NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|926677764|gb|ALD53762|]
View 

elongation factor 1-alpha, partial [Macromeris violacea]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-186 4.04e-118

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: 341.73  E-value: 4.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:PTZ00141 129 KDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNM 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  81 PWFRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:PTZ00141 209 PWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTE 276

                        170       180
                 ....*....|....*....|....*.
gi 926677764 161 VKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:PTZ00141 277 VKSVEMHHEQLAEAVPGDNVGFNVKN 302
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-186 4.04e-118

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 341.73  E-value: 4.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:PTZ00141 129 KDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNM 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  81 PWFRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:PTZ00141 209 PWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTE 276

                        170       180
                 ....*....|....*....|....*.
gi 926677764 161 VKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:PTZ00141 277 VKSVEMHHEQLAEAVPGDNVGFNVKN 302
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 3-185 3.56e-93

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: 277.58  E-value: 3.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   3 GQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPW 82
Cdd:COG5256  124 GQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 FRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVK 162
Cdd:COG5256  202 YNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVK 269

                        170       180
                 ....*....|....*....|...
gi 926677764 163 SVEMHHEALQEAVPGDNVGFNVK 185
Cdd:COG5256  270 SIEMHHEELEQAEPGDNIGFNVR 292
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-186 6.46e-89

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: 266.73  E-value: 6.46e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:TIGR00483 125 VQPQTREHAFLARTLGINQLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENT 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   81 PWFRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:TIGR00483 203 PWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGE 270

                         170       180
                  ....*....|....*....|....*.
gi 926677764  161 VKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:TIGR00483 271 VKSIEMHHEQIEQAEPGDNIGFNVRG 296
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-110 9.60e-57

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: 177.68  E-value: 9.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:cd01883  121 KGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENM 200

                         90       100       110
                 ....*....|....*....|....*....|
gi 926677764  81 PWFRGWqverkegkaegkCLIEALDAILPP 110
Cdd:cd01883  201 PWYKGP------------TLLEALDSLEPP 218
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 3-110 9.57e-18

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: 76.79  E-value: 9.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    3 GQTREHALLAFTLGVKqLIVGVNKMDSTeppySEARFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEvsskmp 81
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------ 176

                          90       100
                  ....*....|....*....|....*....
gi 926677764   82 wfrgwqverkegkaegkcLIEALDAILPP 110
Cdd:pfam00009 177 ------------------LLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-186 4.04e-118

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 341.73  E-value: 4.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:PTZ00141 129 KDGQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIEKSDNM 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  81 PWFRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:PTZ00141 209 PWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVTTE 276

                        170       180
                 ....*....|....*....|....*.
gi 926677764 161 VKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:PTZ00141 277 VKSVEMHHEQLAEAVPGDNVGFNVKN 302
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 3-185 3.56e-93

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: 277.58  E-value: 3.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   3 GQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPW 82
Cdd:COG5256  124 GQTREHAFLARTLGINQLIVAVNKMDAVN--YSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKGDNVVKKSDNMPW 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 FRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVK 162
Cdd:COG5256  202 YNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMPAGVVGEVK 269

                        170       180
                 ....*....|....*....|...
gi 926677764 163 SVEMHHEALQEAVPGDNVGFNVK 185
Cdd:COG5256  270 SIEMHHEELEQAEPGDNIGFNVR 292
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 3-185 1.63e-92

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 276.04  E-value: 1.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   3 GQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKMPW 82
Cdd:PRK12317 125 PQTREHVFLARTLGINQLIVAINKMDAVN--YDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEGDNVVKKSENMPW 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 FRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVK 162
Cdd:PRK12317 203 YNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFMPAGVVGEVK 270

                        170       180
                 ....*....|....*....|...
gi 926677764 163 SVEMHHEALQEAVPGDNVGFNVK 185
Cdd:PRK12317 271 SIEMHHEELPQAEPGDNIGFNVR 293
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-186 1.02e-89

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 269.65  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:PLN00043 129 KDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNL 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  81 PWFRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:PLN00043 209 DWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTE 276

                        170       180
                 ....*....|....*....|....*.
gi 926677764 161 VKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:PLN00043 277 VKSVEMHHESLQEALPGDNVGFNVKN 302
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-186 6.46e-89

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: 266.73  E-value: 6.46e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:TIGR00483 125 VQPQTREHAFLARTLGINQLIVAINKMDSVN--YDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPISAWNGDNVIKKSENT 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   81 PWFRGwqverkegkaegKCLIEALDAILPPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:TIGR00483 203 PWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLKPGDKVVFEPAGVSGE 270

                         170       180
                  ....*....|....*....|....*.
gi 926677764  161 VKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:TIGR00483 271 VKSIEMHHEQIEQAEPGDNIGFNVRG 296
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-110 9.60e-57

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: 177.68  E-value: 9.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   1 KNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEVSSKM 80
Cdd:cd01883  121 KGGQTREHALLARTLGVKQLIVAVNKMDDVTVNWSQERYDEIKKKVSPFLKKVGYNPKDVPFIPISGFTGDNLIEKSENM 200

                         90       100       110
                 ....*....|....*....|....*....|
gi 926677764  81 PWFRGWqverkegkaegkCLIEALDAILPP 110
Cdd:cd01883  201 PWYKGP------------TLLEALDSLEPP 218
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 114-186 1.41e-51

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: 160.43  E-value: 1.41e-51
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 926677764 114 TDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKG 73
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 4-182 1.07e-48

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: 163.33  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEVSSKMPWF 83
Cdd:COG2895  135 QTRRHSYIASLLGIRHVVVAVNKMDLVD--YSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 rgwqverkegkaEGKCLIEALDAILPPTRPTDKALRLPLQDVYKiggigtvP-------VGRVETGVLKPGMVVTFAPAG 156
Cdd:COG2895  211 ------------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSG 271

                        170       180
                 ....*....|....*....|....*.
gi 926677764 157 LTTEVKSVEMHHEALQEAVPGDNVGF 182
Cdd:COG2895  272 KTSTVKSIVTFDGDLEEAFAGQSVTL 297
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 4-180 1.06e-30

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 116.95  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYnpAAVAFVPISGWHGDNMLEVSSKMPWF 83
Cdd:PRK05506 144 QTRRHSFIASLLGIRHVVLAVNKMDLVD--YDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKGDNVVTRSARMPWY 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 rgwqverkegkaEGKCLIEALDAILPPTRPTDKALRLPLQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPAGLT 158
Cdd:PRK05506 220 ------------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKT 282

                        170       180
                 ....*....|....*....|..
gi 926677764 159 TEVKSVEMHHEALQEAVPGDNV 180
Cdd:PRK05506 283 SRVKRIVTPDGDLDEAFAGQAV 304
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 4-180 1.83e-29

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


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 112.08  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    4 QTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGynPAAVAFVPISGWHGDNMLEVSSKMPWF 83
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVD--YDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   84 rgwqverkegkaEGKCLIEALDAILPPTRPTDKALRLPLQDVYKI-----GGIGTVPVGRVEtgvlkPGMVVTFAPAGLT 158
Cdd:TIGR02034 196 ------------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVH-----VGDEVVVLPSGRS 258

                         170       180
                  ....*....|....*....|..
gi 926677764  159 TEVKSVEMHHEALQEAVPGDNV 180
Cdd:TIGR02034 259 SRVARIVTFDGDLEQARAGQAV 280
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 4-180 5.42e-29

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 111.54  E-value: 5.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPaAVAFVPISGWHGDNMLEVSSKMPWF 83
Cdd:PRK05124 147 QTRRHSFIATLLGIKHLVVAVNKMDLVD--YSEEVFERIREDYLTFAEQLPGNL-DIRFVPLSALEGDNVVSQSESMPWY 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 rgwqverkegkaEGKCLIEALDAILPPTRPTDKALRLPLQDVYKI-----GGIGTvpvgrVETGVLKPGMVVTFAPAGLT 158
Cdd:PRK05124 224 ------------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKE 286

                        170       180
                 ....*....|....*....|..
gi 926677764 159 TEVKSVEMHHEALQEAVPGDNV 180
Cdd:PRK05124 287 SNVARIVTFDGDLEEAFAGEAI 308
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 4-107 1.22e-27

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: 103.03  E-value: 1.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppYSEARFEEIKKEVSSYIKKIGYNPaaVAFVPISGWHGDNMLEVSSKMPWF 83
Cdd:cd04166  118 QTRRHSYIASLLGIRHVVVAVNKMDLVD--YDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY 193

                         90       100
                 ....*....|....*....|....
gi 926677764  84 rgwqverkegkaEGKCLIEALDAI 107
Cdd:cd04166  194 ------------KGPTLLEHLETV 205
tufA CHL00071
elongation factor Tu
 4-181 3.89e-23

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 94.64  E-value: 3.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppySEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGdnmLEVSSKMPwf 83
Cdd:CHL00071 115 QTKEHILLAKQVGVPNIVVFLNKEDQVD---DEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA---LEALTENP-- 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 rgwQVERKEGKAEGKC--LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFapAGL--- 157
Cdd:CHL00071 187 ---KIKRGENKWVDKIynLMDAVDSYIPtPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEI--VGLret 261

                        170       180
                 ....*....|....*....|....*
gi 926677764 158 -TTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:CHL00071 262 kTTTVTGLEMFQKTLDEGLAGDNVG 286
PRK00049 PRK00049
elongation factor Tu; Reviewed
 4-181 6.39e-22

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 91.02  E-value: 6.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTE-PPYSEARFEEIKKEVSSYikkigynpaavafvpisGWHGDNMlevsskmPW 82
Cdd:PRK00049 115 QTREHILLARQVGVPYIVVFLNKCDMVDdEELLELVEMEVRELLSKY-----------------DFPGDDT-------PI 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 FRGWQVERKEGKAEGKC------LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTF 152
Cdd:PRK00049 171 IRGSALKALEGDDDEEWekkileLMDAVDSYIPtPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGeevEIVGI 250

                        170       180
                 ....*....|....*....|....*....
gi 926677764 153 APAGLTTeVKSVEMHHEALQEAVPGDNVG 181
Cdd:PRK00049 251 RDTQKTT-VTGVEMFRKLLDEGQAGDNVG 278
PRK12735 PRK12735
elongation factor Tu; Reviewed
 4-181 3.16e-21

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 89.13  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEPPyseARFEEIKKEVSSYIKKIGYNpaavafvpisgwhGDNMlevsskmPWF 83
Cdd:PRK12735 115 QTREHILLARQVGVPYIVVFLNKCDMVDDE---ELLELVEMEVRELLSKYDFP-------------GDDT-------PII 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 RGWQVERKEGKAEGKC------LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFA 153
Cdd:PRK12735 172 RGSALKALEGDDDEEWeakileLMDAVDSYIPePERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGdevEIVGIK 251

                        170       180
                 ....*....|....*....|....*...
gi 926677764 154 PaGLTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:PRK12735 252 E-TQKTTVTGVEMFRKLLDEGQAGDNVG 278
PLN03127 PLN03127
Elongation factor Tu; Provisional
 4-181 6.31e-21

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 88.73  E-value: 6.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIKkigynpaavafvpisgWHGDNMlevsskmPWF 83
Cdd:PLN03127 164 QTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYK----------------FPGDEI-------PII 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 RGWQVERKEGKAE--GKC----LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFA 153
Cdd:PLN03127 221 RGSALSALQGTNDeiGKNailkLMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGeevEIVGLR 300

                        170       180
                 ....*....|....*....|....*....
gi 926677764 154 PAG-LTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:PLN03127 301 PGGpLKTTVTGVEMFKKILDQGQAGDNVG 329
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 4-181 6.38e-21

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: 88.28  E-value: 6.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEPPY-SEARFEEIKKEVSSYikkigynpaavafvpisGWHGDNMlevsskmPW 82
Cdd:COG0050  115 QTREHILLARQVGVPYIVVFLNKCDMVDDEElLELVEMEVRELLSKY-----------------GFPGDDT-------PI 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 FRGWQVERKEGKAEGKC------LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTF 152
Cdd:COG0050  171 IRGSALKALEGDPDPEWekkileLMDAVDSYIPePERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGdevEIVGI 250

                        170       180
                 ....*....|....*....|....*....
gi 926677764 153 APAgLTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:COG0050  251 RDT-QKTVVTGVEMFRKLLDEGEAGDNVG 278
PRK12736 PRK12736
elongation factor Tu; Reviewed
 4-181 2.10e-20

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 86.92  E-value: 2.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFE-EIKKEVSSYikkigynpaavafvpisGWHGDNmlevsskMPW 82
Cdd:PRK12736 115 QTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEmEVRELLSEY-----------------DFPGDD-------IPV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 FRGWQVERKEGKAEG----KCLIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAP 154
Cdd:PRK12736 171 IRGSALKALEGDPKWedaiMELMDAVDEYIPtPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGdevEIVGIKE 250

                        170       180
                 ....*....|....*....|....*..
gi 926677764 155 AgLTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:PRK12736 251 T-QKTVVTGVEMFRKLLDEGQAGDNVG 276
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 4-181 9.22e-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: 85.21  E-value: 9.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    4 QTREHALLAFTLGVKQLIVGVNKMD-STEPPYSEARFEEIKKEVSSYikkigynpaavafvpisGWHGDNMlevsskmPW 82
Cdd:TIGR00485 115 QTREHILLARQVGVPYIVVFLNKCDmVDDEELLELVEMEVRELLSQY-----------------DFPGDDT-------PI 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   83 FRGWQVERKEGKAEGKC----LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPG---MVVTFAP 154
Cdd:TIGR00485 171 IRGSALKALEGDAEWEAkileLMDAVDEYIPtPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGeevEIVGLKD 250

                         170       180
                  ....*....|....*....|....*..
gi 926677764  155 AGLTTeVKSVEMHHEALQEAVPGDNVG 181
Cdd:TIGR00485 251 TRKTT-VTGVEMFRKELDEGRAGDNVG 276
PLN03126 PLN03126
Elongation factor Tu; Provisional
 4-181 2.10e-19

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 84.67  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppySEARFEEIKKEVSSYIKKIGYNPAAVafvPISGWHGDNMLEVSSKMPwf 83
Cdd:PLN03126 184 QTKEHILLAKQVGVPNMVVFLNKQDQVD---DEELLELVELEVRELLSSYEFPGDDI---PIISGSALLALEALMENP-- 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  84 rgwQVERKEGKAEGKC--LIEALDAILP-PTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLT-- 158
Cdd:PLN03126 256 ---NIKRGDNKWVDKIyeLMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETrs 332

                        170       180
                 ....*....|....*....|...
gi 926677764 159 TEVKSVEMHHEALQEAVPGDNVG 181
Cdd:PLN03126 333 TTVTGVEMFQKILDEALAGDNVG 355
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 4-183 3.67e-19

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: 84.19  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREH-ALLAFtLGVKQLIVGVNKMDSTEPpyseARFEEIKKEVSSYIKKigynpaavafvpiSGWHGDNMLEVSSKmpw 82
Cdd:COG3276   91 QTREHlAILDL-LGIKRGIVVLTKADLVDE----EWLELVEEEIRELLAG-------------TFLEDAPIVPVSAV--- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  83 frgwqveRKEGKAEgkcLIEALDAIL--PPTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTE 160
Cdd:COG3276  150 -------TGEGIDE---LRAALDALAaaVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVR 219

                        170       180
                 ....*....|....*....|...
gi 926677764 161 VKSVEMHHEALQEAVPGDNVGFN 183
Cdd:COG3276  220 VRGIQVHGQPVEEAYAGQRVALN 242
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 118-186 3.67e-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: 77.30  E-value: 3.67e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926677764 118 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILG 69
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 3-110 9.57e-18

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: 76.79  E-value: 9.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    3 GQTREHALLAFTLGVKqLIVGVNKMDSTeppySEARFEEIKKEVSS-YIKKIGYNPAAVAFVPISGWHGDNMLEvsskmp 81
Cdd:pfam00009 108 PQTREHLRLARQLGVP-IIVFINKMDRV----DGAELEEVVEEVSReLLEKYGEDGEFVPVVPGSALKGEGVQT------ 176

                          90       100
                  ....*....|....*....|....*....
gi 926677764   82 wfrgwqverkegkaegkcLIEALDAILPP 110
Cdd:pfam00009 177 ------------------LLDALDEYLPS 187
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 118-180 1.98e-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: 62.53  E-value: 1.98e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 926677764 118 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNV 180
Cdd:cd16267    2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNV 64
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 4-184 2.15e-13

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 67.59  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764    4 QTREHALLAFTLGVKQLIVGVNKMDSTEppysEARFEEIKKEVSSYIKKIGYNPAAVAFVpISGWHGDNMLEVsskmpwf 83
Cdd:TIGR00475  90 QTGEHLAVLDLLGIPHTIVVITKADRVN----EEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGEL------- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   84 rgwqverkegKAEGKCLIEALDailppTRPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKS 163
Cdd:TIGR00475 158 ----------KKELKNLLESLD-----IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKA 222

                         170       180
                  ....*....|....*....|.
gi 926677764  164 VEMHHEALQEAVPGDNVGFNV 184
Cdd:TIGR00475 223 IQAQNQDVEIAYAGQRIALNL 243
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 120-181 3.24e-13

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: 62.15  E-value: 3.24e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 926677764 120 LPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFA--PAGLTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:cd03697    3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVgfKETLKTTVTGIEMFRKTLDEAEAGDNVG 66
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 118-186 9.44e-13

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: 60.62  E-value: 9.44e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926677764 118 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTG 69
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 132-185 9.57e-13

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: 60.36  E-value: 9.57e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 926677764  132 GTVPVGRVETGVLKPGMVVTFAPAG-----LTTEVKSVEMHHEALQEAVPGDNVGFNVK 185
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGtgkkkIVTRVTSLLMFHAPLREAVAGDNAGLILA 59
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 3-75 4.17e-11

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 58.85  E-value: 4.17e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 926677764   3 GQTREHALLAFtLGVKQLIVGVNKMDSTeppySEARFEEIKKEVSSYIKKIGY---NPAAVAFVPISGWHGDNMLE 75
Cdd:cd00881  101 PQTREHLNIAL-AGGLPIIVAVNKIDRV----GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIEE 171
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 118-182 2.37e-10

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: 54.49  E-value: 2.37e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 926677764 118 LRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGF 182
Cdd:cd03695    1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 118-186 1.16e-07

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: 47.09  E-value: 1.16e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926677764 118 LRLPLQDVYKigGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMHHEALQEAVPGDNVGFNVKN 186
Cdd:cd04089    2 LRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKG 68
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 124-185 1.19e-06

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: 44.52  E-value: 1.19e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 926677764 124 DVYKIGGIGTVPVGRVETGVLKPGMVVTFAPAG----LTTEVKSVEMHHEALQEAVPGDNVGFNVK 185
Cdd:cd03694    7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALK 72
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 118-185 2.73e-06

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: 43.64  E-value: 2.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 926677764 118 LRLPLQDVYKiGGIGTVPVGRVETGVLKPGMVVTFAPAGLTTEVKSVEMH-HEALQEAVPGDNVGFNVK 185
Cdd:cd03698    2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLR 69
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 123-181 2.03e-05

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: 41.13  E-value: 2.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 926677764 123 QDVYKIGGiGTVPVGRVETGVLKPGMVVTfAPAGlTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:cd16265    6 EKVFKILG-RQVLTGEVESGVIYVGYKVK-GDKG-VALIRAIEREHRKVDFAVAGDEVA 61
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 4-110 2.40e-05

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


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 42.96  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEppySEARFEEIKKEVSSYIKKIGYNPAAVAFVPISGWhgdNMLEvsskmpwf 83
Cdd:cd01884  105 QTREHLLLARQVGVPYIVVFLNKADMVD---DEELLELVEMEVRELLSKYGFDGDDTPIVRGSAL---KALE-------- 170

                         90       100
                 ....*....|....*....|....*....
gi 926677764  84 rgwqvERKEGKAEGKC--LIEALDAILPP 110
Cdd:cd01884  171 -----GDDPNKWVDKIleLLDALDSYIPT 194
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 4-181 3.29e-04

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 40.22  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHaLLAFT-LGVKQLIVGVNKMDSTEPPYSEARFEEIKKEVSSYIkkigynpAAVA-FVPISGWHGDNMlevsskmp 81
Cdd:PRK04000 126 QTKEH-LMALDiIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGTV-------AENApIIPVSALHKVNI-------- 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764  82 wfrgwqverkegkaegKCLIEALDAILP-PTRPTDKALRLPLQ---DVYK--------IGGI--GTVPVGRVETG---VL 144
Cdd:PRK04000 190 ----------------DALIEAIEEEIPtPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeiEI 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 926677764 145 KPGMVVTFAPAG----LTTEVKSVEMHHEALQEAVPGDNVG 181
Cdd:PRK04000 254 RPGIKVEEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVG 294
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 4-113 5.68e-04

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 38.74  E-value: 5.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926677764   4 QTREHALLAFTLGVKQLIVGVNKMDSTEPPYSEARFEEIKkevssyikkigynpaavAFVPISGWHGDNMLEVSSKMPwf 83
Cdd:cd04171   90 QTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEIL-----------------ELLAGTFLADAPIFPVSSVTG-- 150

                         90       100       110
                 ....*....|....*....|....*....|
gi 926677764  84 rgwqverkEGKAEgkcLIEALDAILPPTRP 113
Cdd:cd04171  151 --------EGIEE---LKNYLDELAEPQSK 169
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH