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Conserved domains on  [gi|1802442779|gb|QHQ71109|]
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translation elongation factor 1-alpha, partial [Pholiota aurivella]

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 ...
 1-203 4.29e-128

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: 367.92  E-value: 4.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:PTZ00141  112 AILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFI 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  79 PISGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGI 158
Cdd:PTZ00141  192 PISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGI 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1802442779 159 IKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:PTZ00141  260 LKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVS 304
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-203 4.29e-128

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 367.92  E-value: 4.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:PTZ00141  112 AILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFI 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  79 PISGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGI 158
Cdd:PTZ00141  192 PISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGI 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1802442779 159 IKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:PTZ00141  260 LKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVS 304
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-203 1.65e-99

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: 294.46  E-value: 1.65e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFVPI 80
Cdd:TIGR00483 112 AVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPI 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  81 SGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 160
Cdd:TIGR00483 188 SAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLK 255

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1802442779 161 AGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:TIGR00483 256 PGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVS 298
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-203 1.06e-95

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: 284.52  E-value: 1.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFVPI 80
Cdd:COG5256   112 AILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPV 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  81 SGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 160
Cdd:COG5256   185 SAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLK 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1802442779 161 AGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:COG5256   253 VGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVE 295
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-126 6.35e-66

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: 201.95  E-value: 6.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:cd01883   104 AVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFI 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1802442779  79 PISGWHGDNMLEESPNMPWYKGWtketkagvvkgkTLLDAIDAIEPPV 126
Cdd:cd01883   184 PISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-125 5.30e-19

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: 80.26  E-value: 5.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-IFIKKVGYNPKAVAFVP 79
Cdd:pfam00009  96 AILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPVVP 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1802442779  80 ISGWHGDNMleespnmpwykgwtketkagvvkgKTLLDAIDAIEPP 125
Cdd:pfam00009 166 GSALKGEGV------------------------QTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-203 4.29e-128

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 367.92  E-value: 4.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMD--TTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:PTZ00141  112 AILVVASTAGEFEAGISKDGQTREHALLAFTLGVKQMIVCINKMDdkTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFI 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  79 PISGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGI 158
Cdd:PTZ00141  192 PISGWQGDNMIEKSDNMPWYKG------------PTLLEALDTLEPPKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGI 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1802442779 159 IKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:PTZ00141  260 LKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVS 304
EF-1_alpha TIGR00483
translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial ...
 1-203 1.65e-99

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: 294.46  E-value: 1.65e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEagisKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFVPI 80
Cdd:TIGR00483 112 AVLVVAVGDGEFE----VQPQTREHAFLARTLGINQLIVAINKMDSVNYDEEEFEAIKKEVSNLIKKVGYNPDTVPFIPI 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  81 SGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 160
Cdd:TIGR00483 188 SAWNGDNVIKKSENTPWYKG------------KTLLEALDALEPPEKPTDKPLRIPIQDVYSITGVGTVPVGRVETGVLK 255

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1802442779 161 AGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:TIGR00483 256 PGDKVVFEPAGVSGEVKSIEMHHEQIEQAEPGDNIGFNVRGVS 298
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-203 1.06e-95

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: 284.52  E-value: 1.06e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEfeagiskDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFVPI 80
Cdd:COG5256   112 AILVVSAKDGV-------MGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEEVSKLLKMVGYKVDKIPFIPV 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  81 SGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 160
Cdd:COG5256   185 SAWKGDNVVKKSDNMPWYNG------------PTLLEALDNLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLK 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1802442779 161 AGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:COG5256   253 VGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVE 295
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-203 2.50e-95

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 283.74  E-value: 2.50e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGgtgefEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPKAVAFVPI 80
Cdd:PRK12317  111 AVLVVAA-----DDAGGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  81 SGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIK 160
Cdd:PRK12317  186 SAFEGDNVVKKSENMPWYNG------------PTLLEALDNLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLK 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1802442779 161 AGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:PRK12317  254 VGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVG 296
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-203 7.25e-94

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 280.82  E-value: 7.25e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:PLN00043  112 AVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATtpKYSKARYDEIVKEVSSYLKKVGYNPDKIPFV 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  79 PISGWHGDNMLEESPNMPWYKGwtketkagvvkgKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGI 158
Cdd:PLN00043  192 PISGFEGDNMIERSTNLDWYKG------------PTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGV 259

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1802442779 159 IKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:PLN00043  260 IKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVA 304
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-126 6.35e-66

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: 201.95  E-value: 6.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDTT--KWSEDRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:cd01883   104 AVLVVSARKGEFEAGFEKGGQTREHALLARTLGVKQLIVAVNKMDDVtvNWSQERYDEIKKKVSPFLKKVGYNPKDVPFI 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1802442779  79 PISGWHGDNMLEESPNMPWYKGWtketkagvvkgkTLLDAIDAIEPPV 126
Cdd:cd01883   184 PISGFTGDNLIEKSENMPWYKGP------------TLLEALDSLEPPE 219
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 21-197 6.71e-50

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: 167.19  E-value: 6.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPkaVAFVPISGWHGDNMLEESPNMPWYkg 100
Cdd:COG2895   135 QTRRHSYIASLLGIRHVVVAVNKMDLVDYSEEVFEEIVADYRAFAAKLGLED--ITFIPISALKGDNVVERSENMPWY-- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779 101 wtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKiggigtvP-------VGRVETGIIKAGMVVNFAPSNVT 173
Cdd:COG2895   211 ----------DGPTLLEHLETVEVAEDRNDAPFRFPVQYVNR-------PnldfrgyAGTIASGTVRVGDEVVVLPSGKT 273

                         170       180
                  ....*....|....*....|....
gi 1802442779 174 TEVKSVEMHHEQLEQGNPGDNVGF 197
Cdd:COG2895   274 STVKSIVTFDGDLEEAFAGQSVTL 297
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 129-203 1.61e-49

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: 155.81  E-value: 1.61e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802442779 129 SDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVS 75
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 21-195 6.28e-32

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 121.19  E-value: 6.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNpkAVAFVPISGWHGDNMLEESPNMPWYkg 100
Cdd:PRK05506  144 QTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVFDEIVADYRAFAAKLGLH--DVTFIPISALKGDNVVTRSARMPWY-- 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779 101 wtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGIIKAGMVVNFAPSNVTTE 175
Cdd:PRK05506  220 ----------EGPSLLEHLETVEIASDRNLKDFRFPVQYVNRPnldfrGFAGT-----VASGVVRPGDEVVVLPSGKTSR 284

                         170       180
                  ....*....|....*....|
gi 1802442779 176 VKSVEMHHEQLEQGNPGDNV 195
Cdd:PRK05506  285 VKRIVTPDGDLDEAFAGQAV 304
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
 21-195 2.16e-31

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


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 117.86  E-value: 2.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGynPKAVAFVPISGWHGDNMLEESPNMPWYkg 100
Cdd:TIGR02034 120 QTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVFENIKKDYLAFAEQLG--FRDVTFIPLSALKGDNVVSRSESMPWY-- 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779 101 wtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTVPVGRVETGiikaGMVVnFAPSNVTTE 175
Cdd:TIGR02034 196 ----------SGPTLLEILETVEVERDAQDLPLRFPVQYVNRPnldfrGYAGTIASGSVHVG----DEVV-VLPSGRSSR 260

                         170       180
                  ....*....|....*....|
gi 1802442779 176 VKSVEMHHEQLEQGNPGDNV 195
Cdd:TIGR02034 261 VARIVTFDGDLEQARAGQAV 280
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 21-125 2.17e-31

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: 113.43  E-value: 2.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPkaVAFVPISGWHGDNMLEESPNMPWYkg 100
Cdd:cd04166   118 QTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADYLAFAASLGIED--ITFIPISALEGDNVVSRSENMPWY-- 193

                          90       100
                  ....*....|....*....|....*
gi 1802442779 101 wtketkagvvKGKTLLDAIDAIEPP 125
Cdd:cd04166   194 ----------KGPTLLEHLETVEIA 208
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 21-195 9.41e-31

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 116.94  E-value: 9.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTKWSEDRFNEIIKETSIFIKKVGYNPKaVAFVPISGWHGDNMLEESPNMPWYkg 100
Cdd:PRK05124  147 QTRRHSFIATLLGIKHLVVAVNKMDLVDYSEEVFERIREDYLTFAEQLPGNLD-IRFVPLSALEGDNVVSQSESMPWY-- 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779 101 wtketkagvvKGKTLLDAIDAIEPPVRPSDKPLRLPLQDVYKI-----GGIGTvpvgrVETGIIKAGMVVNFAPSNVTTE 175
Cdd:PRK05124  224 ----------SGPTLLEVLETVDIQRVVDAQPFRFPVQYVNRPnldfrGYAGT-----LASGVVKVGDRVKVLPSGKESN 288

                         170       180
                  ....*....|....*....|
gi 1802442779 176 VKSVEMHHEQLEQGNPGDNV 195
Cdd:PRK05124  289 VARIVTFDGDLEEAFAGEAI 308
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-196 1.46e-25

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: 101.77  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGgtgefeagisKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwsEDrfNEIIK----ETSIFIKKVGYNPK 73
Cdd:COG0050   102 AILVVSA----------TDGpmpQTREHILLARQVGVPYIVVFLNKCDMV---DD--EELLElvemEVRELLSKYGFPGD 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  74 AVAFVPISGWhgdNMLEESPNMPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVG 152
Cdd:COG0050   167 DTPIIRGSAL---KALEGDPDPEWEK-----------KILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTG 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1802442779 153 RVETGIIKAG---MVVNFAPSnVTTEVKSVEMHHEQLEQGNPGDNVG 196
Cdd:COG0050   233 RVERGIIKVGdevEIVGIRDT-QKTVVTGVEMFRKLLDEGEAGDNVG 278
tufA CHL00071
elongation factor Tu
 1-196 1.02e-24

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 99.65  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDttKWSEDRFNEIIK-ETSIFIKKVGYNPKAVAFVP 79
Cdd:CHL00071  102 AILVVSAADGPMP-------QTKEHILLAKQVGVPNIVVFLNKED--QVDDEELLELVElEVRELLSKYDFPGDDIPIVS 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  80 ISGWHGDNMLEESPNmpwykgWTKETKAGVVKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGI 158
Cdd:CHL00071  173 GSALLALEALTENPK------IKRGENKWVDKIYNLMDAVDSyIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGT 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1802442779 159 IKAGMVVN---FAPSNVTTeVKSVEMHHEQLEQGNPGDNVG 196
Cdd:CHL00071  247 VKVGDTVEivgLRETKTTT-VTGLEMFQKTLDEGLAGDNVG 286
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-196 5.79e-24

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 97.57  E-value: 5.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGtgefeagiskDG---QTREHALLAFTLGVRQLIVAVNKMDTtkwSEDRfnEIIK----ETSIFIKKVGYNPK 73
Cdd:PRK00049  102 AILVVSAA----------DGpmpQTREHILLARQVGVPYIVVFLNKCDM---VDDE--ELLElvemEVRELLSKYDFPGD 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  74 AVAFVPISGWHGdnmLEESPNMPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVG 152
Cdd:PRK00049  167 DTPIIRGSALKA---LEGDDDEEWEK-----------KILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTG 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1802442779 153 RVETGIIKAG---MVVNFAPSNVTTeVKSVEMHHEQLEQGNPGDNVG 196
Cdd:PRK00049  233 RVERGIIKVGeevEIVGIRDTQKTT-VTGVEMFRKLLDEGQAGDNVG 278
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-196 1.55e-23

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 96.17  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIK-ETSIFIKKVGYNPKAVA 76
Cdd:PRK12736  102 AILVVA----------ATDGpmpQTREHILLARQVGVPYLVVFLNKVDLV--DDEELLELVEmEVRELLSEYDFPGDDIP 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  77 FVPISGWHGdnmLEESPnmPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 155
Cdd:PRK12736  170 VIRGSALKA---LEGDP--KWED-----------AIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVE 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1802442779 156 TGIIKAG---MVVNFAPSnVTTEVKSVEMHHEQLEQGNPGDNVG 196
Cdd:PRK12736  234 RGTVKVGdevEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVG 276
PLN03127 PLN03127
Elongation factor Tu; Provisional
 8-196 1.78e-22

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 93.74  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   8 GTGEFEAGI----SKDG---QTREHALLAFTLGVRQLIVAVNKMDTTKWSE--DRFNEIIKETSIFIKKVGYNPKAVAFV 78
Cdd:PLN03127  144 GAAQMDGGIlvvsAPDGpmpQTKEHILLARQVGVPSLVVFLNKVDVVDDEEllELVEMELRELLSFYKFPGDEIPIIRGS 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  79 PISGWHGDNmleespnmpwykgwTKETKAGVVKgktLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETG 157
Cdd:PLN03127  224 ALSALQGTN--------------DEIGKNAILK---LMDAVDEYIPePVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQG 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1802442779 158 IIKAG---MVVNFAPS-NVTTEVKSVEMHHEQLEQGNPGDNVG 196
Cdd:PLN03127  287 TIKVGeevEIVGLRPGgPLKTTVTGVEMFKKILDQGQAGDNVG 329
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-196 1.39e-21

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 90.67  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAggtgefeagiSKDG---QTREHALLAFTLGVRQLIVAVNKMDTTKWSEdrFNEIIK-ETSIFIKKVGYNpkava 76
Cdd:PRK12735  102 AILVVS----------AADGpmpQTREHILLARQVGVPYIVVFLNKCDMVDDEE--LLELVEmEVRELLSKYDFP----- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  77 fvpisgwhGDNM----------LEESPNMPWYKgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGG 145
Cdd:PRK12735  165 --------GDDTpiirgsalkaLEGDDDEEWEA-----------KILELMDAVDSyIPEPERAIDKPFLMPIEDVFSISG 225

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1802442779 146 IGTVPVGRVETGIIKAG---MVVNFAPSNVTTeVKSVEMHHEQLEQGNPGDNVG 196
Cdd:PRK12735  226 RGTVVTGRVERGIVKVGdevEIVGIKETQKTT-VTGVEMFRKLLDEGQAGDNVG 278
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-196 2.65e-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: 84.44  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIK-ETSIFIKKVGYNPKAVAFV- 78
Cdd:TIGR00485 102 AILVVSATDGPMP-------QTREHILLARQVGVPYIVVFLNKCDMV--DDEELLELVEmEVRELLSQYDFPGDDTPIIr 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  79 --PISGWHGDNMLEEspnmpwykgwtketkagvvKGKTLLDAIDA-IEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVE 155
Cdd:TIGR00485 173 gsALKALEGDAEWEA-------------------KILELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVE 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1802442779 156 TGIIKAG---MVVNFAPSNVTTeVKSVEMHHEQLEQGNPGDNVG 196
Cdd:TIGR00485 234 RGIIKVGeevEIVGLKDTRKTT-VTGVEMFRKELDEGRAGDNVG 276
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-202 2.73e-19

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 85.05  E-value: 2.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMDTTKwSEDRFNEIIKETSIFIKKVGYNPKAVAFVPI 80
Cdd:PLN03126  171 AILVVSGADGPMP-------QTKEHILLAKQVGVPNMVVFLNKQDQVD-DEELLELVELEVRELLSSYEFPGDDIPIISG 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  81 SGWHGDNMLEESPNMpwykgwTKETKAGVVKGKTLLDAIDAIEP-PVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGII 159
Cdd:PLN03126  243 SALLALEALMENPNI------KRGDNKWVDKIYELMDAVDSYIPiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTV 316

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1802442779 160 KAGMVVNFAPSNVT--TEVKSVEMHHEQLEQGNPGDNVGFNVKNV 202
Cdd:PLN03126  317 KVGETVDIVGLRETrsTTVTGVEMFQKILDEALAGDNVGLLLRGI 361
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-125 5.30e-19

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: 80.26  E-value: 5.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGefeagisKDGQTREHALLAFTLGVRqLIVAVNKMDTTkwSEDRFNEIIKETS-IFIKKVGYNPKAVAFVP 79
Cdd:pfam00009  96 AILVVDAVEG-------VMPQTREHLRLARQLGVP-IIVFINKMDRV--DGAELEEVVEEVSrELLEKYGEDGEFVPVVP 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1802442779  80 ISGWHGDNMleespnmpwykgwtketkagvvkgKTLLDAIDAIEPP 125
Cdd:pfam00009 166 GSALKGEGV------------------------QTLLDALDEYLPS 187
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 133-203 8.58e-17

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


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 71.53  E-value: 8.58e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802442779 133 LRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK 71
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-203 8.11e-16

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: 8.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAggtgefeagiSKDG---QTREH-ALLAFtLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSIFIKkvGYNPKAVA 76
Cdd:COG3276    78 VLLVVA----------ADEGvmpQTREHlAILDL-LGIKRGIVVLTKADLV--DEEWLELVEEEIRELLA--GTFLEDAP 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  77 FVPISGwhgdnmleespnmpwykgwtkETKAGVvkgKTLLDAIDAI--EPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRV 154
Cdd:COG3276   143 IVPVSA---------------------VTGEGI---DELRAALDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTL 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1802442779 155 ETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:COG3276   199 LSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVE 247
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 21-202 1.37e-14

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: 71.44  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDRFNEIIKETSIFIKKVGYNPKAVAFVpISGWHGDNMLEESPNMpwykg 100
Cdd:TIGR00475  90 QTGEHLAVLDLLGIPHTIVVITKADRV--NEEEIKRTEMFMKQILNSYIFLKNAKIFK-TSAKTGQGIGELKKEL----- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779 101 wtketkagvvkgKTLLDAIDAieppvRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVE 180
Cdd:TIGR00475 162 ------------KNLLESLDI-----KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQ 224

                         170       180
                  ....*....|....*....|..
gi 1802442779 181 MHHEQLEQGNPGDNVGFNVKNV 202
Cdd:TIGR00475 225 AQNQDVEIAYAGQRIALNLMDV 246
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 133-203 2.43e-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: 62.54  E-value: 2.43e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802442779 133 LRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVD 71
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 135-203 4.92e-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: 4.92e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802442779 135 LPLQDVYKIGGIGTVPVGRVETGIIKAGM---VVNFAPSNVTTeVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:cd03697     3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDeveIVGFKETLKTT-VTGIEMFRKTLDEAEAGDNVGVLLRGVK 73
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-125 6.83e-12

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: 61.54  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779   1 AILIIAGGTGEfeagiskDGQTREHALLAFtLGVRQLIVAVNKMDTTKwsEDRFNEIIKETSIFIKKVGY---NPKAVAF 77
Cdd:cd00881    89 ALLVVDANEGV-------EPQTREHLNIAL-AGGLPIIVAVNKIDRVG--EEDFDEVLREIKELLKLIGFtflKGKDVPI 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1802442779  78 VPISGWHGDNMLEespnmpwykgwtketkagvvkgktLLDAIDAIEPP 125
Cdd:cd00881   159 IPISALTGEGIEE------------------------LLDAIVEHLPP 182
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 132-195 9.89e-12

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: 58.29  E-value: 9.89e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802442779 132 PLRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNV 195
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNV 64
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 147-202 1.59e-09

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: 52.27  E-value: 1.59e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802442779 147 GTVPVGRVETGIIKAGMVVNFAP-----SNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNV 202
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPngtgkKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGV 61
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 132-202 2.12e-09

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: 52.10  E-value: 2.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802442779 132 PLRLPLQDVYKigGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNV 202
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTGIYIDEEEVDSAKPGENVKLKLKGV 69
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 133-197 1.32e-08

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


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 49.87  E-value: 1.32e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802442779 133 LRLPLQDVYKIGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMHHEQLEQGNPGDNVGF 197
Cdd:cd03695     1 FRFPVQYVNRPNLDFRGYAGTIASGSIRVGDEVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVTL 65
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 139-203 2.50e-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: 44.13  E-value: 2.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802442779 139 DVYKIGGIGTVPVGRVETGIIKAGMVVNFAP----SNVTTEVKSVEMHHEQLEQGNPGDNVGFNVKNVS 203
Cdd:cd03694     7 DIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdadgKFRPVTVKSIHRNRQPVDRARAGQSASFALKKIK 75
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 132-200 2.86e-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: 44.03  E-value: 2.86e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779 132 PLRLPLQDVYKiGGIGTVPVGRVETGIIKAGMVVNFAPSNVTTEVKSVEMH-HEQLEQGNPGDNVGFNVK 200
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNsDEETDWAIAGDTVTLRLR 69
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-45 1.60e-04

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: 41.03  E-value: 1.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1802442779   1 AILIIAGGTGEFEagiskdgQTREHALLAFTLGVRQLIVAVNKMD 45
Cdd:cd01884    92 AILVVSATDGPMP-------QTREHLLLARQVGVPYIVVFLNKAD 129
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 21-196 2.65e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 37.91  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  21 QTREHALLAFTLGVRQLIVAVNKMDTTkwSEDR----FNEiIKEtsiFIKkvGYNPKAVAFVPISGWHGDNMleespnmp 96
Cdd:PRK04000  126 QTKEHLMALDIIGIKNIVIVQNKIDLV--SKERalenYEQ-IKE---FVK--GTVAENAPIIPVSALHKVNI-------- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802442779  97 wykgwtketkagvvkgKTLLDAIDA-IEPPVRPSDKPLRLPLQ---DVYK--------IGGI--GTVPVGRVETG--I-I 159
Cdd:PRK04000  190 ----------------DALIEAIEEeIPTPERDLDKPPRMYVArsfDVNKpgtppeklKGGVigGSLIQGVLKVGdeIeI 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1802442779 160 KAGMVVNFAPSN----VTTEVKSVEMHHEQLEQGNPGDNVG 196
Cdd:PRK04000  254 RPGIKVEEGGKTkwepITTKIVSLRAGGEKVEEARPGGLVG 294
 
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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