVIVVNKWDLVDEKTMEEFKKELRRRLP---- 314

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2289442737 159 ntKFRGAPIIPVAAKPGgpeapeteapQGISELIEL 194
Cdd:PRK00093  315 --FLDYAPIVFISALTG----------QGVDKLLEA 338
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 9-135 2.08e-04

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 42.40  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARALSTTASTAAFDKQPQSR---------ERGITL-DLGFSCF-------VVPLPGAEPGSSdtl 71
Cdd:PLN00116   21 NMSVIAHVDHGKSTLTDSLVAAAGIIAQEVAGDVRmtdtradeaERGITIkSTGISLYyemtdesLKDFKGERDGNE--- 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2289442737  72 LQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVTKG--MQTQSaeclVIGQIACQKL--VVVLNKID 135
Cdd:PLN00116   98 YLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGvcVQTET----VLRQALGERIrpVLTVNKMD 161
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 9-199 2.35e-04

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 40.99  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARAL--------STTASTAAfdkqpqsrergITLdLGFSCfvvplpgaepgssdtLLQVTLVDCP 80
Cdd:cd09912     2 LLAVVGEFSAGKSTLLNALlgeevlptGVTPTTAV-----------ITV-LRYGL---------------LKGVVLVDTP 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  81 G-------HASLIRTIIGGAqiiDLMMLVIDVTKGMqTQSaECLVIGQIA---CQKLVVVLNKIDLLAEGKRQAAIDKMT 150
Cdd:cd09912    55 GlnstiehHTEITESFLPRA---DAVIFVLSADQPL-TES-EREFLKEILkwsGKKIFFVLNKIDLLSEEELEEVLEYSR 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2289442737 151 KKMQKTLENTKFrgAPIIPVAAKPG----GPEAPETEAPQGISELIELLKSQI 199
Cdd:cd09912   130 EELGVLELGGGE--PRIFPVSAKEAlearLQGDEELLEQSGFEELEEHLEEFL 180
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 10-242 2.61e-04

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 41.92  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  10 VGVLGHIDSGKTALARALSTT--ASTAAfdkqpqsreRGITLDLGfsCFVVPLPGAepgssdtllQVTLVDCPGHASL-- 85
Cdd:COG0532     7 VTVMGHVDHGKTSLLDAIRKTnvAAGEA---------GGITQHIG--AYQVETNGG---------KITFLDTPGHEAFta 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  86 --IRtiigGAQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDllaegKRQAAIDK-MTKKMQKTLENTKF 162
Cdd:COG0532    67 mrAR----GAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKID-----KPGANPDRvKQELAEHGLVPEEW 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737 163 RG-APIIPVAAKPGgpeapeteapQGISELIE--LLKSQI----SIPTRDPSGPFL-MSVDhcfsiKGQGTVMTGTILSG 234
Cdd:COG0532   138 GGdTIFVPVSAKTG----------EGIDELLEmiLLQAEVlelkANPDRPARGTVIeAKLD-----KGRGPVATVLVQNG 202


                  ....*...
gi 2289442737 235 TISLGDSV 242
Cdd:COG0532   203 TLKVGDIV 210
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 97-216 5.22e-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: 40.54  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  97 DLMMLVIDVTKGmQTQSAECLVIGQIACQKLVVVLNKIDLLaegkrqaaidkmtkkmQKTLENTKFRGAPIIPVAAKPGg 176
Cdd:pfam12631 175 DLVLLVLDASRP-LDEEDLEILELLKDKKPIIVVLNKSDLL----------------GEIDELEELKGKPVLAISAKTG- 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2289442737 177 peapeteapQGISELIELLKSQISIPTRDPSGPFLMSVDH 216
Cdd:pfam12631 237 ---------EGLDELEEAIKELFLAGEIASDGPIITNARH 267
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 9-133 1.20e-03

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 37.60  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARALSTTASTAAfdKQPqsrerGITLDLgfSCFVVPLPGAepgssdtllQVTLVDCPGhasLIRT 88
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVS--DYP-----GTTRDP--NEGRLELKGK---------QIILVDTPG---LIEG 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2289442737  89 IIGGAQII---------DLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNK 133
Cdd:pfam01926  60 ASEGEGLGraflaiieaDLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 97-197 1.52e-03

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: 38.24  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  97 DLMMLVIDVTKGMQTQSAEclVIGQIACQKLVVVLNKIDLLAEGKRQAAIDkmtkkmqktlentkfrGAPIIPVAAKPGg 176
Cdd:cd04164    84 DLVLLVVDASEGLDEEDLE--ILELPAKKPVIVVLNKSDLLSDAEGISELN----------------GKPIIAISAKTG- 144

                          90       100
                  ....*....|....*....|.
gi 2289442737 177 peapeteapQGISELIELLKS 197
Cdd:cd04164   145 ---------EGIDELKEALLE 156
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
97-197 4.20e-03

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 38.17  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  97 DLMMLVIDVTKGMQTQSAEclVIGQIACQKLVVVLNKIDLLAEgkrqaaidkmtkkmqktLENTKFRGAPIIPVAAKPGg 176
Cdd:PRK05291  296 DLVLLVLDASEPLTEEDDE--ILEELKDKPVIVVLNKADLTGE-----------------IDLEEENGKPVIRISAKTG- 355

                          90       100
                  ....*....|....*....|.
gi 2289442737 177 peapeteapQGISELIELLKS 197
Cdd:PRK05291  356 ---------EGIDELREAIKE 367
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 128-201 4.82e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.38  E-value: 4.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289442737 128 VVVLNKIDLLAEGKRQAAIDKMTKkmqktlentkfRGAPIIPVAAKpggpeapeteAPQGISELIELLKSQISI 201
Cdd:cd01854    37 VIVLNKADLVDDEELEELLEIYEK-----------LGYPVLAVSAK----------TGEGLDELRELLKGKTSV 89
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
 9-151 5.40e-03

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 37.27  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737   9 NVGVLGHIDSGKTALARALST--------TASTAAFdKQPQSRERG----ITLD-LGFSC--FVVPLPGAEPGSSDTLLQ 73
Cdd:cd04165     1 RVAVVGNVDAGKSTLLGVLTQgeldngrgKARLNLF-RHKHEVESGrtssVSNDiLGFDSdgEVVNYPDNHLGELDVEIC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2289442737  74 ------VTLVDCPGHASLIRTIIGG--AQIIDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVVLNKIDLLAEGKRQAA 145
Cdd:cd04165    80 eksskvVTFIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKIDMTPANVLQET 159


                  ....*.
gi 2289442737 146 IDKMTK 151
Cdd:cd04165   160 LKDLKR 165
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 126-197 8.02e-03

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 35.89  E-value: 8.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2289442737 126 KLVVVLNKIDLLAegKRQAAIDkmTKKMQKTLentkfrGAPIIPVAAKPGgpeapeteapQGISELIELLKS 197
Cdd:cd01879   104 PVVVALNMIDEAE--KRGIKID--LDKLSELL------GVPVVPTSARKG----------EGIDELLDAIAK 155
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 96-169 8.47e-03

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: 36.08  E-value: 8.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2289442737  96 IDLMMLVIDVTKGMQTQSAECLVIGQIACQKLVVvLNKIDLLAEGKRQAAIDKMTKKMQktlentkfRGAPIIP 169
Cdd:pfam02492 115 LDGVITVVDAANEADGEKIPRKAGDQIAFADLIV-LNKTDLAPEVALLEVLEEDLRRLN--------PGAPVVP 179
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
 9-48 8.77e-03

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


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 36.70  E-value: 8.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2289442737   9 NVGVLGHIDSGKTALA-RALSTTAST----------AAFDKQPQSRERGIT 48
Cdd:cd01886     1 NIGIIAHIDAGKTTTTeRILYYTGRIhkigevhgggATMDWMEQERERGIT 51
 
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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