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Conserved domains on  [gi|1957425434|gb|QQQ16486|]
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translation elongation factor 1-alpha, partial [Occultibambusa kunmingensis]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-283 0e+00

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


The actual alignment was detected with superfamily member PTZ00141:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 446  Bit Score: 537.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMD--TTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkst 78
Cdd:PTZ00141  144 GVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG---------- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  79 gKTLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVP 158
Cdd:PTZ00141  214 -PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVP 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 159 GDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTG 238
Cdd:PTZ00141  293 GDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSG 372

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1957425434 239 KSVENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:PTZ00141  373 KVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-283 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 537.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMD--TTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkst 78
Cdd:PTZ00141  144 GVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG---------- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  79 gKTLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVP 158
Cdd:PTZ00141  214 -PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVP 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 159 GDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTG 238
Cdd:PTZ00141  293 GDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSG 372

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1957425434 239 KSVENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:PTZ00141  373 KVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-283 4.08e-159

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 449.31  E-value: 4.08e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkstgK 80
Cdd:TIGR00483 140 GINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG-----------K 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGD 160
Cdd:TIGR00483 209 TLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGD 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 161 NVGFNVKNVSVKEIRRGNVAGDSKNdPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKS 240
Cdd:TIGR00483 289 NIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQV 367

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1957425434 241 VENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:TIGR00483 368 LEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDM 410
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-283 1.28e-148

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: 422.80  E-value: 1.28e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkstgK 80
Cdd:COG5256   137 GINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG-----------P 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGD 160
Cdd:COG5256   206 TLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGD 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 161 NVGFNVKNVSVKEIRRGNVAGDSKNdPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKS 240
Cdd:COG5256   286 NIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQV 364

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1957425434 241 VENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:COG5256   365 KEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDM 407
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 189-283 3.82e-65

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


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 198.96  E-value: 3.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 189 KGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENAPKFIKSGDAAIVKMIPSKPMCVEA 268
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                          90
                  ....*....|....*
gi 1957425434 269 FTQYPPLGRFAVRDM 283
Cdd:cd03705    81 FSEYPPLGRFAVRDM 95
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 187-283 7.01e-31

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 111.20  E-value: 7.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 187 PPKGCDSFNAQVIVLNH-----PGQVGAGYAPVLDCHTAHIACKFSELLEKIDrrTGKSVENaPKFIKSGDAAIVKMIPS 261
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|..
gi 1957425434 262 KPMCVEAFTqypplgRFAVRDM 283
Cdd:pfam03143  78 KPIALEKGQ------RFAIREG 93
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-283 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 537.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMD--TTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkst 78
Cdd:PTZ00141  144 GVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG---------- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  79 gKTLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVP 158
Cdd:PTZ00141  214 -PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVP 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 159 GDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTG 238
Cdd:PTZ00141  293 GDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSG 372

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1957425434 239 KSVENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:PTZ00141  373 KVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVRDM 417
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-283 4.08e-159

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]


Pssm-ID: 129574 [Multi-domain]  Cd Length: 426  Bit Score: 449.31  E-value: 4.08e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkstgK 80
Cdd:TIGR00483 140 GINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG-----------K 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGD 160
Cdd:TIGR00483 209 TLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGD 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 161 NVGFNVKNVSVKEIRRGNVAGDSKNdPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKS 240
Cdd:TIGR00483 289 NIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQV 367

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1957425434 241 VENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:TIGR00483 368 LEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIRDM 410
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-283 1.28e-148

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: 422.80  E-value: 1.28e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkstgK 80
Cdd:COG5256   137 GINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG-----------P 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGD 160
Cdd:COG5256   206 TLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGD 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 161 NVGFNVKNVSVKEIRRGNVAGDSKNdPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKS 240
Cdd:COG5256   286 NIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQV 364

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1957425434 241 VENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:COG5256   365 KEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIRDM 407
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-283 3.35e-147

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 419.33  E-value: 3.35e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkstgK 80
Cdd:PRK12317  138 GINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG-----------P 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGD 160
Cdd:PRK12317  207 TLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGD 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 161 NVGFNVKNVSVKEIRRGNVAGdSKNDPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKS 240
Cdd:PRK12317  287 NIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQV 365

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1957425434 241 VENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:PRK12317  366 AEENPQFIKTGDAAIVKIKPTKPLVIEKVKEIPQLGRFAIRDM 408
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-283 6.36e-146

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 416.80  E-value: 6.36e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTT--KWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGweketktkst 78
Cdd:PLN00043  144 GVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG---------- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  79 gKTLLEAIDAIDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVP 158
Cdd:PLN00043  214 -PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALP 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 159 GDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTG 238
Cdd:PLN00043  293 GDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSG 372

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1957425434 239 KSVENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRDM 283
Cdd:PLN00043  373 KELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYPPLGRFAVRDM 417
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 189-283 3.82e-65

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


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 198.96  E-value: 3.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 189 KGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENAPKFIKSGDAAIVKMIPSKPMCVEA 268
Cdd:cd03705     1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                          90
                  ....*....|....*
gi 1957425434 269 FTQYPPLGRFAVRDM 283
Cdd:cd03705    81 FSEYPPLGRFAVRDM 95
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 96-186 5.99e-61

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 187.78  E-value: 5.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  96 SDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIR 175
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                          90
                  ....*....|.
gi 1957425434 176 RGNVAGDSKND 186
Cdd:cd03693    81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-278 8.18e-52

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 174.89  E-value: 8.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTvpFVPISGFNGDNMIEVSSNCPWYKgweketktkstGK 80
Cdd:COG2895   147 GIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWYD-----------GP 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKiggigtvP-------VGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQL 153
Cdd:COG2895   214 TLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDL 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 154 SEGVPGDNVGFNVK---NVSvkeirRGNVAGDSkNDPPKGCDSFNAQVIVLN-HPGQVGAGYapVLDCHTAHIACKFSEL 229
Cdd:COG2895   287 EEAFAGQSVTLTLEdeiDIS-----RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAI 358

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1957425434 230 LEKIDRRTGKsvENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRF 278
Cdd:COG2895   359 KYRIDVNTLE--HEAADSLELNDIGRVTLRLAEPIAFDPYADNRATGSF 405
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-92 6.00e-42

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: 143.40  E-value: 6.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTT--KWSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIEVSSNCPWYKGWeketktkst 78
Cdd:cd01883   136 GVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP--------- 206

                          90
                  ....*....|....
gi 1957425434  79 gkTLLEAIDAIDTP 92
Cdd:cd01883   207 --TLLEALDSLEPP 218
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 187-283 7.01e-31

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 111.20  E-value: 7.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 187 PPKGCDSFNAQVIVLNH-----PGQVGAGYAPVLDCHTAHIACKFSELLEKIDrrTGKSVENaPKFIKSGDAAIVKMIPS 261
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77

                          90       100
                  ....*....|....*....|..
gi 1957425434 262 KPMCVEAFTqypplgRFAVRDM 283
Cdd:pfam03143  78 KPIALEKGQ------RFAIREG 93
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 1-282 7.63e-31

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 119.01  E-value: 7.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGynPKTVPFVPISGFNGDNMIEVSSNCPWYkgweketktksTGK 80
Cdd:TIGR02034 132 GIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY-----------SGP 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKI-----GGIGTVPVGRVETgvikaGMVVTFAPAGVTTEVKSVEMHHEQLSE 155
Cdd:TIGR02034 199 TLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHV-----GDEVVVLPSGRSSRVARIVTFDGDLEQ 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 156 GVPGDNVGFNVKNVSvkEIRRGN--VAGDSkndPPKGCDSFNAQVIVL-NHPGQVGAGYapVLDCHTAHIACKFSELLEK 232
Cdd:TIGR02034 274 ARAGQAVTLTLDDEI--DISRGDllAAADS---APEVADQFAATLVWMaEEPLLPGRSY--DLKLGTRKVRASVAAIKHK 346

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1957425434 233 IDRRTGKsvENAPKFIKSGDAAIVKMIPSKPMCVEAFTQYPPLGRFAVRD 282
Cdd:TIGR02034 347 VDVNTLE--KGAAKSLELNEIGRVNLSLDEPIAFDPYAENRTTGAFILID 394
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-199 2.70e-28

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 112.70  E-value: 2.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPkTVPFVPISGFNGDNMIEVSSNCPWYKgweketktkstGK 80
Cdd:PRK05124  159 GIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYS-----------GP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSE 155
Cdd:PRK05124  227 TLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEE 301

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1957425434 156 GVPGDNVGFNVKNvsvkE--IRRGNVAGDSKNDPPKGcDSFNAQVI 199
Cdd:PRK05124  302 AFAGEAITLVLED----EidISRGDLLVAADEALQAV-QHASADVV 342
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 189-283 6.47e-27

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


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 100.93  E-value: 6.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 189 KGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKsvENAPKFIKSGDAAIVKMIPSKPMCVEA 268
Cdd:cd01513     1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKE--KKPPDSLQPGENGTVEVELQKPVVLER 78

                          90
                  ....*....|....*
gi 1957425434 269 FTQYPPLGRFAVRDM 283
Cdd:cd01513    79 GKEFPTLGRFALRDG 93
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-199 1.22e-26

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 108.86  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNpkTVPFVPISGFNGDNMIEVSSNCPWYkgweketktksTGK 80
Cdd:PRK05506  156 GIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY-----------EGP 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 TLLEAIDAIDTPTRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSE 155
Cdd:PRK05506  223 SLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDE 297

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1957425434 156 GVPGDNVgfnvkNVSVK---EIRRGNVAGDSkNDPPKGCDSFNAQVI 199
Cdd:PRK05506  298 AFAGQAV-----TLTLAdeiDISRGDMLARA-DNRPEVADQFDATVV 338
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 191-282 6.05e-24

C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 93.00  E-value: 6.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 191 CDSFNAQVIVLNHPGQV-GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENAPKFIKSGDAAIVKMIPSKPMCVEAF 269
Cdd:cd03704     3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETF 82

                          90
                  ....*....|...
gi 1957425434 270 TQYPPLGRFAVRD 282
Cdd:cd03704    83 KDFPQLGRFTLRD 95
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-201 6.26e-24

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: 99.84  E-value: 6.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTkwsEDrfQEIIK----ETSNFIKKVGYNPKTVPFVPISGFNGdnmIEVSSNCPWYKGWEKetktk 76
Cdd:COG0050   127 GVPYIVVFLNKCDMV---DD--EELLElvemEVRELLSKYGFPGDDTPIIRGSALKA---LEGDPDPEWEKKILE----- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  77 stgktLLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAgVTTEVKSVEMHHEQ 152
Cdd:COG0050   194 -----LMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKL 267

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1957425434 153 LSEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGCDSFNAQVIVL 201
Cdd:COG0050   268 LDEGEAGDNVGLLLRGIKREDVERGQVL--AKPGSITPHTKFEAEVYVL 314
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-90 1.44e-22

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: 92.63  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEDRFQEIIKETSNFIKKVGYNPKTvpFVPISGFNGDNMIEVSSNCPWYKgweketktkstGK 80
Cdd:cd04166   130 GIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWYK-----------GP 196

                          90
                  ....*....|
gi 1957425434  81 TLLEAIDAID 90
Cdd:cd04166   197 TLLEHLETVE 206
tufA CHL00071
elongation factor Tu
 1-202 1.92e-22

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 95.79  E-value: 1.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDttKWSEDRFQEIIK-ETSNFIKKVGYNPKTVPFVPISGFNGDNmiEVSSNCPWYKGwekETKTKSTG 79
Cdd:CHL00071  127 GVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVSGSALLALE--ALTENPKIKRG---ENKWVDKI 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  80 KTLLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVT---FAPAGVTTeVKSVEMHHEQLSE 155
Cdd:CHL00071  200 YNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDE 278

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1957425434 156 GVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKgcDSFNAQVIVLN 202
Cdd:CHL00071  279 GLAGDNVGILLRGIQKEDIERGMVLAKPGTITPH--TKFEAQVYILT 323
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-179 2.40e-22

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 95.40  E-value: 2.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTkwSEDRFQEIIK-ETSNFIKKVGYNPKTVPFVPISGF---NGDNmievssncPWYKGWEKetktk 76
Cdd:PRK12736  127 GVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDDIPVIRGSALkalEGDP--------KWEDAIME----- 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  77 stgktLLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAgVTTEVKSVEMHHEQ 152
Cdd:PRK12736  192 -----LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKL 265

                         170       180
                  ....*....|....*....|....*..
gi 1957425434 153 LSEGVPGDNVGFNVKNVSVKEIRRGNV 179
Cdd:PRK12736  266 LDEGQAGDNVGVLLRGVDRDEVERGQV 292
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-179 3.85e-22

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 94.87  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTtkwSEDrfQEIIK----ETSNFIKKVGYNPKTVPFVPISGFNGdnmIEVSSNCPWYKGWEKetktk 76
Cdd:PRK00049  127 GVPYIVVFLNKCDM---VDD--EELLElvemEVRELLSKYDFPGDDTPIIRGSALKA---LEGDDDEEWEKKILE----- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  77 stgktLLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAGVTTeVKSVEMHHEQ 152
Cdd:PRK00049  194 -----LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKL 267

                         170       180
                  ....*....|....*....|....*..
gi 1957425434 153 LSEGVPGDNVGFNVKNVSVKEIRRGNV 179
Cdd:PRK00049  268 LDEGQAGDNVGALLRGIKREDVERGQV 294
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-202 1.36e-20

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 90.65  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKWSEdrFQEI----IKETSNFIKkvgynpktvpfvpisgFNGDNM-IEVSSNCPWYKGWEKETKT 75
Cdd:PLN03127  176 GVPSLVVFLNKVDVVDDEE--LLELvemeLRELLSFYK----------------FPGDEIpIIRGSALSALQGTNDEIGK 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  76 KSTGKtLLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAG-VTTEVKSVEMHH 150
Cdd:PLN03127  238 NAILK-LMDAVDEyIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPGGpLKTTVTGVEMFK 316

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1957425434 151 EQLSEGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGCDSFNAQVIVLN 202
Cdd:PLN03127  317 KILDQGQAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLT 366
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-203 1.57e-20

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: 91.13  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTkwSEDRFQEIIKETSNFIKkvGYNPKTVPFVPISGFNGdnmievssncpwyKGWEKetktkstgk 80
Cdd:COG3276   103 GIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLEDAPIVPVSAVTG-------------EGIDE--------- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 tLLEAIDAI--DTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVP 158
Cdd:COG3276   157 -LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYA 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1957425434 159 GDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGCDSFNAQVIVLNH 203
Cdd:COG3276   236 GQRVALNLAGVEKEEIERGDVL--AAPGALRPTDRIDVRLRLLPS 278
PRK12735 PRK12735
elongation factor Tu; Reviewed
 82-179 3.44e-20

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 89.13  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  82 LLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAGVTTeVKSVEMHHEQLSEGV 157
Cdd:PRK12735  194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQ 272

                          90       100
                  ....*....|....*....|..
gi 1957425434 158 PGDNVGFNVKNVSVKEIRRGNV 179
Cdd:PRK12735  273 AGDNVGVLLRGTKREDVERGQV 294
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-201 3.12e-19

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: 86.37  E-value: 3.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTkwSEDRFQEIIK-ETSNFIKKVGYNPKTVPFVPISGFngdnmievssncpwyKGWEKETKTKSTG 79
Cdd:TIGR00485 127 GVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSQYDFPGDDTPIIRGSAL---------------KALEGDAEWEAKI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  80 KTLLEAIDA-IDTPTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAGVTTeVKSVEMHHEQLSE 155
Cdd:TIGR00485 190 LELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDE 268

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1957425434 156 GVPGDNVGFNVKNVSVKEIRRGNVAGDSKNDPPKgcDSFNAQVIVL 201
Cdd:TIGR00485 269 GRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPH--TKFEAEVYVL 312
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 100-179 4.73e-19

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


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 79.23  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 100 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGDNVGFNVKNvsVKEIRRGNV 179
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-282 1.33e-18

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 85.05  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKQLIVAINKMDTTKwSEDRFQEIIKETSNFIKKVGYNPKTVPFVPISGFNGdnmIEVSSNCPWYKGWEKETKTKstgk 80
Cdd:PLN03126  196 GVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPIISGSALLA---LEALMENPNIKRGDNKWVDK---- 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  81 tLLEAIDAIDT----PTRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVT--TEVKSVEMHHEQLS 154
Cdd:PLN03126  268 -IYELMDAVDSyipiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILD 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 155 EGVPGDNVGFNVKNVSVKEIRRGNVAgdSKNDPPKGCDSFNAQVIVLNHP-----GQVGAGYAPVLDCHTAHIACKFSEL 229
Cdd:PLN03126  347 EALAGDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMRTTDVTGKVTSI 424

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1957425434 230 LEKIDRRTgksvenapKFIKSGDAaiVKMIPS--KPMCVEAFTqypplgRFAVRD 282
Cdd:PLN03126  425 MNDKDEES--------KMVMPGDR--VKMVVEliVPVACEQGM------RFAIRE 463
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 187-282 8.13e-17

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 74.12  E-value: 8.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 187 PPKGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSVENAPKFIKSGDAAIVKMIPSKPMCV 266
Cdd:cd04093     1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80

                          90
                  ....*....|....*.
gi 1957425434 267 EAFTQYPPLGRFAVRD 282
Cdd:cd04093    81 ETFKDNKELGRFVLRR 96
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 100-179 2.63e-16

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: 72.17  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 100 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIRRGNV 179
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 102-179 6.24e-16

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


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 71.40  E-value: 6.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434 102 LPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFA--PAGVTTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIRRGNV 179
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 114-179 1.74e-15

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 69.60  E-value: 1.74e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957425434 114 GTVPVGRVETGVIKAGMVVTFAPAGV-----TTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIRRGNV 179
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 99-182 5.32e-14

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


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 66.00  E-value: 5.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  99 PLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIRRGN 178
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80


                  ....
gi 1957425434 179 VAGD 182
Cdd:cd16267    81 ILCD 84
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-59 1.16e-11

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: 62.16  E-value: 1.16e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434   1 GVKqLIVAINKMDTTkwSEDRFQEIIKETSN-FIKKVGYNPKTVPFVPISGFNGDNMIEV 59
Cdd:pfam00009 121 GVP-IIVFINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQTL 177
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 99-179 9.92e-11

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


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 56.72  E-value: 9.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  99 PLRLPLQDVYKigGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIRRGN 178
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                  .
gi 1957425434 179 V 179
Cdd:cd04089    79 V 79
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 99-182 1.05e-09

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation 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: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 54.04  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957425434  99 PLRLPLQDVYKiGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMH-HEQLSEGVPGDNVGFNVKNVSVKEIRRG 177
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....*
gi 1957425434 178 NVAGD 182
Cdd:cd03698    80 DILSS 84
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 106-179 1.65e-09

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: 53.76  E-value: 1.65e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957425434 106 DVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAG----VTTEVKSVEMHHEQLSEGVPGDNVGFNVKNVSVKEIRRGNV 179
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 100-164 3.63e-08

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.87  E-value: 3.63e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957425434 100 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAGVTTEVKSVEMHHEQLSEGVPGDNVGF 164
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-56 4.30e-08

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: 51.91  E-value: 4.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1957425434   1 GVKQLIVAINKMDTTKwsEDRFQEIIKETSNFIKKVGY---NPKTVPFVPISGFNGDNM 56
Cdd:cd00881   113 GGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGI 169
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 189-252 1.55e-04

Domain III of the GP-1 family of GTPases; This family 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 the 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: 294007 [Multi-domain]  Cd Length: 87  Bit Score: 39.81  E-value: 1.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1957425434 189 KGCDSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFsellEKIDR---RTGKSVE------NAPKFIKSGD 252
Cdd:cd03708     1 RACWEFEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDKevlRTGDRALvrfrflYRPEYLREGQ 69
 
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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