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Conserved domains on  [gi|338172972|gb|AEI83249|]
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translation elongation factor 1 alpha, partial [Hypogymnia tubulosa]

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 ...
 1-271 4.89e-180

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: 502.74  E-value: 4.89e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM--*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEA 78
Cdd:PTZ00141 151 CINKMddKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG-----------PTLLEA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  79 IDAIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFN 158
Cdd:PTZ00141 220 LDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFN 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 159 VKNVSVKEIRRGNVAGDSKSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAP 238
Cdd:PTZ00141 300 VKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379

                        250       260       270
                 ....*....|....*....|....*....|...
gi 338172972 239 KFIKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:PTZ00141 380 KAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRF 412
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-271 4.89e-180

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 502.74  E-value: 4.89e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM--*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEA 78
Cdd:PTZ00141 151 CINKMddKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG-----------PTLLEA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  79 IDAIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFN 158
Cdd:PTZ00141 220 LDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFN 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 159 VKNVSVKEIRRGNVAGDSKSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAP 238
Cdd:PTZ00141 300 VKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379

                        250       260       270
                 ....*....|....*....|....*....|...
gi 338172972 239 KFIKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:PTZ00141 380 KAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRF 412
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-271 2.23e-145

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: 414.26  E-value: 2.23e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972    1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:TIGR00483 147 AINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG-----------KTLLEALD 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   81 AIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVK 160
Cdd:TIGR00483 216 ALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVR 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  161 NVSVKEIRRGNVAGDSKsDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKF 240
Cdd:TIGR00483 296 GVSKKDIRRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQF 374

                         250       260       270
                  ....*....|....*....|....*....|.
gi 338172972  241 IKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:TIGR00483 375 LKTGDAAIVKFKPTKPMVIEAVKEIPPLGRF 405
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-271 3.31e-137

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: 393.14  E-value: 3.31e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:COG5256  144 AVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG-----------PTLLEALD 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVK 160
Cdd:COG5256  213 NLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVR 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 161 NVSVKEIRRGNVAGDSkSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKF 240
Cdd:COG5256  293 GVEKNDIKRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQF 371

                        250       260       270
                 ....*....|....*....|....*....|.
gi 338172972 241 IKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:COG5256  372 LKTGDAAIVKIKPTKPLVIEKFKEFPQLGRF 402
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 182-271 3.29e-61

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: 188.56  E-value: 3.29e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 182 KGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKFIKSGDAAIVKMVPSKPMCVEA 261
Cdd:cd03705    1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                         90
                 ....*....|
gi 338172972 262 FTDYPPLGRF 271
Cdd:cd03705   81 FSEYPPLGRF 90
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 180-262 1.43e-27

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: 102.34  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  180 PPKGADSFNAQVIVLNH-----PGQVGAGYAPVLDCHTAHIACKFSELLEKIDrrTGKSIENaPKFIKSGDAAIVKMVPS 254
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77


                  ....*...
gi 338172972  255 KPMCVEAF 262
Cdd:pfam03143  78 KPIALEKG 85
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-271 4.89e-180

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 502.74  E-value: 4.89e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM--*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEA 78
Cdd:PTZ00141 151 CINKMddKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNMPWYKG-----------PTLLEA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  79 IDAIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFN 158
Cdd:PTZ00141 220 LDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFN 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 159 VKNVSVKEIRRGNVAGDSKSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAP 238
Cdd:PTZ00141 300 VKNVSVKDIKRGYVASDSKNDPAKECADFTAQVIVLNHPGQIKNGYTPVLDCHTAHIACKFAEIESKIDRRSGKVLEENP 379

                        250       260       270
                 ....*....|....*....|....*....|...
gi 338172972 239 KFIKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:PTZ00141 380 KAIKSGDAAIVKMVPTKPMCVEVFNEYPPLGRF 412
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-271 2.23e-145

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: 414.26  E-value: 2.23e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972    1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:TIGR00483 147 AINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENTPWYKG-----------KTLLEALD 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   81 AIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVK 160
Cdd:TIGR00483 216 ALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVR 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  161 NVSVKEIRRGNVAGDSKsDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKF 240
Cdd:TIGR00483 296 GVSKKDIRRGDVCGHPD-NPPKVAKEFTAQIVVLQHPGAITVGYTPVFHCHTAQIACRFDELLKKNDPRTGQVLEENPQF 374

                         250       260       270
                  ....*....|....*....|....*....|.
gi 338172972  241 IKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:TIGR00483 375 LKTGDAAIVKFKPTKPMVIEAVKEIPPLGRF 405
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-271 3.31e-137

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: 393.14  E-value: 3.31e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:COG5256  144 AVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPWYNG-----------PTLLEALD 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVK 160
Cdd:COG5256  213 NLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVR 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 161 NVSVKEIRRGNVAGDSkSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKF 240
Cdd:COG5256  293 GVEKNDIKRGDVAGHP-DNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHVHTAQVACTFVELVSKLDPRTGQVKEENPQF 371

                        250       260       270
                 ....*....|....*....|....*....|.
gi 338172972 241 IKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:COG5256  372 LKTGDAAIVKIKPTKPLVIEKFKEFPQLGRF 402
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-271 2.06e-135

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 388.51  E-value: 2.06e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:PRK12317 145 AINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPWYNG-----------PTLLEALD 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVK 160
Cdd:PRK12317 214 NLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVR 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 161 NVSVKEIRRGNVAGdSKSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKF 240
Cdd:PRK12317 294 GVGKKDIKRGDVCG-HPDNPPTVAEEFTAQIVVLQHPSAITVGYTPVFHAHTAQVACTFEELVKKLDPRTGQVAEENPQF 372

                        250       260       270
                 ....*....|....*....|....*....|.
gi 338172972 241 IKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:PRK12317 373 IKTGDAAIVKIKPTKPLVIEKVKEIPQLGRF 403
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 3-271 1.15e-134

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 387.91  E-value: 1.15e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   3 NKM--*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:PLN00043 153 NKMdaTTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKG-----------PTLLEALD 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVK 160
Cdd:PLN00043 222 QINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVK 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 161 NVSVKEIRRGNVAGDSKSDPPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKF 240
Cdd:PLN00043 302 NVAVKDLKRGYVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKF 381

                        250       260       270
                 ....*....|....*....|....*....|.
gi 338172972 241 IKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:PLN00043 382 LKNGDAGFVKMIPTKPMVVETFSEYPPLGRF 412
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 182-271 3.29e-61

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: 188.56  E-value: 3.29e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 182 KGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKFIKSGDAAIVKMVPSKPMCVEA 261
Cdd:cd03705    1 KEAKSFTAQVIILNHPGQIKAGYTPVLDCHTAHVACKFAELKEKIDRRTGKKLEENPKFLKSGDAAIVKMVPTKPLCVET 80

                         90
                 ....*....|
gi 338172972 262 FTDYPPLGRF 271
Cdd:cd03705   81 FSEYPPLGRF 90
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 89-179 8.40e-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: 187.01  E-value: 8.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  89 TDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIR 168
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIK 80

                         90
                 ....*....|.
gi 338172972 169 RGNVAGDSKSD 179
Cdd:cd03693   81 RGDVAGDSKND 91
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-271 1.14e-40

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: 145.23  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTvpFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:COG2895  154 AVNKMDLVDYSEEVFEEIVADYRAFAAKLGLEDIT--FIPISALKGDNVVERSENMPWYDG-----------PTLLEHLE 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKiggigtvP-------VGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGD 153
Cdd:COG2895  221 TVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAGQ 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 154 NVGFNVK---NVSvkeirRGNVAGDSkSDPPKGADSFNAQVIVLN-HPGQVGAGYapVLDCHTAHIACKFSELLEKIDRR 229
Cdd:COG2895  294 SVTLTLEdeiDIS-----RGDVIVAA-DAPPEVADQFEATLVWMDeEPLLPGRKY--LLKHGTRTVRATVTAIKYRIDVN 365

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 338172972 230 TGKsiENAPKFIKSGDAAIVKMVPSKPMCVEAFTDYPPLGRF 271
Cdd:COG2895  366 TLE--HEAADSLELNDIGRVTLRLAEPIAFDPYADNRATGSF 405
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-85 8.24e-32

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: 116.82  E-value: 8.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM--*TAKWSGDRYNEIIKETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNCPW*KGWeketktkttgkTLLEA 78
Cdd:cd01883  143 AVNKMddVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENMPWYKGP-----------TLLEA 211


                 ....*..
gi 338172972  79 IDAIDPP 85
Cdd:cd01883  212 LDSLEPP 218
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 180-262 1.43e-27

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: 102.34  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  180 PPKGADSFNAQVIVLNH-----PGQVGAGYAPVLDCHTAHIACKFSELLEKIDrrTGKSIENaPKFIKSGDAAIVKMVPS 254
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKeeggrHTPFFNGYRPQFYFRTADVTGKFVELLHKLD--PGGVSEN-PEFVMPGDNVIVTVELI 77


                  ....*...
gi 338172972  255 KPMCVEAF 262
Cdd:pfam03143  78 KPIALEKG 85
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 182-271 1.36e-24

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: 94.38  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 182 KGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIEnaPKFIKSGDAAIVKMVPSKPMCVEA 261
Cdd:cd01513    1 QAVWKFDAKVIVLEHPKPIRPGYKPVMDVGTAHVPGRIAKLLSKEDGKTKEKKP--PDSLQPGENGTVEVELQKPVVLER 78

                         90
                 ....*....|
gi 338172972 262 FTDYPPLGRF 271
Cdd:cd01513   79 GKEFPTLGRF 88
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 184-271 3.79e-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: 93.39  E-value: 3.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 184 ADSFNAQVIVLNHPGQV-GAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKFIKSGDAAIVKMVPSKPMCVEAF 262
Cdd:cd03704    3 VTEFEAQIVILDLLKSIiTAGYSAVLHIHTAVEEVTITKLLATIDKKTGKKKKKKPKFVKSGQVVIARLETARPICLETF 82


                 ....*....
gi 338172972 263 TDYPPLGRF 271
Cdd:cd03704   83 KDFPQLGRF 91
PRK00049 PRK00049
elongation factor Tu; Reviewed
 75-194 4.87e-21

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.40  E-value: 4.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  75 LLEAIDA-IDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPANVTTeVKSVEMHHEQLTEGL 150
Cdd:PRK00049 194 LMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQ 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 338172972 151 PGDNVGFNVKNVSVKEIRRGNVAGDSKSDPPKgaDSFNAQVIVL 194
Cdd:PRK00049 273 AGDNVGALLRGIKREDVERGQVLAKPGSITPH--TKFEAEVYVL 314
PRK12735 PRK12735
elongation factor Tu; Reviewed
 75-194 8.74e-21

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 90.67  E-value: 8.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  75 LLEAIDA-IDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPANVTTeVKSVEMHHEQLTEGL 150
Cdd:PRK12735 194 LMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQ 272

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 338172972 151 PGDNVGFNVKNVSVKEIRRGNVAGDSKSDPPKgaDSFNAQVIVL 194
Cdd:PRK12735 273 AGDNVGVLLRGTKREDVERGQVLAKPGSIKPH--TKFEAEVYVL 314
tufA CHL00071
elongation factor Tu
 20-195 1.55e-20

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 90.02  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  20 KETSNFIKKVGYNPKTVPFVPISGFNGDNMIDESPNcpW*KG---WEKETKTkttgktLLEAIDA-IDPPSRPTDKPLRL 95
Cdd:CHL00071 152 LEVRELLSKYDFPGDDIPIVSGSALLALEALTENPK--IKRGenkWVDKIYN------LMDAVDSyIPTPERDTDKPFLM 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  96 PLQDVYKIGGIGTVPVGRVETGVIKAGMVVT---FAPANVTTeVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGNV 172
Cdd:CHL00071 224 AIEDVFSITGRGTVATGRIERGTVKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMV 302

                        170       180
                 ....*....|....*....|...
gi 338172972 173 AGDSKSDPPKgaDSFNAQVIVLN 195
Cdd:CHL00071 303 LAKPGTITPH--TKFEAQVYILT 323
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 28-194 1.78e-20

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: 89.82  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  28 KVGYNPKTVPFVPISGF---NGDnmidesPNCPW*KgweketktktTGKTLLEAIDA-IDPPSRPTDKPLRLPLQDVYKI 103
Cdd:COG0050  160 KYGFPGDDTPIIRGSALkalEGD------PDPEWEK----------KILELMDAVDSyIPEPERDTDKPFLMPVEDVFSI 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 104 GGIGTVPVGRVETGVIKAG---MVVTFAPAnVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGNVAGDSKSDP 180
Cdd:COG0050  224 TGRGTVVTGRVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSIT 302

                        170
                 ....*....|....
gi 338172972 181 PkgADSFNAQVIVL 194
Cdd:COG0050  303 P--HTKFEAEVYVL 314
PRK12736 PRK12736
elongation factor Tu; Reviewed
 75-194 5.31e-20

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 88.46  E-value: 5.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  75 LLEAIDA-IDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPAnVTTEVKSVEMHHEQLTEGL 150
Cdd:PRK12736 192 LMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQ 270

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 338172972 151 PGDNVGFNVKNVSVKEIRRGNVAGDSKSDPPkgADSFNAQVIVL 194
Cdd:PRK12736 271 AGDNVGVLLRGVDRDEVERGQVLAKPGSIKP--HTKFKAEVYIL 312
PLN03127 PLN03127
Elongation factor Tu; Provisional
 75-195 8.24e-20

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 88.34  E-value: 8.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  75 LLEAIDAIDP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAP-ANVTTEVKSVEMHHEQLTEG 149
Cdd:PLN03127 243 LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLRPgGPLKTTVTGVEMFKKILDQG 322

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 338172972 150 LPGDNVGFNVKNVSVKEIRRGNVAgdSKSDPPKGADSFNAQVIVLN 195
Cdd:PLN03127 323 QAGDNVGLLLRGLKREDVQRGQVI--CKPGSIKTYKKFEAEIYVLT 366
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-192 4.18e-19

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 86.52  E-value: 4.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNpkTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:PRK05506 163 AVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWYEG-----------PSLLEHLE 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKI-----GGIGTvpvgrVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNV 155
Cdd:PRK05506 230 TVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAV 304

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 338172972 156 gfnvkNVSVK---EIRRGN--VAGDsksDPPKGADSFNAQVI 192
Cdd:PRK05506 305 -----TLTLAdeiDISRGDmlARAD---NRPEVADQFDATVV 338
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 93-172 5.77e-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: 78.85  E-value: 5.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  93 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNvsVKEIRRGNV 172
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG--VKDILTGDT 78
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 75-194 6.67e-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: 85.21  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   75 LLEAIDA-IDPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAG---MVVTFAPANVTTeVKSVEMHHEQLTEGL 150
Cdd:TIGR00485 192 LMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGR 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 338172972  151 PGDNVGFNVKNVSVKEIRRGNVAGDSKSDPPKgaDSFNAQVIVL 194
Cdd:TIGR00485 271 AGDNVGLLLRGIKREEIERGMVLAKPGSIKPH--TKFEAEVYVL 312
PLN03126 PLN03126
Elongation factor Tu; Provisional
 75-260 1.17e-17

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 81.97  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  75 LLEAIDAIDP-PSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVT--TEVKSVEMHHEQLTEGLP 151
Cdd:PLN03126 271 LMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrsTTVTGVEMFQKILDEALA 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 152 GDNVGFNVKNVSVKEIRRGNVAgdSKSDPPKGADSFNAQVIVLNHP-----GQVGAGYAPVLDCHTAHIACKFSELLEKI 226
Cdd:PLN03126 351 GDNVGLLLRGIQKADIQRGMVL--AKPGSITPHTKFEAIVYVLKKEeggrhSPFFAGYRPQFYMRTTDVTGKVTSIMNDK 428

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 338172972 227 DRRTgksienapKFIKSGDAaiVKMVPS--KPMCVE 260
Cdd:PLN03126 429 DEES--------KMVMPGDR--VKMVVEliVPVACE 454
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 95-172 4.17e-17

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: 74.09  E-value: 4.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  95 LPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFA--PANVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGNV 172
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 93-172 4.45e-17

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 74.10  E-value: 4.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  93 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGNV 172
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFV 80
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 180-271 3.31e-16

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: 72.58  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972 180 PPKGADSFNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFSELLEKIDRRTGKSIENAPKFIKSGDAAIVKMVPSKPMCV 259
Cdd:cd04093    1 PVATTSKFEARIVTFDLQVPILKGTPVVLHRHSLSEPATISKLVSTLDKSTGEVIKKKPRCLGKNQSAVVEIELERPIPL 80

                         90
                 ....*....|..
gi 338172972 260 EAFTDYPPLGRF 271
Cdd:cd04093   81 ETFKDNKELGRF 92
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-192 9.27e-16

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 76.49  E-value: 9.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPkTVPFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:PRK05124 166 AVNKMDLVDYSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWYSG-----------PTLLEVLE 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  81 AIDPPSRPTDKPLRLPLQDVYKI-----GGIGTvpvgrVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNV 155
Cdd:PRK05124 234 TVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAGEAI 308

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 338172972 156 GFNVKNvsvkE--IRRGNVAGDSKSDPPKGaDSFNAQVI 192
Cdd:PRK05124 309 TLVLED----EidISRGDLLVAADEALQAV-QHASADVV 342
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 107-172 1.27e-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: 1.27e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338172972  107 GTVPVGRVETGVIKAGMVVTFAPANV-----TTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGNV 172
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDT 71
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 75-196 3.14e-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: 74.95  E-value: 3.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  75 LLEAIDAI--DPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPG 152
Cdd:COG3276  157 LRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAG 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 338172972 153 DNVGFNVKNVSVKEIRRGNVAgdSKSDPPKGADSFNAQVIVLNH 196
Cdd:COG3276  237 QRVALNLAGVEKEEIERGDVL--AAPGALRPTDRIDVRLRLLPS 278
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 92-175 1.29e-13

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: 64.84  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  92 PLRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGN 171
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGS 80


                 ....
gi 338172972 172 VAGD 175
Cdd:cd16267   81 ILCD 84
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-86 2.93e-13

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: 66.82  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972   1 AINKM*TAKWSGDRYNEIIKETSNFIKKVGYNPKTvpFVPISGFNGDNMIDESPNCPW*KGweketktkttgKTLLEAID 80
Cdd:cd04166  137 AVNKMDLVDYDEEVFEEIKADYLAFAASLGIEDIT--FIPISALEGDNVVSRSENMPWYKG-----------PTLLEHLE 203


                 ....*.
gi 338172972  81 AIDPPS 86
Cdd:cd04166  204 TVEIAS 209
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 92-172 1.56e-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: 59.04  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  92 PLRLPLQDVYKigGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGN 171
Cdd:cd04089    1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGF 78


                 .
gi 338172972 172 V 172
Cdd:cd04089   79 V 79
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 92-175 2.83e-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: 55.59  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338172972  92 PLRLPLQDVYKiGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMH-HEQLTEGLPGDNVGFNVKNVSVKEIRRG 170
Cdd:cd03698    1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLRGIEVEDIQPG 79


                 ....*
gi 338172972 171 NVAGD 175
Cdd:cd03698   80 DILSS 84
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 99-172 5.16e-10

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: 54.92  E-value: 5.16e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338172972  99 DVYKIGGIGTVPVGRVETGVIKAGMVVTFAPAN----VTTEVKSVEMHHEQLTEGLPGDNVGFNVKNVSVKEIRRGNV 172
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 ...
 93-157 1.01e-07

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: 48.33  E-value: 1.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338172972  93 LRLPLQDVYKIGGIGTVPVGRVETGVIKAGMVVTFAPANVTTEVKSVEMHHEQLTEGLPGDNVGF 157
Cdd:cd03695    1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-49 1.34e-07

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: 50.60  E-value: 1.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 338172972    1 AINKM*TAkwSGDRYNEIIKETSN-FIKKVGYNPKTVPFVPISGFNGDNM 49
Cdd:pfam00009 127 FINKMDRV--DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGV 174
GTPBP_III cd03708
Domain III of the GP-1 family of GTPases; This family includes proteins similar to GTPBP1 and ...
 187-251 1.98e-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: 1.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338172972 187 FNAQVIVLNHPGQVGAGYAPVLDCHTAHIACKFsellEKIDRrtgksienapKFIKSGDAAIVKM 251
Cdd:cd03708    6 FEAEVLVLHHPTTISPGYQPVVHCGTIRQTARI----ISIDK----------EVLRTGDRALVRF 56
 
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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