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Conserved domains on  [gi|34147814|gb|AAQ62485|]
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elongation factor-1 alpha, partial [Megalodoras uranoscopus]

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 ...
 1-257 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: 505.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:PTZ00141 188 VPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEAGSFNAQVIIL 160
Cdd:PTZ00141 256 ETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVL 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:PTZ00141 336 NHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVR 415

                        250
                 ....*....|....*..
gi 34147814  241 DMRQTVAVGVIKSVEKK 257
Cdd:PTZ00141 416 DMKQTVAVGVIKSVEKK 432
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-257 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 505.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:PTZ00141 188 VPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEAGSFNAQVIIL 160
Cdd:PTZ00141 256 ETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVL 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:PTZ00141 336 NHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVR 415

                        250
                 ....*....|....*..
gi 34147814  241 DMRQTVAVGVIKSVEKK 257
Cdd:PTZ00141 416 DMKQTVAVGVIKSVEKK 432
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-257 6.66e-135

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: 386.91  E-value: 6.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814     1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:TIGR00483 182 VPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRV 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNdPPQEAGSFNAQVIIL 160
Cdd:TIGR00483 250 ETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVL 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:TIGR00483 329 QHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIR 408

                         250
                  ....*....|....*..
gi 34147814   241 DMRQTVAVGVIKSVEKK 257
Cdd:TIGR00483 409 DMGQTVAAGMIIDVDPT 425
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-257 1.37e-132

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: 380.82  E-value: 1.37e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:COG5256 179 IPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRV 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNdPPQEAGSFNAQVIIL 160
Cdd:COG5256 247 ETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVL 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:COG5256 326 QHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIR 405

                       250
                ....*....|....*..
gi 34147814 241 DMRQTVAVGVIKSVEKK 257
Cdd:COG5256 406 DMGQTVAAGVVLDVKPK 422
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 149-251 6.37e-73

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: 217.83  E-value: 6.37e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 149 EAGSFNAQVIILNHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESF 228
Cdd:cd03705   2 EAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETF 81

                        90       100
                ....*....|....*....|...
gi 34147814 229 STYPPLGRFAVRDMRQTVAVGVI 251
Cdd:cd03705  82 SEYPPLGRFAVRDMRQTVAVGVI 104
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 146-254 1.38e-37

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: 127.77  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   146 PPQEAGSFNAQVIILNH-----PGQISQGYAPVLDCHTAHIACKFAELKEKIDrrSGKKLEdNPKNLKSGDAAIVEMIPG 220
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 34147814   221 KPMCVESFStypplgRFAVRDMRQTVAVGVIKSV 254
Cdd:pfam03143  78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-257 0e+00

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 505.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:PTZ00141 188 VPFIPISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEAGSFNAQVIIL 160
Cdd:PTZ00141 256 ETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVL 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:PTZ00141 336 NHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENPKAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRFAVR 415

                        250
                 ....*....|....*..
gi 34147814  241 DMRQTVAVGVIKSVEKK 257
Cdd:PTZ00141 416 DMKQTVAVGVIKSVEKK 432
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-257 6.66e-135

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: 386.91  E-value: 6.66e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814     1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:TIGR00483 182 VPFIPISAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRV 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNdPPQEAGSFNAQVIIL 160
Cdd:TIGR00483 250 ETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVSKKDIRRGDVCGHPDN-PPKVAKEFTAQIVVL 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:TIGR00483 329 QHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQFLKTGDAAIVKFKPTKPMVIEAVKEIPPLGRFAIR 408

                         250
                  ....*....|....*..
gi 34147814   241 DMRQTVAVGVIKSVEKK 257
Cdd:TIGR00483 409 DMGQTVAAGMIIDVDPT 425
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-257 5.44e-134

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 385.60  E-value: 5.44e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:PLN00043 188 IPFVPISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRV 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEAGSFNAQVIIL 160
Cdd:PLN00043 256 ETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIM 335

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:PLN00043 336 NHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSEYPPLGRFAVR 415

                        250
                 ....*....|....*..
gi 34147814  241 DMRQTVAVGVIKSVEKK 257
Cdd:PLN00043 416 DMRQTVAVGVIKSVEKK 432
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-257 1.37e-132

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: 380.82  E-value: 1.37e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:COG5256 179 IPFIPVSAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRV 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNdPPQEAGSFNAQVIIL 160
Cdd:COG5256 247 ETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDN-PPTVAEEFTAQIVVL 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:COG5256 326 QHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQFLKTGDAAIVKIKPTKPLVIEKFKEFPQLGRFAIR 405

                       250
                ....*....|....*..
gi 34147814 241 DMRQTVAVGVIKSVEKK 257
Cdd:COG5256 406 DMGQTVAAGVVLDVKPK 422
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-257 6.99e-132

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 379.27  E-value: 6.99e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFKGwkierkegnasgTTLLEALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRV 80
Cdd:PRK12317 180 IPFIPVSAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRV 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   81 ETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNVAGdSKNDPPQEAGSFNAQVIIL 160
Cdd:PRK12317 248 ETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVL 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  161 NHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTYPPLGRFAVR 240
Cdd:PRK12317 327 QHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQFIKTGDAAIVKIKPTKPLVIEKVKEIPQLGRFAIR 406

                        250
                 ....*....|....*..
gi 34147814  241 DMRQTVAVGVIKSVEKK 257
Cdd:PRK12317 407 DMGQTIAAGMVIDVKPA 423
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 149-251 6.37e-73

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: 217.83  E-value: 6.37e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 149 EAGSFNAQVIILNHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESF 228
Cdd:cd03705   2 EAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVETF 81

                        90       100
                ....*....|....*....|...
gi 34147814 229 STYPPLGRFAVRDMRQTVAVGVI 251
Cdd:cd03705  82 SEYPPLGRFAVRDMRQTVAVGVI 104
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 55-145 4.34e-63

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: 192.40  E-value: 4.34e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  55 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIR 134
Cdd:cd03693   1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                        90
                ....*....|.
gi 34147814 135 RGNVAGDSKND 145
Cdd:cd03693  81 RGDVAGDSKND 91
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 146-254 1.38e-37

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: 127.77  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   146 PPQEAGSFNAQVIILNH-----PGQISQGYAPVLDCHTAHIACKFAELKEKIDrrSGKKLEdNPKNLKSGDAAIVEMIPG 220
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSE-NPEFVMPGDNVIVTVELI 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 34147814   221 KPMCVESFStypplgRFAVRDMRQTVAVGVIKSV 254
Cdd:pfam03143  78 KPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-254 2.04e-37

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: 135.99  E-value: 2.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   1 VAFVPISGWHGDNMLEPSSNMGWFKgwkierkegnasGTTLLEALDAILPPSRPTDKPLRLPLQDVYKiggigtvP---- 76
Cdd:COG2895 187 ITFIPISALKGDNVVERSENMPWYD------------GPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------Pnldf 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  77 ---VGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGF----NVknvsvkDIRRGNVAGDSkNDPPQE 149
Cdd:COG2895 248 rgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLtledEI------DISRGDVIVAA-DAPPEV 320

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 150 AGSFNAQVIILN-HPGQISQGYapVLDCHTAHIACKFAELKEKIDRRSGKKLEdnPKNLKSGDAAIVEMIPGKPMCVESF 228
Cdd:COG2895 321 ADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVNTLEHEA--ADSLELNDIGRVTLRLAEPIAFDPY 396

                       250       260
                ....*....|....*....|....*...
gi 34147814 229 STYPPLGRFAV--RDMRQTVAVGVIKSV 254
Cdd:COG2895 397 ADNRATGSFILidRLTNATVGAGMIRGA 424
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 152-251 9.00e-33

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: 115.18  E-value: 9.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 152 SFNAQVIILNHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKleDNPKNLKSGDAAIVEMIPGKPMCVESFSTY 231
Cdd:cd01513   5 KFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEK--KPPDSLQPGENGTVEVELQKPVVLERGKEF 82

                        90       100
                ....*....|....*....|
gi 34147814 232 PPLGRFAVRDMRQTVAVGVI 251
Cdd:cd01513  83 PTLGRFALRDGGRTVGAGLI 102
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 153-251 1.12e-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: 94.54  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 153 FNAQVIILNHPGQI-SQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCVESFSTY 231
Cdd:cd03704   6 FEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETFKDF 85

                        90       100
                ....*....|....*....|
gi 34147814 232 PPLGRFAVRDMRQTVAVGVI 251
Cdd:cd03704  86 PQLGRFTLRDEGKTIAIGKV 105
PLN03126 PLN03126
Elongation factor Tu; Provisional
 41-254 5.18e-22

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 94.30  E-value: 5.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHESLPEATP 117
Cdd:PLN03126 271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALA 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  118 GDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEagSFNAQVIILNHP--GQIS---QGYAPVLDCHTAHIACKFAELKEKI 192
Cdd:PLN03126 351 GDNVGLLLRGIQKADIQRGMVLAKPGSITPHT--KFEAIVYVLKKEegGRHSpffAGYRPQFYMRTTDVTGKVTSIMNDK 428

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34147814  193 DRRSgkklednpKNLKSGDAA--IVEMIpgKPMCVESFStypplgRFAVRDMRQTVAVGVIKSV 254
Cdd:PLN03126 429 DEES--------KMVMPGDRVkmVVELI--VPVACEQGM------RFAIREGGKTVGAGVIQSI 476
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 146-254 1.15e-21

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: 86.44  E-value: 1.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 146 PPQEAGSFNAQVIILNHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKNLKSGDAAIVEMIPGKPMCV 225
Cdd:cd04093   1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80

                        90       100
                ....*....|....*....|....*....
gi 34147814 226 ESFSTYPPLGRFAVRDMRQTVAVGVIKSV 254
Cdd:cd04093  81 ETFKDNKELGRFVLRRGGETIAAGIVTEI 109
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 59-138 7.25e-21

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: 83.47  E-value: 7.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  59 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNvsVKDIRRGNV 138
Cdd:cd01342   1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
PLN03127 PLN03127
Elongation factor Tu; Provisional
 41-254 9.92e-21

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 90.65  E-value: 9.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAP-VNVTTEVKSVEMHHESLPEA 115
Cdd:PLN03127 243 LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQG 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  116 TPGDNVGFNVKNVSVKDIRRGNVAgdSKNDPPQEAGSFNAQVIILN------HPGQISQgYAPVLDCHTAHIACKFaelk 189
Cdd:PLN03127 323 QAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLTkdeggrHTPFFSN-YRPQFYLRTADVTGKV---- 395

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34147814  190 ekidrrsgkKLEDNPKNLKSGD--AAIVEMIpgKPMCVEsfstypPLGRFAVRDMRQTVAVGVIKSV 254
Cdd:PLN03127 396 ---------ELPEGVKMVMPGDnvTAVFELI--SPVPLE------PGQRFALREGGRTVGAGVVSKV 445
tufA CHL00071
elongation factor Tu
 40-251 2.53e-20

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 88.86  E-value: 2.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   40 TLLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVT--TEVKSVEMHHESLPEAT 116
Cdd:CHL00071 201 NLMDAVDSYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETktTTVTGLEMFQKTLDEGL 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  117 PGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEagSFNAQVIILN------HPGqISQGYAPVLDCHTAHIACKFaelke 190
Cdd:CHL00071 281 AGDNVGILLRGIQKEDIERGMVLAKPGTITPHT--KFEAQVYILTkeeggrHTP-FFPGYRPQFYVRTTDVTGKI----- 352

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34147814  191 kidrrsgkklednpKNLKSGDAAIVEMI-PGK--PMCVESFStypPLG-----RFAVRDMRQTVAVGVI 251
Cdd:CHL00071 353 --------------ESFTADDGSKTEMVmPGDriKMTVELIY---PIAiekgmRFAIREGGRTVGAGVV 404
PRK12735 PRK12735
elongation factor Tu; Reviewed
 41-160 4.24e-20

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 88.36  E-value: 4.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHESLPEAT 116
Cdd:PRK12735 194 LMDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQ 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 34147814  117 PGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEagSFNAQVIIL 160
Cdd:PRK12735 273 AGDNVGVLLRGTKREDVERGQVLAKPGSIKPHT--KFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 41-256 4.91e-20

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 88.08  E-value: 4.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVnVTTEVKSVEMHHESLPEAT 116
Cdd:PRK12736 192 LMDAVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQ 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  117 PGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEagSFNAQVIILN------HPGQISqGYAPVLDCHTAhiackfaelke 190
Cdd:PRK12736 271 AGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHT--KFKAEVYILTkeeggrHTPFFN-NYRPQFYFRTT----------- 336

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34147814  191 kiDRRSGKKLEDNPKNLKSGDAA--IVEMIpgKPMCVESFStypplgRFAVRDMRQTVAVGVIKSVEK 256
Cdd:PRK12736 337 --DVTGSIELPEGTEMVMPGDNVtiTVELI--HPIAMEQGL------KFAIREGGRTVGAGTVTEILD 394
PRK00049 PRK00049
elongation factor Tu; Reviewed
 41-138 6.49e-20

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 87.94  E-value: 6.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPVNVTTeVKSVEMHHESLPEAT 116
Cdd:PRK00049 194 LMDAVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQ 272

                         90       100
                 ....*....|....*....|..
gi 34147814  117 PGDNVGFNVKNVSVKDIRRGNV 138
Cdd:PRK00049 273 AGDNVGALLRGIKREDVERGQV 294
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 41-254 7.18e-20

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: 87.53  E-value: 7.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTE--VKSVEMHHESLPEATP 117
Cdd:TIGR00485 192 LMDAVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKttVTGVEMFRKELDEGRA 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   118 GDNVGFNVKNVSVKDIRRGNVAGDSKNDPPQEagSFNAQVIILN------HPGQISqGYAPVLDCHTAHIACKFaelkek 191
Cdd:TIGR00485 272 GDNVGLLLRGIKREEIERGMVLAKPGSIKPHT--KFEAEVYVLSkeeggrHTPFFS-GYRPQFYFRTTDVTGTI------ 342

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34147814   192 idrrsgkKLEDNPKNLKSGD--AAIVEMIpgKPMCVESFStypplgRFAVRDMRQTVAVGVIKSV 254
Cdd:TIGR00485 343 -------ELPEGVEMVMPGDnvKMTVELI--SPIALEQGM------RFAIREGGRTVGAGVVSKI 392
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 41-138 2.65e-19

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: 85.97  E-value: 2.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  41 LLEALDAILP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAPvNVTTEVKSVEMHHESLPEAT 116
Cdd:COG0050 194 LMDAVDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGIRD-TQKTVVTGVEMFRKLLDEGE 272

                        90       100
                ....*....|....*....|..
gi 34147814 117 PGDNVGFNVKNVSVKDIRRGNV 138
Cdd:COG0050 273 AGDNVGLLLRGIKREDVERGQV 294
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-251 2.49e-18

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 83.83  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFkgwkierkegnaSGTTLLEALDAILPPSRPTDKPLRLPLQDVYKI-----GGIGTv 75
Cdd:PRK05506 196 VTFIPISALKGDNVVTRSARMPWY------------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT- 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   76 pvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVgfnvkNVSVKD---IRRGNVAGDSkNDPPQEAGS 152
Cdd:PRK05506 263 ----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV-----TLTLADeidISRGDMLARA-DNRPEVADQ 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  153 FNAQVIILN----HPGqisQGYapVLDCHTAHIACKFAELKEKID-----RRSGKKLEDNpknlksgDAAIVEMIPGKPM 223
Cdd:PRK05506 333 FDATVVWMAeeplLPG---RPY--LLKHGTRTVPASVAAIKYRVDvntleRLAAKTLELN-------EIGRCNLSTDAPI 400

                        250       260       270
                 ....*....|....*....|....*....|
gi 34147814  224 CVESFSTYPPLGRFAV--RDMRQTVAVGVI 251
Cdd:PRK05506 401 AFDPYARNRTTGSFILidRLTNATVGAGMI 430
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 61-138 8.91e-18

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: 75.63  E-value: 8.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  61 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN--VTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNV 138
Cdd:cd03697   3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKetLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 59-138 5.63e-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: 73.33  E-value: 5.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  59 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNV 138
Cdd:cd03696   1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 73-138 1.71e-16

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: 71.91  E-value: 1.71e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34147814    73 GTVPVGRVETGVLKPGMVVTFAPVNV-----TTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNV 138
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 41-251 1.25e-15

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: 76.11  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  41 LLEALDAIL--PPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPG 118
Cdd:COG3276 157 LRAALDALAaaVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAG 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 119 DNVGFNVKNVSVKDIRRGNVAgdSKNDPPQEAGSFNAQVIILNHPGQ-ISQGyAPVLdCH--TAHIACKFAELkekidrr 195
Cdd:COG3276 237 QRVALNLAGVEKEEIERGDVL--AAPGALRPTDRIDVRLRLLPSAPRpLKHW-QRVH-LHhgTAEVLARVVLL------- 305

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34147814 196 sgkkledNPKNLKSGDAAIVEMIPGKPMCVEsfstyppLG-RFAVRDM--RQTVAVGVI 251
Cdd:COG3276 306 -------DREELAPGEEALAQLRLEEPLVAA-------RGdRFILRDYspRRTIGGGRV 350
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 58-141 2.36e-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: 66.38  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  58 PLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGN 137
Cdd:cd16267   1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80


                ....
gi 34147814 138 VAGD 141
Cdd:cd16267  81 ILCD 84
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-51 5.99e-14

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: 68.67  E-value: 5.99e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 34147814   1 VAFVPISGWHGDNMLEPSSNMGWFKGWkierkegnasgtTLLEALDAILPP 51
Cdd:cd01883 180 VPFIPISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPP 218
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 58-138 5.93e-13

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: 62.50  E-value: 5.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  58 PLRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGN 137
Cdd:cd04089   1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                .
gi 34147814 138 V 138
Cdd:cd04089  79 V 79
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-253 2.40e-12

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 66.09  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814    1 VAFVPISGWHGDNMLEPSSNMGWFkgwkierkegnaSGTTLLEALDAILPPSRPTDKPLRLPLQDVYKI-----GGIGTv 75
Cdd:PRK05124 200 IRFVPLSALEGDNVVSQSESMPWY------------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT- 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814   76 pvgrVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKNVSvkDIRRGNVAGDSkNDPPQEAGSFNA 155
Cdd:PRK05124 267 ----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLEDEI--DISRGDLLVAA-DEALQAVQHASA 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  156 QVIILN-HPGQISQGYapvldchTAHIACKF-----AELKEKIDRRSGKKLEdnPKNLKSGDAAIVEMIPGKPMCVESFS 229
Cdd:PRK05124 340 DVVWMAeQPLQPGQSY-------DIKIAGKKtrarvDAIRYQVDINTLTQRE--AENLPLNGIGLVELTFDEPLVLDPYQ 410

                        250       260
                 ....*....|....*....|....*.
gi 34147814  230 TYPPLGRFAV--RDMRQTVAVGVIKS 253
Cdd:PRK05124 411 QNRVTGGFIFidRLTNVTVGAGMVRE 436
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 58-141 1.17e-10

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: 56.36  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  58 PLRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMH-HESLPEATPGDNVGFNVKNVSVKDIRRG 136
Cdd:cd03698   1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                ....*
gi 34147814 137 NVAGD 141
Cdd:cd03698  80 DILSS 84
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 65-138 1.74e-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: 53.38  E-value: 1.74e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34147814  65 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVN----VTTEVKSVEMHHESLPEATPGDNVGFNVKNVSVKDIRRGNV 138
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 ...
 59-138 3.33e-09

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: 52.57  E-value: 3.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814  59 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHESLPEATPGDNVGFNVKN-VsvkDIRRGN 137
Cdd:cd03695   1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLEDeI---DVSRGD 77


                .
gi 34147814 138 V 138
Cdd:cd03695  78 L 78
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-52 4.88e-06

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: 46.02  E-value: 4.88e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 34147814   1 VAFVPISGWHGDNMLEPSSNMGWFKgwkierkegnasGTTLLEALDAILPPS 52
Cdd:cd04166 170 ITFIPISALEGDNVVSRSENMPWYK------------GPTLLEHLETVEIAS 209
FERM_C_CCM1 cd13197
FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev ...
 206-242 4.10e-05

FERM domain C-lobe of Cerebral cavernous malformation 1; CCM1 (also called KRIT-1/Krev interaction trapped 1;ankyrin repeat-containing protein Krit1; CAM), a Rap1-binding protein, is expressed in endothelial cells where it is present in cell-cell junctions and associated with junctional proteins. Together with CCM2/MGC4607 and CCM3/PDCD10, KRIT1 constitutes a set of proteins, mutations of which are found in cerebral cavernous malformations which are characterized by cerebral hemorrhages and vascular malformations in the central nervous system. KRIT-1 possesses four ankyrin repeats, a FERM domain, and multiple NPXY sequences, one of which is essential for integrin cytoplasmic domain-associated protein-1alpha (ICAP1alpha) binding and all of which mediate binding of CCM2. KRIT-1 localization is mediated by its FERM domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270018  Cd Length: 100  Bit Score: 41.45  E-value: 4.10e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 34147814 206 NLKSGDAAIVEMIpGKPMCVESFSTYPPLGRFAVRDM 242
Cdd:cd13197  36 NMETKALLLSLKY-GCFMWQLGDADTCFQIHSLENKM 71
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 153-254 1.60e-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: 39.42  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 153 FNAQVIILNHPGQISQGYAPVLDCHTAHIACKFaelkEKIDRrsgkklednpKNLKSGDAAIVEMipgkpmcveSFSTYP 232
Cdd:cd03708   6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDK----------EVLRTGDRALVRF---------RFLYRP 62

                        90       100
                ....*....|....*....|....*.
gi 34147814 233 ----PLGRFAVRDMRqTVAVGVIKSV 254
Cdd:cd03708  63 eylrEGQRLIFREGR-TKGIGTVTKV 87
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 64-122 4.32e-04

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


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 38.04  E-value: 4.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34147814  64 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfAPVNVTTeVKSVEMHHESLPEATPGDNVG 122
Cdd:cd16265   6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKGVAL-IRAIEREHRKVDFAVAGDEVA 61
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 153-251 6.66e-03

Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 294005 [Multi-domain]  Cd Length: 93  Bit Score: 34.90  E-value: 6.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147814 153 FNAQVIILN------HPGqISQGYAPVLDCHTAHIACKFaelkekidrrsgkKLEDNPKNLKSGDAAIVEMIPGKPMCVE 226
Cdd:cd03706   6 FEAQVYLLSkeeggrHKP-FTSGFQQQMFSKTWDCACRI-------------DLPEGKEMVMPGEDTSVKLTLLKPMVLE 71

                        90       100
                ....*....|....*....|....*
gi 34147814 227 sfstypPLGRFAVRDMRQTVAVGVI 251
Cdd:cd03706  72 ------KGQRFTLREGGRTIGTGVV 90
 
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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